Institute for Mathematics and its Applications University of Minnesota 114 Lind Hall 207 Church Street SE Minneapolis, MN 55455 
20082009 Program
See http://www.ima.umn.edu/20082009 for a full description of the 20082009 program on Mathematics and Chemistry.
Annual thematic program on Simulating our complex world: Modeling, computation and analysis approved by IMA Board of Governors for 2010–2011
See http://www.ima.umn.edu/20102011/ for the preliminary program description.
Dr. Juan Meza, department head of the High Performance Computing Research Department at Lawrence Berkeley National Laboratory, was awarded the BlackwellTapia Prize November 14, 2008. The prize is named after David Blackwell and Richard Tapia, two influential figures who inspired a generation of AfricanAmerican, Native American and Latino/Latina students to pursue careers in mathematics. The award recognizes a mathematical scientist who has contributed significantly to research and who has served as a role model for mathematical scientists and students from underrepresented minority groups.
Dr. Meza received the award as a result of his exceptionally distinguished record as a mathematical scientist, an accomplished and effective head of a large department doing cuttingedge explorations in the computational sciences, computational mathematics, and future technologies, and a role model and active advocate for others from groups underrepresented in the mathematical sciences.
Dr. Meza served on the IMA Board of Governors from January 1999 to December 2001. He has also provided scientific leadership to the IMA by organizing workshops, most recently, the September 2008 workshop on Electronic Structures.
For more information on the 2008 BlackwellTapia Conference, go to: http://www.samsi.info.
Margaret Wright, a member of the IMA Board of Governors since 2005, was awarded an honorary PhD degree by the Royal Institute of Technology (KTH) in Stockholm on November 21. A Professor at New York University, Wright has made major contributions to applied mathematics, especially in the fields of optimization and scientific computing. She has also worked to include more women in the mathematical sciences.
The Board of Governors consists of 15 distinguished mathematical scientists from academia, industry, and government laboratories. It provides oversight and direction for all major aspects of the organization.
Wright is a member of the National Academy of Sciences. She completed her doctoral degree in computer science at Stanford University in 1976 and stayed here until 1988. Between 1988 and 2000, she worked at Bell Laboratories and then moved on to the Courant Institute of Mathematical Sciences at New York University in 2001 as Professor and Chair of the Computer Science Department.
10:45am11:15am  Coffee break  Lind Hall 400  
2:30pm3:30pm  Math 8994: Topics in classical and
quantum mechanics Electronic structure calculations and molecular simulation: A mathematical initiation  Eric Cances (CERMICS) Claude Le Bris (CERMICS)  Lind Hall 305 
10:45am11:15am  Coffee break  Lind Hall 400  
11:15am12:15pm  Maximum dissipation principle for numerical methods in complex fluids  Yunkyong Hyon (University of Minnesota)  Lind Hall 305  PS 
3:00pm4:00pm  Reading group for Professor Ridgway Scott's book "Digital Biology"  Ridgway Scott (University of Chicago)  Lind Hall 401 
10:45am11:15am  Coffee break  Lind Hall 400  
1:15pm2:15pm  Stability of traveling waves in quasilinear hyperbolic systems with relaxation and diffusion  Tong Li (University of Iowa)  Lind Hall 305  SMC 
2:30pm3:30pm  Math 8994: Topics in classical and
quantum mechanics Electronic structure calculations and molecular simulation: A mathematical initiation  Eric Cances (CERMICS) Claude Le Bris (CERMICS)  Lind Hall 305 
10:45am11:15am  Coffee break  Lind Hall 400  
11:15am12:15pm  Polynomial extension operators in Sobolev spaces  Jay Gopalakrishnan (University of Florida)  Vincent Hall 570  AMS 
10:45am11:15am  Coffee break  Lind Hall 400 
8:15am8:45am  Registration and coffee  EE/CS 3176  T12.7.08  
8:45am9:00am  Welcome to the IMA  Fadil Santosa (University of Minnesota)  EE/CS 3180  T12.7.08 
9:00am9:40am  Simulations of solvent effects using combined QM/MM methods  Jiali Gao (University of Minnesota)  EE/CS 3180  T12.7.08 
9:40am10:20am  An introduction to quantum mechanical continuum solvation models  Benedetta Mennucci (Università di Pisa)  EE/CS 3180  T12.7.08 
10:20am10:50am  Coffee  EE/CS 3176  T12.7.08  
10:50am11:30am  Ab initio molecular dynamics via the CarParrinello method: Basic ideas, theory, and algorithms  Mark E. Tuckerman (New York University)  EE/CS 3180  T12.7.08 
11:30am12:30pm  Discussion  EE/CS 3180  T12.7.08  
12:30pm2:30pm  Lunch  T12.7.08  
2:30pm3:10pm  Applications of combined QM/MM methods  Jiali Gao (University of Minnesota)  EE/CS 3180  T12.7.08 
3:10pm3:50pm  Applications of quantum mechanical continuum solvation models to the study of molecular properties and spectroscopic features of molecular solutes in different environments  Benedetta Mennucci (Università di Pisa)  EE/CS 3180  T12.7.08 
3:50pm4:20pm  Coffee  EE/CS 3176  T12.7.08  
4:20pm5:00pm  Ab initio pathintegrals and specific applications of the CarParrinello approach to problems of aqueous ion solvation and transport  Mark E. Tuckerman (New York University)  EE/CS 3180  T12.7.08 
5:00pm5:30pm  Discussion  EE/CS 3180  T12.7.08 
All Day  Session (Protein Solvation) Chair: Benedetta Mennucci (Università di Pisa)  W12.812.08  
8:15am9:00am  Registration and coffee  EE/CS 3176  W12.812.08  
9:00am9:20am  Welcome to the IMA  Fadil Santosa (University of Minnesota)  EE/CS 3180  W12.812.08 
9:20am10:00am  Solvation and the energetics of protein folding  Robert L. Baldwin (Stanford University)  EE/CS 3180  W12.812.08 
10:00am10:40am  Intricate role of water molecules in protein dynamics  Donald Hamelberg (Georgia State University)  EE/CS 3180  W12.812.08 
10:40am11:10am  Coffee  EE/CS 3176  W12.812.08  
11:10am11:50am  Solubility profiles of amyloidogenic molecular structures. Theory and experiment  Florin Despa (University of California, Davis)  EE/CS 3180  W12.812.08 
11:50am12:30pm  Probing the prion hydration by Molecular dynamics simulations: from native via misfolded to amyloid conformations  Alfonso De Simone (University of Cambridge)  EE/CS 3180  W12.812.08 
12:30pm2:30pm  Lunch  W12.812.08  
2:30pm3:10pm  Second chances  Ridgway Scott (University of Chicago)  EE/CS 3180  W12.812.08 
3:10pm3:25pm  Group photo  W12.812.08  
3:30pm5:30pm  Poster Session and Reception Poster submissions welcome from all participants  Lind Hall 400  W12.812.08  
Solvation and the energetics of protein folding (poster)  Robert L. Baldwin (Stanford University)  
Competition of steric repulsion and electrostatic attraction determines the selectivity of calcium channels  Dezső Boda (University of Pannonia)  
On the Vibrational effective polarizabilities calculation from continuum solvation models  Roberto Cammi (Università di Parma, email: roberto.cammi@unipr.it)  
Modeling environment effects on electronic energy transfer  Carles Curutchet (University of Toronto) Aurora Muñoz (Università di Pisa)  
An adaptive fast multipole algorithm for electrostatic interactions in biomolecular system  Jingfang Huang (University of North Carolina)  
Optimization of transition pathways using interpolated parameters from swarms of trajectories  Dmitry A. Kondrashov (University of Wisconsin)  
Slip boundary conditions in nanofluidics from the molecular theory of solvation  Andriy Kovalenko (National Institute for Nanotechnology)  
3D molecular theory of solvation in multiscale modeling of chemical nanostructures in solution  Andriy Kovalenko (National Institute for Nanotechnology)  
Novel stochastic methods in biochemical electrostatics  Michael Mascagni (Florida State University)  
Cross sections and photoelectron angular distributions in photodetachment from negative ions using EOMCCSD Dyson orbitals  C. Melania Oana (University of Southern California)  
Macroscopic pattern formation of liquid crystal in kappacarrageenan gel  Isamu Ohnishi (Hiroshima University)  
Optimization of a hybrid implicit/explicit solvation model  Jason A. Wagoner (Stanford University) 
All Day  Session (QM/MM & Cont) Morning Chair: B. Montgomery Pettitt (University of Houston) Afternoon Chair: Jingfang Huang (University of North Carolina)  W12.812.08  
8:30am9:00am  Coffee  EE/CS 3176  W12.812.08  
9:00am9:40am  QM or MM? Development of a nextgeneration force field for chemical and biomolecular simulations  Jiali Gao (University of Minnesota)  EE/CS 3180  W12.812.08 
9:40am10:20am  An overview of the non linearity in Quantum Chemical continuum solvation models  Roberto Cammi (Università di Parma, email: roberto.cammi@unipr.it)  EE/CS 3180  W12.812.08 
10:20am10:50am  Coffee  EE/CS 3176  W12.812.08  
10:50am11:30am  Quantum chemical modelling of molecules at dielectric surfaces and interfaces  Luca Frediani (University of Tromsø)  EE/CS 3180  W12.812.08 
11:30am2:20pm  Lunch  W12.812.08  
2:20pm3:00pm  Biomolecular solvation: from molecular to continuum models  Nathan A. Baker (Washington University School of Medicine)  EE/CS 3180  W12.812.08 
3:00pm3:40pm  Coupling the levelset method with variational implicitsolvent models for molecular solvation  Bo Li (University of California, San Diego)  EE/CS 3180  W12.812.08 
3:40pm4:10pm  Coffee  EE/CS 3176  W12.812.08  
4:10pm5:00pm  Second chances  Mark E. Tuckerman (New York University)  EE/CS 3180  W12.812.08 
All Day  Morning session (SimMD) Chair: Nina Singhal Hinrichs (University of Chicago) Afternoon session: TBA  W12.812.08  
8:30am9:00am  Coffee  EE/CS 3176  W12.812.08  
9:00am9:40am  Hydration from organic molecules to proteinligand complexes  William L. Jorgensen (Yale University)  EE/CS 3180  W12.812.08 
9:40am10:20am  Solvation and hydration at different scales  Bernard R. Brooks (National Institutes of Health)  EE/CS 3180  W12.812.08 
10:20am10:50am  Coffee  EE/CS 3176  W12.812.08  
10:50am11:30am  Calculation of small molecule solvation free energy by molecular dynamics and Monte Carlo simulations.  Yuqing Deng (Zymeworks Inc.)  EE/CS 3180  W12.812.08 
11:30am12:10pm  Classical molecular dynamics simulations of the liquid watergold interface  Stefano Corni (Consiglio Nazionale delle Ricerche (CNR))  EE/CS 3180  W12.812.08 
12:10pm2:20pm  Lunch  W12.812.08  
2:20pm3:00pm  Firstprinciples simulation of electrochemical systems  Eric Cances (CERMICS)  EE/CS 3180  W12.812.08 
3:00pm3:40pm  Fast algorithms for integral equations  Carl Timothy Kelley (North Carolina State University)  EE/CS 3180  W12.812.08 
3:40pm4:10pm  Coffee  EE/CS 3176  W12.812.08  
4:10pm5:00pm  Second chances  Michael J. Holst (University of California, San Diego)  EE/CS 3180  W12.812.08 
All Day  Session (PoissonBoltzmann (PB)) Morning Chair: Robert D. Skeel (Purdue University) Afternoon Chair: Stephen Bond (University of Illinois at UrbanaChampaign)  W12.812.08  
8:30am9:00am  Coffee  EE/CS 3176  W12.812.08  
9:00am9:40am  A fast Nbody solver for the Poisson(Boltzmann) equation  Robert D. Skeel (Purdue University)  EE/CS 3180  W12.812.08 
9:40am10:20am  The membrane potential and its representation in computer simulations  Benoit Roux (University of Chicago)  EE/CS 3180  W12.812.08 
10:20am10:50am  Coffee  EE/CS 3176  W12.812.08  
10:50am11:30am  Selforganized models of selectivity in Ca and Na channels  Robert S. Eisenberg (Rush University Medical Center)  EE/CS 3180  W12.812.08 
11:30am12:10pm  Molecular recognition in life phenomena probed with the statistical mechanics of liquids  Fumio Hirata (National Institutes of Natural Sciences)  EE/CS 3180  W12.812.08 
12:10pm2:20pm  Lunch  W12.812.08  
2:20pm3:00pm  Estimating electrostatic contributions to solvation via boundaryintegral equation theory  Jaydeep P. Bardhan (Argonne National Laboratory)  EE/CS 3180  W12.812.08 
3:00pm3:40pm  TBA  Marcia O. Fenley (Florida State University)  EE/CS 3180  W12.812.08 
3:40pm4:10pm  Coffee  EE/CS 3176  W12.812.08  
4:10pm5:00pm  Second chances  Matthew Gregg Knepley (Argonne National Laboratory)  EE/CS 3180  W12.812.08 
6:30pm8:00pm  Workshop dinner at Pagoda  Pagoda Restaurant 1417 4th St. SE Minneapolis, MN 6123784710 
W12.812.08 
All Day  Session (Statistics) Chair: Carlos J. GarciaCervera (University of California, Santa Barbara)  W12.812.08  
8:30am9:40am  Coffee  EE/CS 3176  W12.812.08  
9:40am10:20am  Classical density functional theory approach to solvation in polar solvents  Daniel Jean Borgis (École Normale Supérieure)  EE/CS 3180  W12.812.08 
10:20am10:50am  Coffee  EE/CS 3176  W12.812.08  
10:50am11:30am  Dimerization of formamide  Modesto Orozco (Institute for Research in Biomedicine (IRB Barcelona))  EE/CS 3180  W12.812.08 
11:30am12:00pm  Second chances  EE/CS 3180  W12.812.08  
12:00pm12:10pm  Closure  EE/CS 3180  W12.812.08 
10:45am11:15am  Coffee break  Lind Hall 400 
10:45am11:15am  Coffee break  Lind Hall 400  
11:15am12:15pm  Time lags in signaling cascades  Srividhya Jeyaraman (University of Minnesota)  Lind Hall 305  PS 
1:00pm3:00pm  IMA Holiday Potluck Luncheon  Lind Hall 400 
10:45am11:15am  Coffee break  Lind Hall 400 
10:45am11:15am  Coffee break  Lind Hall 400  
3:00pm4:00pm  Reading group for Professor Ridgway Scott's book "Digital Biology"  Ridgway Scott (University of Chicago)  Lind Hall 401 
10:15am11:15am  Coffee break  Lind Hall 400 
All Day  Christmas Day. The IMA is closed. 
All Day  Floating holiday. The IMA is closed. 
Event Legend: 

AMS  Applied Mathematics Seminar 
PS  IMA Postdoc Seminar 
SMC  IMA Seminar on Mathematics and Chemistry 
T12.7.08  Theories of solvation within quantum chemistry 
W12.812.08  Solvation 
Second chances  
Abstract: No Abstract  
IMA Holiday Potluck Luncheon  
Abstract: Please join us for the annual IMA Holiday Potluck Luncheon, December 16, 2008 from 1:003:00pm in 400 Lind Hall. We would like you to share a prepared traditional recipe that means something to you (appetizer, salad, entree, dessert, etc.) If your cooking skills are not something you feel should be shared with the rest of us, Lund's/Byerly's, Whole Foods, and Kowalski's are always willing to cover for you. The IMA will provide the beverages. There is a signup sheet located on the 4th floor, at the break treats table. It is going to be a ton of fun! We hope you can join us! IMA Staff  
Nathan A. Baker (Washington University School of Medicine)  Biomolecular solvation: from molecular to continuum models 
Abstract: Continuum electrostatics methods have become increasingly popular due to their ability to provide approximate descriptions of solvation energies and forces without the expensive sampling required by allatom solvent models. In particular, the Poisson–Boltzmann equation (PBE) provides electrostatic potentials, solvation energies, and forces by modeling the solvent as a featureless dielectric material and the mobile ions as a continuous distribution of charge. Polar solvation forces and energies obtained from the PBE are often supplemented with simple solventaccessible surface area (SASA) models of nonpolar solvation. However, while polar and nonpolar continuum models have been assessed on their ability to reproduce global properties, such as solvation free energies, their ability to provide accurate representations of local solvation properties such as forces has not previously been adequately studied. We have developed efficient software for describing polar biomolecular solvation by solving the PoissonBoltzmann equation using multigrid and adaptive finite element methods. Additionally, we have implemented new models to describe nonpolar solvation phenomena. These models have been used to study solvation forces for protein, RNA, and alkane systems. In particular, we have performed comparisons of continuum and allatom representations of solvation forces for these very different molecular systems in order to assess the performance of continuum models in the presence of widely varying charge densities. The results of these comparisons show that current implementations of the PBE are capable of generating polar solvation forces that correlate well with explicit solvent forces for protein systems but provide significantly less accurate representations of polar solvation forces for RNA systems. Conversely, SASAbased nonpolar forces are found to have no significant correlation with nonpolar explicit solvent forces for either protein or RNA molecules. Good correlation between explicit and continuum nonpolar forces is only obtained when area, volume, and attractive dispersion forces are included in the continuum model. We discuss the implications of these studies in the context of molecular simulation as well as the impact of this work on basic models for understanding experimental observations of biomolecular binding and folding.  
Robert L. Baldwin (Stanford University)  Solvation and the energetics of protein folding 
Abstract: Solvation makes major contributions to the energetics of protein folding. In an unfolded protein the free energy of solvating nonpolar side chains is unfavorable while solvating polar peptide groups is favorable. The classical model for the energetics of burying nonpolar side chains through folding is Kauzmann's 1959 proposal to use transfer data for model hydrocarbons from water to an organic solvent. The simple picture is that 50 square angstroms of wateraccessible surface area (ASA) per average side chain is buried via folding and 25 cal mol1 is gained per square angstrom or 1.25 kcal mol1 per residue. Today this model is regarded as seriously oversimplified and side chain burial is modeled by a 2step process. (1) First remove the nonpolar side chain from water, using liquid to gas phase transfer data; (2) pack the folded protein side chains using the LennardJones potential and protein structural coordinates to find the packing energy. A major unsolved problem is the highly approximate proportionality between solvation free energy and ASA. Model compound data give a huge value for the solvation enthalpy of the peptide group (14.2 kcal/mol, Makhatadze & Privalov, 1993), more than 10 times larger than the free energy change per residue for burying nonpolar side chains. Its size shows that more work is badly needed on determining accurate energetics for peptide solvation and forming peptide Hbonds. Recent work shows that the principle of group additivity is not valid for the polar peptide group.  
Robert L. Baldwin (Stanford University)  Solvation and the energetics of protein folding (poster) 
Abstract: Two classes of protein groups in an unfolded protein interact strongly with water and make major contributions to the energetics of folding. Nonpolar side chains interact unfavorably with water and become buried in the protein interior during folding. Polar peptide groups interact favorably and very strongly with water, and as the protein folds the peptide groups become desolvated and form hydrogen bonds (Hbonds) with each other. Two models are used currently to represent desolvation of nonpolar side chains during folding. Kauzmann’s model (1959) treats the protein interior as an organic liquid and uses liquidliquid transfer data to estimate the enerrgetics. The packingdesolvation model (Privalov and Gill, 1988) treats the protein interior as a semicrystalline solid and uses gas to liquid transfer data to estimate desolvation while using the LennardJones potential and the protein structural coordinates to estimate the packing energetics. Solvation energetics of the peptide group are based on calorimetric data for the solvation enthalpy of dipeptide analogs and monoamides together with electrostatic calculations of solvation energetics for longer peptides. These results indicate that, contrary to the longstanding assumption that group additivity is valid, it is in fact entirely invalid for the polar peptide groups. These new results may explain the 2fold discrepancy between the 1995 simulations of folding energetics by Lazaridis, Archontis and Karplus versus the calorimetric results of Makhatadze and Privalov.  
Jaydeep P. Bardhan (Argonne National Laboratory)  Estimating electrostatic contributions to solvation via boundaryintegral equation theory 
Abstract: Implicitsolvent models commonly decompose the molecular solvation free energy into a sum of electrostatic and nonpolar terms, with separate theoretical and numerical procedures employed for each component. In this talk I will describe a new method for estimating the electrostatic free energy of solvation, called BIBEE (boundaryintegralbased electrostatics estimation). The BIBEE method rapidly approximates the solution of the apparentsurfacecharge (ASC) or polarizablecontinuummodel (PCM) integral equation formulation of the mixeddielectric continuum electrostatics problem that is often solved using finiteelement or finitedifference methods. The method draws inspiration from the surfacegeneralized Born model, but avoids the unphysical interpolations inherent to generalizedBorn method. As a result, BIBEE methods more accurately reproduce solventscreened interactions between charges. Furthermore, it is straightforward to show that variants of the BIBEE method can generate rigorous upper and lower bounds for the actual electrostatic free energy of solvation.  
Dezső Boda (University of Pannonia)  Competition of steric repulsion and electrostatic attraction determines the selectivity of calcium channels 
Abstract: Calcium channels conduct Na ions in the absence of Ca, but they selectively conduct Ca ions when Ca ions are present at physiological concentrations. In an experiment when Ca is added to NaCl gradually, even a micromolar amount of Ca ions effectively blocks Na current. In our model of the selectivity filter of Ca channels, the terminal groups of the side chains of amino acids—four glutamatesin the selectivity filter are represented as mobile ions that are restricted so they move inside the filter These structural ions form a liquidlike selfadjusting environment for the passing ions so that the system assumes minimum free energy. They also fill part of the pore so the counterions have to compete for space in the crowded selectivity filter (charge/space competition (CSC) mechanism). In this picture electrostatic attraction and repulsive entropic excluded volume effects compete with each other to determine which ions can enter the selectivity filter. We argue that this competition is crucial in explaining the selectivity mechanism of Ca channels. We show grand canonical Monte Carlo simulation results for competition between ions of different valence and diameter. We couple our Monte Carlo simulations to the integrated NernstPlanck equation to compute current from equilibrium profiles. Our results are in good agreement with experimental data.  
Daniel Jean Borgis (École Normale Supérieure)  Classical density functional theory approach to solvation in polar solvents 
Abstract: We draw a comparison between the quantum density functional theory for electronic structure calculations and the ''classical'' density functional theory of molecular liquids and we show how, borrowing ideas and techniques from electronic DFT, classical DFT can be used as a useful chemist's tool to provide, at a microscopic level, the solvation properties of complex molecules in polar solvents. This includes the determination of absolute solvation freeenergies, as well as threedimensional microscopic solvation structures. The proposed strategy is as follows: we first compute the homogeneousfluid, position and angledependent, direct correlation function, the cfunction. To this end, we carry out extensive MD simulations of the pure solvent, and compute this way the position and angledependent pair distribution function (the hfunction). We invert subsequently the socalled OrnsteinZernike equation to go from the hfunction to the cfunction. This direct correlation can then be used as the definition of the –unknown– excess freeenergy in the expression of the freeenergy functional. In the presence of a given molecular solute, which provides the external potential, this functional can be minimized with respect to the position and angledependent density, using a 3D cartesian grid for positions and a GaussLegendre angular grid for orientations, to obtain, at the minimum, the absolute solvation freeenergy of the solute and the equilibrium solvent density profile around it. The DFT results can be compared to direct MD simulations of the solute/solvent system or experimental data The procedure is shown to be efficient and accurate for polar solvents such as acetonitrile. [1] Rosa Ramirez, Ralph Gebauer, Michel Mareschal, and Daniel Borgis, Phys. Rev. E, 66, 031206 (2002). [2] Rosa Ramirez and Daniel Borgis, J. Phys. Chem B 109, 6754 (2005). [3] Rosa Ramirez, Michel Mareschal, and Daniel Borgis, Chem. Phys. 319, 261 (2005). [4] Lionel Gendre, PhD Thesis, Université d'Evry, July 2008. Manuscript in preparation.  
Bernard R. Brooks (National Institutes of Health)  Solvation and hydration at different scales 
Abstract: No Abstract  
Roberto Cammi (Università di Parma, email: roberto.cammi@unipr.it)  An overview of the non linearity in Quantum Chemical continuum solvation models 
Abstract: Quantum chemistry computational tools coupled with a continuum description of the solvent offer an effective approach to study molecular properties and processes in condensed phase due to modest increase of the computational effort with respect a QM calculation of isolated molecules [1]. However, this coupling is by no meas free of problems. The QM continuum models are characterized by the use of a nonlinear Hamiltonian, being the solute Hamiltonian term representing by the solutesolvent interaction dependent on the wavefunction of the solute it selves. As a consequence all the conventional Quantum Chemical models to be able to describe in a coherent way the effects of the solutesolvent interaction have to be reconsidered from their basic principles and suitably modified to take into account of this non linearity. The neglecting of this effects may lead to a systematic errors in the numerical outcome of the QM solvation models. In this talk we will give an overview of the systematic work done within the Polarizable Continuum Model group to introduce the nonlinearity effects into the Quantum Chemical methods. The emphasis will be given on the basic principles and problems involved. In particular we will focus on the definition of a new basic energetic functional [2] , different, from that used for isolated molecules, which has to be taken as a starting point to develop QM methods for continuum solvation models. A wide sample of QMsolvation methods will be also discussed, ranging from the abinitio time independent methods (HartreeFock, MCSCF, Moeller Plesset) to the corresponding timedependent response function formalisms, and from the the Density Functional Theory to the Time dependent DFT approach to the excited states of solvated chromophores. Final remarks will regards some still open issues in the coupling of QM methods with continuum solvation models. [1] Tomasi J., B. Mennucci, Cammi, R. "Quantum Mechanical Continuum Solvations Models", Chem. Rev., 2005, 105, 2999. [2] Cammi, R., Tomasi, J. J. Comp. Chem. 16, 1449, 1994  
Roberto Cammi (Università di Parma, email: roberto.cammi@unipr.it)  On the Vibrational effective polarizabilities calculation from continuum solvation models 
Abstract: The increasing efforts devoted to study linear and non linear optical properties (NLO) of solvated molecules have followed the success of modern quantum mechanical (QM) methods in the forecast of the NLO properties of isolated systems. The approaches adopted uses the same QM methodology developed for the isolated systems with the additional introduction of the features due to the solutesolvent interactions. However, even when all the solvent effects are included in the solvation model the computed NLO quantities are still microscopic in nature and cannot be directly compared with their macroscopic manifestation, i.e. the macroscopic scusceptibility.
In recent years we have introduced an effective framework to treat local field effects in linear and nonlinear NLO properties in solution within the quantum mechanical Polarizable Continuum Model [1,2]. In this framework effective polarizabilities are defined to include the effect due to the difference between the local field acting on the solute molecules and the macroscopic field in the medium (Maxwell field).
In this poster we will focus on the vibrational components of the effective polarizabilities within the quantum mechanical Polarizable Continuum Model framework. In particular, we will give a detailed overview of the method for the calculation of the vibrational effective polarizabilities in the double harmonic approximation [3] . As will be show, the double harmonic procedure can be reformulated within the PCM so as to obtain the effective vibrational polarizabilities in terms of the derivatives with respect to normal coordinates of effective electronic molecular properties [4]. We will also discuss the connection between the PCM formulation of the vibrational effective polarizabilities and the parallel approach given within the framework of semiclassical OnsagerWortmannBishop method [5].
[1] R. Cammi, B. Mennucci, and J. Tomasi, J. Phys. Chem. A, 102(1998)870.
[2] R. Cammi, B. Mennucci, and J. Tomasi, J. Phys. Chem. A, 104(2000)4690. [3] J. Tomasi, B. Mennucci and R. Cammi, Chem. Rev., 105(2005)2999. [4] R. Cammi, B. Mennucci, and J. Tomasi, in M.G. Papadopulos (ed.), Nonlinear Optical Response of Molecules Solids and Liquids: Methods and Applications, Research Signpost, Kerala, India, 2003, p.113. [5] R. Wortmann and D. Bishop, J. Chem. Phys., 108(1998)1001. 

Eric Cances (CERMICS), Claude Le Bris (CERMICS)  Math 8994: Topics in classical and
quantum mechanics Electronic structure calculations and molecular simulation: A mathematical initiation 
Abstract: Meeting time: Mondays and Wednesdays 2:30 ‐ 3:30 pm Room 305 Lind Hall. The course will present the basics of the quantum theory commonly used in computational chemistry for electronic structure calculations, and the basics of molecular dynamics simulations. The perspective is definitely mathematical. After the presentation of the models, the mathematical properties will be examined. The state of the art of the mathematical knowledge will be mentioned. Numerical analysis and scientific computing questions will also be thoroughly investigated. The course is intended for students and researchers with a solid mathematical background in mathematical analysis and numerical analysis. Familiarity with the models in molecular simulation in the broad sense is not needed. The purpose of the course to introduce the audience to the field. This is a 1‐3 credit course offered through the School of Mathematics. Non‐student participants are welcome to audit without registering. Note that no particular knowledge of quantum mechanics or classical mechanics will be necessary: the basic elements will be presented. For additional information and course registration, please contact: Markus Keel (keel@math.umn.edu).  
Eric Cances (CERMICS)  Firstprinciples simulation of electrochemical systems 
Abstract: Understanding the electrical response of electrochemical convertors, such as fuel cells or batteries, involves elucidating the effect of the macroscopic voltage on the microscopic charge distribution at the electrodeelectrolyte interface. I will present a quantum/classical model which couples a quantum molecular description of the electrodeelectrolyte interface with a polarizablecontinuum representation of the longrange effects of the ionic solvent. I will mainly focus on the mathematical and numerical aspects. In the last part of my talk, I will present numerical calculations of the vibrational Stark effect for chemisorbed CO, which demonstrate the efficiency of this approach. This is a joint work with I. Dabo, Y. Li and N. Marzari.  
Stefano Corni (Consiglio Nazionale delle Ricerche (CNR))  Classical molecular dynamics simulations of the liquid watergold interface 
Abstract: Several phenomena take place at the interface between liquid water and the gold (111) surface. For example, it is a widespread system for controlled electrochemical investigations, for the study of molecular conduction and of the interaction between proteins and the solid surfaces in water. Despite this great and interdisciplinary importance, the wettability properties of the gold surface are microscopically not well understood. For example, the contact angle between water and clean gold is zero, thus the gold surface is considered hydrophilic [1]. On the other hand, computational DFT studies on single molecules (or model monolayers) on the gold surface pointed out that the goldwater interaction is very small [2]. The term hydrophobic is often used in this context to classify Au(111).
To shed light on the microscopic structure of the waterAu(111) interface, we performed classical molecular dynamics simulations of water on a gold (111) surface. These simulations are based on a force field for goldwater and goldprotein interactions that we have recently developed [3]. It is based on available experimental results and quantum mechanical (DFT and MP2) calculations. Gold polarization effects are also taken into account.
In this talk I will discuss the developed force field and the results of our simulations for a neutral gold surface, with particular emphasis on the microscopic nature of the watergold interface
[1] K.W. Bewing, and W. A. Zisman, J. Phys. Chem 69, 4238 (1965).
[2] A. Michaelides et al., Phys. Rev. Lett. 90, 216102 (2003). [3] F. Iori, and S. Corni J. Comp. Chem. 29, 1656 (2008); F. Iori et al. J. Comp. Chem. in press. 

Carles Curutchet (University of Toronto), Aurora Muñoz (Università di Pisa)  Modeling environment effects on electronic energy transfer 
Abstract: Understanding solvent effects, which cause line broadening and screen electronic interactions, is fundamentally important because of its central role in the control of EET dynamics. Recent work has furthermore shown that simple models for solvation may not be sufficient to explain effects that go beyond Förster theory, such as coherent contribution to energy transfer.[1] Here results obtained from novel quantummechanical methodologies will be reported as a starting point for an atomistic description of the interplay between solvation and electronic energy transfer. First, we will present results obtained with a quantummechanical method that accounts for the actual shape of the molecules inside the dielectric environment through the Polarizable Continuum Model (PCM), thus overcoming the pointdipole assumption of Förster theory. This model predicts an exponential distancedependent attenuation of the solvent screening in chromophore pairs taken from light harvesting antenna proteins,[2] thus indicating a substantial underestimation of EET rates by Förster theory at separations less than about 20 Å. As a further step towards a realistic model of solvation in EET, we will present a combined quantum mechanics/molecular mechanics (QM/MM) method that adopts an atomistic description of the solvent, thus going beyond the continuum dielectric approximation.
[1] (a) Jang, S.; Newton, M. D.; Silbey, R. J. Phys. Rev. Lett. 2004, 92, 218301. (b) Engel, G. S.; Calhoun, T. R.; Read, E. L.; Ahn, T.K.; Mancal, T.; Cheng, Y.C.; Blankenship, R. E.; Fleming, G. R. Nature 2007, 446, 782.
[2] (a) Scholes, G. D.; Curutchet, C.; Mennucci, B.; Cammi, R.; Tomasi, J. J. Phys. Chem. B 2007, 111, 6978. (b) Curutchet, C.; Scholes, G. D.; Mennucci, B.; Cammi, R. J. Phys. Chem. B 2007, 111, 13253. 

Alfonso De Simone (University of Cambridge)  Probing the prion hydration by Molecular dynamics simulations: from native via misfolded to amyloid conformations 
Abstract: Water at the surface of proteins plays a crucial biological
role. The study of hydration is therefore fundamental for
achieving a complete description of key factors determining the
protein biology. In this framework, Molecular Dynamics
simulations have provided precious tools for elucidating the
structure and dynamics of waters in the protein hydration
shell. We employed Molecular Dynamics to address on the
hydration properties of the Prion Protein, whose misfolding and
aggregation is associated to Transmissible Spongiform
Encephalopathies. The investigations focused on different
states along a likely aggregation pathway specifically
analyzing native state, misfolded state and amyloidlike state.
The presentation will discuss on the influence that water
exerts on protein structural stability [1, 2], intermolecular
interactions [3], misfolding [4] and selfassembly [5, 6].
References 1. PNAS (2005) 102:75357540. 2. FEBS Letters (2006) 580:24882494. 3. Biophysical Journal (2006) 90:305261. 4. Biophysical Journal (2007) 93:12841292. 5. Proteins (2008) 70:863872. 6. BBRC (2008) 366:800806. 

Yuqing Deng (Zymeworks Inc.)  Calculation of small molecule solvation free energy by molecular dynamics and Monte Carlo simulations. 
Abstract: Solvation free energy determines the thermostability of molecules in solution. Accurate prediction of solvation free energy from atomistic simulations have great impact on the understanding of many biologically important processes. What makes the simulation of the solvation free energy difficult is that it consists of competing effects from opposing interactions at a molecular level. To accelerate convergence, separations of the competing forces are necessary. Traditionally formulation of solvation free energy separates van der Waals and electrostatics. We find that further separation of the attractive and repulsive forces within the van der Waals interactions is also necessary. Test calculations with constant pressure molecular dynamics (MD) in water show that the seemingly small nonpolar solvation free energy is made up of relatively large unfavorable contribution from repulsive forces and a canceling favorable contribution from the attractive forces. Our results show good agreement with experimental solvation free energies and those of other computational studies. Alternative to the constant pressure simulation with a fluctuating volume, the same results can be generated with fixed volume but fluctuating number of water molecules  grand canonical ensemble. With the grand canonical Monte Carlo (GCMC) moves on solvent water, we are able to obtain accurate solvation free energy as well. The GCMC/MD method is shown to yielded accurate results for ligand binding in cytochrome p450, in which case water displacement from a confined binding pocket can not be account for in typical MD simulation time.  
Florin Despa (University of California, Davis)  Solubility profiles of amyloidogenic molecular structures. Theory and experiment 
Abstract: Hydration shells of normal proteins display both structured and bulk like waters. Isomers with considerable bulklike hydration tend to aggregate. In my talk, I will present both theoretical and experimental data showing that different morphological states of aggregated isomers differ by hydration distribution profiles and water magnetic resonance (MR) signals. The results help explain the MR contrast patterns of amyloids, a subject of long controversy, and suggest a new approach for identifying unusual protein aggregation related to disease. As an example, I will present MRI data and cell toxicity measurements revealing the relationship between the structural conformations of several amyloidogenic peptides and the mechanisms of cellular dysfunction.  
Robert S. Eisenberg (Rush University Medical Center)  Selforganized models of selectivity in Ca and Na channels 
Abstract: Selectivity is one of the most important properties of living systems. One of the founders of molecular biology (Nobel Laureate Aaron Klug) recently said (with some hyperbole I suspect) "There is only one word that matters in biology and that is specificity." My collaborators and I study selectivity in ion channels. Ion channels are proteins with a hole down their middle that are the (nano nearly pico)valves of life. Ion channels control an enormous range of biological function in health and disease. A large amount of data is available about selectivity in many channels. Selectivity in ion channels occurs without structural change of the channel protein (on the biological time scale of 105 sec or longer) and does not involve changes in covalent bonds (i.e., changes in shape of electron orbitals). Selectivity in channels involves only electrodiffusion—usually of charged hard spheres. Thus, physical analysis of selectivity in ion channels is easier than analysis of specificity in enzymes or many other proteins while being at least as important biologically. A simple pillbox model with two adjustable parameters accounts for the selectivity of both DEEA Ca channels (Aspartate Glutamate Glutamate Alanine) and DEKA Na channels (Aspartate Glutamate Lysine Alanine) in many ionic solutions of different composition and concentration. The predicted properties of the Na and Ca channels are very different even though 'Pauling' crystal radii are used for ions and all parameters are the same for both channels in all solutions. Only the side chains are different in the model of the Ca and Na channels. No information from crystal structures is used in the model. Side chains of the channel protein are grossly approximated as spheres. How can such a simple model give such powerful results when chemical intuition says that selectivity depends on the precise relation of ions and side chains? We use Monte Carlo simulations of this model that determine the most stablelowest free energystructure of the ions and side chains. Structure is the computed consequence of the forces in this model and so is different in different conditions. The relationship of ions and side chains vary with ionic solution and are very different in simulations of the Na and Ca channels. Selectivity is a consequence of the 'induced fit' of side chains to ions and depends on the flexibility (entropy) of the side chains as well as their location. The induced fit depends on the concentrations of ions in the surrounding solutions in a complex way. Thus, calculations in a single set of conditions are of limited use. In particular, calculations of 'free energy of binding' in infinitely dilute or ideal solutions are not likely to give useful estimates of binding in physiological solutions. Physiological solutions are typically ~ 200 mM, far from dilute. The selforganized inducedfit model captures the relation of side chains and ions well enough to account for selectivity of both Na channels and Ca channels in the wide range of conditions measured in experiments, even though the components of the model are grossly oversimplified. Perhaps the simplified model works because the structures in both the model and the real channel are the most stable, selforganized, and at their free energy minimum, different in different conditions. It seems that an important biological function can be understood by an oversimplified model if the model calculates the 'most stable' structure as it changes from solution to solution, and mutation to mutation.  
Luca Frediani (University of Tromsø)  Quantum chemical modelling of molecules at dielectric surfaces and interfaces 
Abstract: The study of chromophores located at surfaces and interfaces is important both in material science and in biological chemistry: coated materials, sensors, nanoparticles, cell membranes, micelles are systems where the interface is not a mere boundary between different bulk regions but the central part of the investigated system. Chromophores are often employed to probe and investigate the surface by making use of surfacespecific techniques as second harmonic generation (SHG) and sumfrequency generation (SFG). It is therefore important to develop the theoretical tools necessary to model chromophores in such a peculiar environment in order to interpret and understand the spectroscopic findings. Continuum solvation models have in recent years been extended to surfaces and interfaces. A brief account of the challenges faced and the theoretical developments needed to achieve the goal will here be given. Recent results making use of the developed theoretical models will also be presented.  
Jiali Gao (University of Minnesota)  QM or MM? Development of a nextgeneration force field for chemical and biomolecular simulations 
Abstract: Traditionally, molecular dynamics and Monte Carlo simulations of condensed phase systems including biopolymers are carried out using molecular mechanics or force fields that describe intermolecular interactions. In fact, the formalism of these force fields for biomolecular simulatiosn was established in the 1960s. Although the computational accuracy has increased enormously through parameterization, little has changed in the functional terms used in the force fields. In this talk, I will describe an explicit polarization (XPol) method based on quantum mechanics for developing force fields in condensed phase simulations. The theory, algorithm and application of this approach will be illustrated and its feasibility is demonstrated.  
Jiali Gao (University of Minnesota)  Simulations of solvent effects using combined QM/MM methods 
Abstract: There are two main advantages of using a combined quantum mechanical and molecular mechanical (QM/MM) potential in molecular dynamics and Monte Carlo simulations. First, since only a small portion of the condensed phase system is treated by an explicit electronic structure method, combined QM/MM methods can be applied to large molecular systems along with extensive configurational sampling. Secondly, the accuracy of the QM model representing the solute molecule can be systematically improved by using larger basis sets and by including better treatment of electron correlation. Parallel to the QM treatment, the quality of the MM approximation for the solvent system can also be improved by including polarization terms to account for the mutual solute (QM) and solvent (MM) charge polarization. In this talk, I will summarize early studies and highlight some recent developments including the use of mixed molecular orbital and valence bond (MOVB) models and the incorporation of solvent polarization in combined QM/MM simulations.  
Jiali Gao (University of Minnesota)  Applications of combined QM/MM methods 
Abstract: In this tutorial, I will present a few specific applications in which the need for an explicit treatment of the electronic structure of the solute is particularly important and cannot be conveniently circumvented by developing a problemspecific force field. The examples include the computation of the pKa of organic acid in the electronically excited state, the solvatochormic shifts of an organic chromophore from steam vapor to ambient water, the vibrational energy relaxation of a ligand in the enzyme active site, and the kinetic isotope effects in a proton transfer reaction in water using Feynman path integrals.  
Donald Hamelberg (Georgia State University)  Intricate role of water molecules in protein dynamics 
Abstract: Water molecules are ubiquitous in living organisms and have therefore been viewed more as an environment for biomolecules rather than as a collection of interacting molecules. Water molecules make up an integral part of protein structures, while assisting in catalysis, providing stability and controlling the plasticity of binding sites. In order to realistically mimic the environment of biomolecules, molecular dynamics simulations are routinely done in explicit water. Unfortunately, most of the computational resources go into computing the interactions between these water molecules. Therefore, many implicit solvation models pursued over the years have only viewed the presence of water as a continuum dielectric. However, critical questions do arise about the inherent faster dynamics that are usually obtained with implicit solvation models. We show that explicit water does not only slow down protein dynamics by increasing the frictional drag, but also by increasing the local energetic roughness of the energy landscape by as much as 1.0 kcal/mol, an effect which is lacking in typical implicit solvation models. The possible implications of this effect in catalysis will also be discussed.  
Fumio Hirata (National Institutes of Natural Sciences)  Molecular recognition in life phenomena probed with the statistical mechanics of liquids 
Abstract: Few years ago, we have succeeded to “probe” water molecules bound in a cavity of a protein by means of the statistical mechanics of molecular liquids, or the RISM/3DRISM theory. This is the first finding in the history of the statistical mechanics to show that the theory is applicable to such fluids in an extremely inhomogeneous field in atomic scale. On the other hand, the finding implies that we got a powerful machinery in our hand to clarify the “molecular recognition” which is the most fundamental process in living cells. It will become a “bridgehead” in our theoretical challenge on life phenomena. In the succeeding applications of the method, we have focused on a variety of molecular processes in biosystems, in which the molecular recognition plays an essential role: the selective ionbinding by protein, an enzymatic reaction, water channels (aquaporin), the preferential binding of inert gas by protein, and the pressure denaturation of protein. In the talk, I will present our recent studies on the chemical processes concerned with the molecular recognition, focusing especially on the possibility of ion permeation through aquaporins. The talk will include also prospects of the theory to be extended to the temporal fluctuation of protein structure coupled with the solvent dynamics.  
Michael J. Holst (University of California, San Diego)  Second chances 
Abstract: No Abstract  
Jingfang Huang (University of North Carolina)  An adaptive fast multipole algorithm for electrostatic interactions in biomolecular system 
Abstract: PoissonBoltzmann (PB) electrostatics is a well established model in biophysics, however its application to the study of large scale biosystem dynamics such as the proteinprotein encounter is still limited by the efficiency and memory constraints of existing numerical techniques. In this poster, we present an efficient and accurate scheme which incorporates recently developed novel numerical techniques to further enhance the present computational ability. In particular, a boundary integral equation approach is applied to discretize the linearized PoissonBoltzmann (LPB) equation; the resulting integral formulas are well conditioned and are extended to systems with arbitrary number of biomolecules; the solution process is accelerated by the Krylov subspace methods and an adaptive new version of fast multipole method (FMM); and in addition to the full electrostatic interaction energy, the forces and torques are computed in the postprocessing procedure using interpolation. The Adaptive Fast Multipole PoissonBoltzmann (AFMPB) solver will be released under open source license agreement.  
Yunkyong Hyon (University of Minnesota)  Maximum dissipation principle for numerical methods in complex fluids 
Abstract: We discuss the general energetic variational approaches for hydrodynamic systems of complex fluids. In these energetic variational approaches, the least action principle (LAP) with action functional gives the Hamiltonian parts (conservative force) of the hydrodynamic systems, and the maximum/minimum dissipation principle (MDP), i.e., Onsager's principle, gives the dissipative parts (dissipative force) of the systems. When we combine the two systems derived from the two different principles, we obtain a whole coupled nonlinear system of equations satisfying the dissipative energy laws. We will discuss the important roles of MDP in designing numerical method for computations of hydrodynamic system in complex fluids. We will reformulate the dissipation in energy equation in terms of a rate in time by using an appropriate evolution equations, then the MDP is employed in the reformulated dissipation to obtain the dissipative force for the hydrodynamic system. The systems are consistent with the Hamiltonian parts which are derived from LAP. This procedure allows the usage of lower order element (a continuous $C^0$ finite element) in numerical method to solve the system rather than high order elements, and at the same time preserves the dissipative energy law.  
Srividhya Jeyaraman (University of Minnesota)  Time lags in signaling cascades 
Abstract: Biochemical Signaling cascades are the primary source of information transfer in cellular mechanisms. Cell signaling is predominantly achieved by PhosphorylationDephosphorylation (PD) reactions knit in a cascade like fashion. These cascades respond to a stimulus and conduct the information that regulates several key events within the cell. Mathematical models of these cascades predict a phenomenon called "Zeroorder Ultrasensitivity" which corresponds to an unusually increased sensitivity to conduct the signals across the cascades. This has been confirmed experimentally. However, experiments have also observed a certain time lag in the response of these cascades. In this talk I will discuss the effect of time lag in some of the mathematical models to see what effect they may bring in. A small amount of time lag brings in the capability of sustained signal transduction even when the stimulus strength is very weak. This suggests that PD cascades coupled with time lags may be one of the fundamental mechanisms of signal transduction in cellular processes under weak stimuluses.  
William L. Jorgensen (Yale University)  Hydration from organic molecules to proteinligand complexes 
Abstract: No Abstract  
Carl Timothy Kelley (North Carolina State University)  Fast algorithms for integral equations 
Abstract: We will discuss a class of fast algorithms for linear and nonlinear integral equations. These are twolevel algorithms based on the classic AtkinsonBrakhage method from the 1970s. We will present more efficient approach which uses a matrixfree NewtonKrylov iteration on the coarse mesh and does the finetocoarse intergrid transfer with an average. We will then apply the approach to the OrnsteinZernike (OZ) equations for atomic fluids and some extensions of the OZ equations for molecular fluids.  
Dmitry A. Kondrashov (University of Wisconsin)  Optimization of transition pathways using interpolated parameters from swarms of trajectories 
Abstract: Joint work with A.C. Pan and B. Roux. Understanding the mechanism of conformational changes in macromolecules requires the knowledge of the intermediate states. A version of the string method, which uses multiple short dynamics trajectories to propagate the pathway, was recently developed by Pan et al. We use data from swarms of trajectories calculated at discrete points in phase space to interpolate the average displacement and variance of the system at arbitrary points. This is tested on model potentials using statistics from actual swarms of trajectories. We use the interpolated parameters to compute the Markovian propagators from one point on the transition path to the next. We use them to obtain a timedependent action of a path, which can be optimized to produce the highest probability pathway. We describe the optimization protocol and demonstrate that in artificial flat potentials the existing string method cannot correct problems such as loops in the initial path, while the new method produces the correct pathway. The method will be tested by applying it to protein conformational transitions, such as the KcsA potassium channel, and comparing its performance to existing transition pathway methods.  
Andriy Kovalenko (National Institute for Nanotechnology)  Slip boundary conditions in nanofluidics from the molecular theory of solvation 
Abstract: Joint work with Alexander E. Kobryn (National Institute for Nanotechnology, National Research Council of Canada). Motivated by the fundamental questions raised by the most recent experimental achievements in nanofluidics, we propose the firstever derivation and calculation of the hydrodynamic slip length from the first principles of statistical mechanics, based on a combination of linear response theory and equilibrium molecular theory of solvation. The slip length obtained is independent of the type of flow and is related to the fluid organization near the solid surface, as governed by the solidliquid interaction. In the wide range of shear rates and surfaceliquid interactions, the slip length is expressed in terms of the GreenKuboNakano relations as a function of the anisotropic inhomogeneous time correlation function of density fluctuations of the liquid in contact with the surface. The time dependence of the correlation function is factored out by treating it in the hydrodynamic limit. And the spatially inhomogeneous twobody correlation function is represented in the Kirkwoodlike approximation as a product of the threedimensional density distributions of interaction sites of the liquid near the surface and the sitesite pair correlations of the bulk liquid. The presented treatment generalizes the phenomenological definition of the friction coefficient (as well as the slip length) to a tensor quantity, which reflects an anisotropic nature of an ordered crystalline surface. This enables theoretical prediction of friction forces acting aslant to the liquid flow direction for such surfaces. We derive generic analytical expressions for the liquidsurface friction coefficient (and slip length) for an arbitrary surfaceliquid interaction potential. We further illustrate it by numerical calculations for the case of a laminar flow of acetonitrile, benzene, ethanol, ethanolamine, dimethylsulfoxide, glycerol, methanol, tertbutyl alcohol, and water, at ambient conditions in contact with the (100) FCC surface of gold, copper and nickel modeled by using allatom or unitedatom models for liquids and the Steele potential for crystalline surfaces. The obtained values for slip length range from few to hundreds of nanometers and are consistent with experimental measurements. We complement calculations by obtaining pressure and temperature dependence of the slip length for water in wide range of these thermodynamic parameters.  
Andriy Kovalenko (National Institute for Nanotechnology)  3D molecular theory of solvation in multiscale modeling of chemical nanostructures in solution 
Abstract: A salient feature of nanoscale objects and phenomena is that they are very different from the atomic constituents as well as from those described by the conventional, macroscopic laws of continuous media. The behavior of nanostructures can be changed in a wide range, which constitutes the promise of nanoscience on control over properties of materials. Examples are selfassembly of synthetic organic supramolecular nanoarchitectures in solution, nanocatalysis, and electrochemistry in disordered nanoporous electrodes. Modeling of nanosystems should operate at length scale from one to hundreds nanometers and time scale up to microseconds and more, and yet derive their properties from the chemical functionalities of the constituents. Explicit molecular modeling of such nanosystems involves longtime description of millions of molecules which is by far not feasible with ab initio methods, very problematic for molecular simulations, and thus requires multiplescale approaches. Statisticalmechanical, molecular theory of solvation, a.k.a. threedimensional reference interaction site model (3DRISM), predicts from the first principles the molecular structure and thermodynamics of nanosystems, with proper account of their chemical functionalities [1]. The theory operates with 3D distributions of species averaged over the statistical ensemble rather than with trajectories of individual molecules, and yields the thermodynamics and volumetrics of solvation analytically. It represents both longrange electrostatic and shortrange steric features of the solvation structure of chemical specificities, such as hydrogen bonding, hydrophobicity, and electrochemical effects. The 3DRISM theory can be regarded as a molecular extension to the PoissonBoltzmann solvation electrostatics. This presentation describes the 3DRISM methodology for the solvation structure and thermodynamics, and its selfconsistent combination with ab initio quantum chemical methods in multiscale theory of electronic structure in solution. The methodology is illustrated with applications to solvation of different molecules and chemical reactions in solution [2], selfassembly and conformational stability of synthetic organic supramolecular nanoarchitectures [3], and supercapacitor and electrosorption cell devices with nanoporous carbon electrodes [4]. References [1] A. Kovalenko, Threedimensional RISM theory for molecular liquids and solidliquid interfaces, in: Molecular Theory of Solvation, F. Hirata (Ed.) Series: Understanding Chemical Reactivity, P. G. Mezey (Ed.), vol.24, (Kluwer Academic Publishers, Dordrecht, 2003, 360 p.) pp.169275. [2] S. Gusarov, T. Ziegler, A. Kovalenko, SelfConsistent Combination of the ThreeDimensional RISM Theory of Molecular Solvation with Analytical Gradients and the Amsterdam Density Functional Package, J. Phys. Chem. A, 110, 6083 (2006); D. Casanova, S. Gusarov, A. Kovalenko, T. Ziegler, Evaluation of the SCF Combination of KSDFT and 3DRISMKH; Solvation Effect on Conformational Equilibria, Tautomerization Energies, and Activation Barriers, J. Chem. Theory Comput., 3, 458 (2007). [3] R.S. Johnson, T. Yamazaki, A. Kovalenko, H. Fenniri, Molecular Basis for WaterPromoted Supramolecular Chirality Inversion in Helical Rosette Nanotubes, J. Am. Chem. Soc., 129, 5735 (2007); J.G. Moralez, J. Raez, T. Yamazaki, R.K. Motkuri, A. Kovalenko, H.Fenniri, Helical Rosette Nanotubes with Tunable Stability and Hierarchy, J. Am. Chem. Soc. Communications, 127, 8307 (2005). [4] A. Kovalenko, Molecular description of electrosorption in a nanoporous carbon electrode, J. Comput. Theor. Nanosci., 1, 398 (2004); A. Tanimura, A. Kovalenko, F. Hirata, A molecular theory of a double layer formed by aqueous electrolyte solution sorbed in a carbonized polyvinylidene chloride nanoporous electrode, Chem. Phys. Lett., 378, 638 (2003).  
Bo Li (University of California, San Diego)  Coupling the levelset method with variational implicitsolvent models for molecular solvation 
Abstract: Recent studies have questioned the consistency and applicability of the existing implicitsolvent models in which solvent accessible surfaces (SAS) or solvent excluded surfaces (SES) are predefined, and used for the calculation of solvation free energies. As an emerging concept and theory, the variational implicit solvation determines equilibrium solutesolvent interfaces and solvation free energies by minimizing a meanfield freeenergy functional. This free energy couples the surface energy, dispersive interaction, and electrostatic contribution. It can also incorporate molecular mechanical interactions. A levelset method is developed to numerically relax an initial interface of high free energy to an equilibrium in the direction of steepest descent. Numerical results demonstrate the initial success of the coupling of the levelset method with the variational theory of solvation, particularly in capturing the hydrophobic interaction. Such interactions are crucial to biomolecular structuring and dynamics, but are not well accounted for by SAS/SES implicitsolvent models. This is joint work with LiTien Cheng, Zhongming Wang, Yang Xie, Jianwei Che, Joachim Dzubiella, and J. Andrew McCammon.  
Tong Li (University of Iowa)  Stability of traveling waves in quasilinear hyperbolic systems with relaxation and diffusion 
Abstract: We establish the existence and the stability of traveling wave solutions of quasilinear hyperbolic systems with both relaxation and diffusion. The traveling wave solutions are shown to be asymptotically stable against small perturbations provided that the diffusion coefficient is bounded by a constant multiple of the relaxation time. The result provides an important first step toward the understanding of the transition from stability to instability as the diffusion coefficient increases.  
Michael Mascagni (Florida State University)  Novel stochastic methods in biochemical electrostatics 
Abstract: We present a novel Monte Carlo method for solving partial differential equation (PDE) boundaryvalue problems (BVPs) involving the PoissonBoltzmann equation (PBE). Such BVPs arise in many situations where the calculation of electrostatic properties of solvated large molecules is desired. These techniques are very accurate, and are fundamentally different than their deterministic counterparts. They are based on using the FeynmanKac formula to solve the Poisson and the linearized PBE, as well as the introduction of a stochastic method to enforce the boundary conditions on the surface of the molecule. In addition, we present an algorithm for computing the electrostatic free energy for all salt concentrations of interest, simultaneously. This, coupled with the naturally parallel nature of Monte Carlo methods, makes these techniques very appealing for studying solvationbased effects.  
Benedetta Mennucci (Università di Pisa)  An introduction to quantum mechanical continuum solvation models 
Abstract: Continuum solvation models have a quite long history which goes back to the first versions by Onsager (1936) and Kirkwood (1934), however only recently (starting since the 90’s) they have become one of the most used computational techniques in the field of molecular modelling. This has been made possible by two factors which will be presented and discussed in the present talk, namely the increase in the realism of the model on the one hand, and the coupling with quantummechanical approaches on the other hand. In particular, the talk will focus on a specific class of continuum solvation models, namely those using as a descriptor for the solvent polarization an apparent surface charge (ASC) spreading on the molecular cavity which contains the solute.  
Benedetta Mennucci (Università di Pisa)  Applications of quantum mechanical continuum solvation models to the study of molecular properties and spectroscopic features of molecular solutes in different environments 
Abstract: Examples of application of QM continuum models to the study of solvent effects on molecular properties and spectroscopies are presented and discussed together with their generalizations to hybrid continuum/discrete approaches in which the presence of specific interactions (e.g. solutesolvents Hbonds) is explicitly taken into account by including some solvent molecules strongly interacting with the solute.  
C. Melania Oana (University of Southern California)  Cross sections and photoelectron angular distributions in photodetachment from negative ions using EOMCCSD Dyson orbitals 
Abstract: Joint work with Anna I. Krylov. Experimental photoelectron angular distributions (PADs) contain information about the excited states of less stable compounds and their dissociation mechanism, but the interpretation of the results is difficult for molecules with complex electronic structure, e.g. NO dimer, CS2 photodissociation. Ionization crosssections and PADs can be calculated from the corresponding electronic transition dipole matrix elements. The wavefunction of the leaving electron is given by Dyson orbitals, which are the overlap between an N electron molecular wavefunction and the N1/N+1 electron wavefunction of the corresponding cation/anion. Our implementation of the Dyson orbitals calculation within the high level ab initio EOMIP/EACCSD method, allows the calculation of these terms for the ionization of electronically excited states and openshell species, when correlation effects become important. As a first approximation, the states of the ionized electron are described by plane waves expressed in the bases of spherical waves, E, l, m>. Currently, the calculation of photodetachment crosssections and anisotropies is benchmarked on atoms, and small molecules. Calculated PADs for NO dimer photodissociation allow qualitative comparison with experimental distributions. In the case of larger, anisotropic molecules, the development of better approximations for the description of the ionized electron is necessary.  
Isamu Ohnishi (Hiroshima University)  Macroscopic pattern formation of liquid crystal in kappacarrageenan gel 
Abstract: A macroscopic pattern consisting of liquid crystal layers in hydorgel is selforganized. The pattern forms when potassium ion diffuses into a kappacarrageenan solution from one end of the glass capillary that contains the kappacarrageenan solution. Both the distance between two adjacent liquidcrystalline layers (spacing, xn+1 −xn,) and thickness of liquid crystalline layers (width, wn) depend linearly on the distance from the diffusing end of the potassium ion xn. The time prior to the formation of the nth liquid crystalline layer tn depends linearly on x2 n. In addition, the spacing coefficient p is inversely proportional to the concentration of potassium ions. These results are in good agreement with the Liesegang henomenon. In this system the kappacarrageenan solution behaves as a supporting medium for the spatial pattern, as well as the pattern forming substance. The lower values of p, rather than the common Liesegang pattern, in this system could be attributed to the large molecular weight of the kappacarrageenan–potassium complex. The pattern consisted of discrete liquid crystal phases must be formed due to the much larger diffusion constant of potassium ion (diffusant) than that of kappacarrageenan (product).  
Modesto Orozco (Institute for Research in Biomedicine (IRB Barcelona))  Dimerization of formamide 
Abstract: No Abstract  
Benoit Roux (University of Chicago)  The membrane potential and its representation in computer simulations 
Abstract: A modified PoissonBoltzmann equation is developed from statistical mechanical considerations to describe the influence of the transmembrane potential on macromolecular systems [1]. Using a Green's function formalism, the electrostatic free energy of a protein associated with the membrane is expressed as the sum of three terms: a contribution from the energy required to charge the system's capacitance, a contribution corresponding to the interaction of the protein charges with the membrane potential, and a contribution corresponding to a voltageindependent reaction field free energy. The membrane potential, which is due to the polarization interface, is calculated in the absence of the protein charges, whereas the reaction field is calculated in the absence of transmembrane potential. Then, a theoretical framework is elaborated to account for the effect of a transmembrane potential in computer simulations with explicit solvent. It is shown that a simulation with a constant external electric field applied in the direction normal to the membrane is equivalent to the influence of surrounding infinite baths maintained to a voltage difference via ionexchanging electrodes connected to an electromotive force [2]. It is also shown that the linearlyweighted displacement charge within the simulation system tracks the net flow of charge through the external circuit comprising the electromotive force and the electrodes. Using a statistical mechanical reduction of the degrees of freedom of the external system, three distinct theoretical routes are formulated and examined for the purpose of characterizing the free energy of a protein embedded in a membrane that is submitted to a voltage difference. The two methods are compared and applied to the voltagegated potassium channel. 1. Roux, B. 1997. Influence of the membrane potential on the free energy of an intrinsic protein. Biophysical J. 73:29802989. 2. Roux, B. 2008. The membrane potential and its representation by a constant electric field in computer simulations. Biophys J. 95:42054216.  
Ridgway Scott (University of Chicago)  Second chances 
Abstract: No Abstract  
Robert D. Skeel (Purdue University)  A fast Nbody solver for the Poisson(Boltzmann) equation 
Abstract: Descriptions of implicit solvent models like the PoissonBoltzmann equation express the electrostatic potential as the solution of an elliptic PDE with delta function source terms. These equations are particularly good fits with iterative solvers that use a fast Nbody solver as a preconditioner. Also, modern architectures favor such algorithms due to their high ratio of floatingpoint operations to memory references. Two types of Nbody solvers can be distinguished: hierarchicalclustering algorithms, such as the celebrated fast multipole method, and kernelsplitting algorithms, such as the popular particlemesh Ewald method. By formulating the problem as that of computing a matrixvector product, the basic structure of these algorithms is elucidated. Additionally, evidence is presented indicating that kernelsplitting algorithms are much to be preferred for molecular simulations and that the virtually unknown multilevel summation method of Brandt and Lubrecht is the best among these. This method uses hierarchical interpolation of interaction potentials on nested grids to calculate energies and forces in linear time for both periodic and nonperiodic boundary conditions. This is joint work with David Hardy. Its application to the Poisson(Boltzmann) equation is being pursued in a collaboration with Stephen Bond.  
Mark E. Tuckerman (New York University)  Second chances 
Abstract: No Abstract  
Mark E. Tuckerman (New York University)  Ab initio molecular dynamics via the CarParrinello method: Basic ideas, theory, and algorithms 
Abstract: In an ab initio molecular dynamics calculation, the finitetemperature dynamics of a system is generated using forces obtained directly from electronic structure calculations performed ``on the fly'' as the simulation proceeds. Within this approach, manybody forces, electronic polarization, and chemical bondbreaking and forming evnets are treated explicitly, thereby allowing chemical processes in condensed phases to be studied efficiently and with reasonable accuracy. The method of Car and Parrinello, first introduced in 1985, allows such calculations to be performed within the elegant framework of an extended Lagrangian and has become an immensely popular approach for performing ab initio molecular dynamics simulations. The aim of this tutorial is to develop the basic theory of ab initio molecular dynamics and its implementation via the CarParrinello method. Questions of how ab initio molecular dynamics is derived from the Schroedinger equation, adiabatic dynamics and the justification of the CarParrinello approach, and several algorithmic issues including basis sets and pseudopotentials will be addressed.  
Mark E. Tuckerman (New York University)  Ab initio pathintegrals and specific applications of the CarParrinello approach to problems of aqueous ion solvation and transport 
Abstract: In this tutorial, we will show how to incorporate nuclear quantum effects into an ab initio molecular dynamics calculation via the Feynman pathintegral formulation of quantum statistical mechanics. Important algorithmic advances needed to accelerate the convergence of the calculations will be discussed as well as approximation dynamical pathintegral schemes. Finally, an application of the ab initio molecular dynamics and ab initio pathintegral approaches to the problem of the solvation and transport of topological charged defects in water will be discussed.  
Jason A. Wagoner (Stanford University)  Optimization of a hybrid implicit/explicit solvation model 
Abstract: Hybrid solvation models can be used in molecular dynamics simulations to extract the salient features of both explicit and implicit solvent methods, maintaining the atomic detail of solvent near regions of interest while removing such degrees of freedom elsewhere. We present such a hybrid solvation model that, in the spirit of previous methods, decomposes the simulation domain into explicit and bulk regions separated by an energetic barrier. The use of a Grand Canonical Monte Carlo scheme at the boundary is used to represent particle exchange with the bulk reservoir and extends the applicability of this model by allowing the use of a dynamic explicit domain. Current testing of this model is aimed at obtaining thermodynamic quantities within the explicit region with a focus on removing boundary artifacts for bulk liquid simulations. 
Donald G. Aronson  University of Minnesota  9/1/2002  8/31/2009 
Nathan A. Baker  Washington University School of Medicine  12/9/2008  12/12/2008 
Robert L. Baldwin  Stanford University  12/7/2008  12/11/2008 
Jaydeep P. Bardhan  Argonne National Laboratory  12/7/2008  12/12/2008 
Dezső Boda  University of Pannonia  12/7/2008  12/12/2008 
Stephen Bond  University of Illinois at UrbanaChampaign  12/8/2008  12/13/2008 
Daniel Jean Borgis  École Normale Supérieure  12/7/2008  12/12/2008 
Bernard R. Brooks  National Institutes of Health  12/7/2008  12/11/2008 
Peter Brune  University of Chicago  9/8/2008  6/30/2009 
MariaCarme T. Calderer  University of Minnesota  9/1/2008  6/30/2009 
Hannah Callender  University of Minnesota  9/1/2007  8/31/2009 
Roberto Cammi  Università di Parma, email: roberto.cammi@unipr.it  11/14/2008  12/20/2008 
Eric Cances  CERMICS  9/1/2008  12/23/2008 
Chiara Cappelli  Università di Pisa  12/6/2008  12/13/2008 
Alessandro Cembran  University of Minnesota  12/7/2008  12/12/2008 
Xianjin Chen  University of Minnesota  9/1/2008  8/31/2010 
Daniel M. Chipman  University of Notre Dame  9/14/2008  12/14/2008 
Stefano Corni  Consiglio Nazionale delle Ricerche (CNR)  12/7/2008  12/13/2008 
Ludovica Cecilia CottaRamusino  University of Minnesota  10/1/2007  12/12/2008 
Carles Curutchet  University of Toronto  12/6/2008  12/12/2008 
Allison Cuttler  University of California, San Diego  12/6/2008  12/11/2008 
Ismaila Dabo  Massachusetts Institute of Technology  12/7/2008  12/14/2008 
Yuqing Deng  Zymeworks Inc.  12/7/2008  12/12/2008 
Alfonso De Simone  University of Cambridge  12/3/2008  12/12/2008 
Florin Despa  University of California, Davis  12/7/2008  12/12/2008 
Olivier Dubois  University of Minnesota  9/3/2007  8/31/2009 
Robert S. Eisenberg  Rush University Medical Center  12/4/2008  12/12/2008 
Jorge Estevez  University of Minnesota  12/7/2008  12/12/2008 
Marcia O. Fenley  Florida State University  12/7/2008  12/12/2008 
Daniel Flath  Macalester College  8/27/2008  12/20/2008 
James Fonseca  Rush University Medical Center  12/6/2008  12/12/2008 
Christopher Fraser  University of Chicago  8/27/2008  6/30/2009 
Luca Frediani  University of Tromsø  12/7/2008  12/13/2008 
Jiali Gao  University of Minnesota  12/7/2008  12/12/2008 
Weiguo Gao  Fudan University  9/27/2008  12/8/2008 
Carlos J. GarciaCervera  University of California, Santa Barbara  9/2/2008  12/12/2008 
Janhavi Giri  Rush University Medical Center  12/6/2008  12/12/2008 
Jay Gopalakrishnan  University of Florida  9/1/2008  2/28/2009 
Donald Hamelberg  Georgia State University  12/7/2008  12/12/2008 
Jaeboem Han  University of Minnesota  12/7/2008  12/12/2008 
Timothy F. Havel  Massachusetts Institute of Technology  10/31/2008  12/12/2008 
Mark S. Herman  University of Minnesota  9/1/2008  8/31/2010 
Masahiro Higashi  University of Minnesota  12/8/2008  12/12/2008 
Peter Hinow  University of Minnesota  9/1/2007  8/31/2009 
Nina Singhal Hinrichs  University of Chicago  12/7/2008  12/12/2008 
Fumio Hirata  National Institutes of Natural Sciences  12/7/2008  12/12/2008 
Michael J. Holst  University of California, San Diego  12/7/2008  12/12/2008 
Jingfang Huang  University of North Carolina  12/30/2008  5/31/2009 
Jingfang Huang  University of North Carolina  12/7/2008  12/13/2008 
Yunkyong Hyon  University of Minnesota  9/1/2008  8/31/2010 
Mark Iwen  University of Minnesota  9/1/2008  8/31/2010 
Alexander Izzo  Bowling Green State University  9/1/2008  6/30/2009 
Lasse Jensen  Pennsylvania State University  12/7/2008  12/12/2008 
Srividhya Jeyaraman  University of Minnesota  9/1/2008  8/31/2010 
Lijian Jiang  University of Minnesota  9/1/2008  8/31/2010 
William L. Jorgensen  Yale University  12/8/2008  12/10/2008 
Hiqmet Kamberaj  University of Minnesota  12/7/2008  12/12/2008 
Markus Keel  University of Minnesota  7/21/2008  6/30/2009 
Carl Timothy Kelley  North Carolina State University  12/7/2008  12/12/2008 
Yongho Kim  University of Minnesota  12/7/2008  12/12/2008 
Matthew Gregg Knepley  Argonne National Laboratory  12/7/2008  12/13/2008 
Dmitry A. Kondrashov  University of Chicago  12/8/2008  12/13/2008 
Andriy Kovalenko  National Institute for Nanotechnology  12/6/2008  12/13/2008 
Anna Krylov  University of Southern California  9/25/2008  12/20/2008 
Claude Le Bris  CERMICS  9/11/2008  5/30/2009 
ChiunChang Lee  National Taiwan University  8/26/2008  7/31/2009 
Hijin Lee  Korea Advanced Institute of Science and Technology (KAIST)  12/8/2008  12/12/2008 
Bo Li  University of California, San Diego  12/7/2008  12/11/2008 
Tong Li  University of Iowa  11/2/2008  12/10/2008 
Yongfeng Li  University of Minnesota  9/1/2008  8/31/2010 
Pinsker Lin  University of Minnesota  12/7/2008  12/12/2008 
TaiChia Lin  National Taiwan University  8/23/2008  7/31/2009 
Chun Liu  University of Minnesota  9/1/2008  8/31/2010 
Mitchell Luskin  University of Minnesota  9/1/2008  6/30/2009 
Vasileios Maroulas  University of Minnesota  9/1/2008  8/31/2010 
Marcelo Marucho  Washington University School of Medicine  12/7/2008  12/12/2008 
Michael Mascagni  Florida State University  12/6/2008  12/12/2008 
Benedetta Mennucci  Università di Pisa  12/6/2008  12/13/2008 
Aurora Muñoz  Università di Pisa  12/6/2008  12/13/2008 
C. Melania Oana  University of Southern California  12/4/2008  12/20/2008 
Isamu Ohnishi  Hiroshima University  11/1/2008  1/17/2009 
Modesto Orozco  Institute for Research in Biomedicine (IRB Barcelona)  12/7/2008  12/12/2008 
B. Montgomery Pettitt  University of Houston  12/7/2008  12/12/2008 
Benoit Roux  University of Chicago  12/10/2008  12/12/2008 
Fadil Santosa  University of Minnesota  7/1/2008  6/30/2010 
Arnd Scheel  University of Minnesota  9/1/2008  6/30/2009 
Ridgway Scott  University of Chicago  9/1/2008  6/30/2009 
Tsvetanka Sendova  University of Minnesota  9/1/2008  8/31/2010 
Yuk Sham  University of Minnesota  9/1/2008  6/30/2009 
Tei Shi  University of Minnesota  12/7/2008  12/12/2008 
Heinz Siedentop  LudwigMaximiliansUniversität München  9/22/2008  12/19/2008 
Robert D. Skeel  Purdue University  12/8/2008  12/11/2008 
Lingchun Song  University of Minnesota  12/7/2008  12/12/2008 
Andrew M. Stein  University of Minnesota  9/1/2007  8/31/2009 
Andrij Trokhymchuk  Institute for condensed matter physics  12/6/2008  12/14/2008 
Donald G. Truhlar  University of Minnesota  9/1/2008  6/30/2009 
Mark E. Tuckerman  New York University  12/6/2008  12/15/2008 
Erkan Tüzel  University of Minnesota  9/1/2007  8/31/2009 
Sinisa Vukovic  University of Toronto  12/6/2008  12/13/2008 
Jason A. Wagoner  Stanford University  12/7/2008  12/12/2008 
Zhian Wang  University of Minnesota  9/1/2007  8/31/2009 
Zhongming Wang  University of California, San Diego  12/7/2008  12/12/2008 
Guowei Wei  Michigan State University  12/7/2008  12/11/2008 
KinYiu Wong  University of Minnesota  12/7/2008  12/12/2008 
Dexuan Xie  University of Wisconsin  9/1/2008  1/15/2009 
Wei Xiong  University of Minnesota  9/1/2008  8/31/2010 
Ke Yang  University of Minnesota  12/7/2008  12/12/2008 
Dmytro S. Yershov  University of Illinois at UrbanaChampaign  12/8/2008  12/13/2008 
Norio Yoshida  National Institutes of Natural Sciences  12/7/2008  12/12/2008 
Weigang Zhong  University of Minnesota  9/1/2008  8/31/2010 
Yongcheng Zhou  University of California, San Diego  12/7/2008  12/12/2008 