|Other titles||Electrostatic interactions in solution., Computational chemistry, biophysics, and aqueous solutions.|
|Statement||editors, Lawrence R. Pratt, Gerhard Hummer.|
|Series||AIP conference proceedings -- 492., AIP conference proceedings -- no. 492.|
|Contributions||Pratt, Lawrence Riley, 1950-, Hummer, Gerhard., Workshop on Treatment of Electrostatic Interactions in Computer Simulations of Condensed Media (1999 : Santa Fe, N.M.)|
|The Physical Object|
|Pagination||ix, 534 p. :|
|Number of Pages||534|
|LC Control Number||99067531|
Abstract. Electrostatic interactions are crucial for both the accuracy and performance of atomistic biomolecular simulations. In this chapter we review well-established methods and current developments aiming at efficiency and by: 4. On the theory of electrostatic interactions in suspensions This book is designed to critically review experimental findings on ionic polymers and colloidal particles and to prove a theoretical Author: Willem Mulder. Conference on Simulation And Theory Of Electrostatic Interactions In Solution. By Gerhard Hummer and Lawrence R Pratt. Topics: Nuclear Physics. Year: OAI identifier: oai: Provided by: Joint Author: Gerhard Hummer and Lawrence R Pratt. Conference on Simulation And Theory Of Electrostatic Interactions In Solution By Gerhard Hummer and Lawrence R Pratt Topics: Nuclear Physics.
The electrostatic theory was developed by nineteenth-century phys-icists who did not have a complete picture of the atomic structure of matter. This led to a theory that viewed any matter as a featureless continuum. Such a large-scale macroscopic theory can be used in considering average electrostatic interactions for distances much. Using a Debye–Hückel approximation for the correlation functions of the bulk electrolyte and a simple basis expansion for the protein–salt direct correlation functions, we obtain a very simple variational expression for the electrostatic component of the excess chemical potential of a protein in an electrolyte solution. The predictions of. An Overview of Electrostatic Free Energy Computations for Solutions and Proteins | Journal of Chemical Theory and Computation Free energy simulations for electrostatic and charging processes in complex molecular systems encounter specific difficulties owing to the long-range, 1/r Coulomb interaction. Thus the key requirement for quantative understanding of the action of biological molecules is the ability to correlate electrostatic interactions with structural information. To appreciate this point it is useful to compare the electrostatic energy of a charged amino acid in a polar solvent to the corresponding van der Waals energy.
For molecular dynamics simulation, the long-range interactions between particles, such as electrostatic interactions, are the most time-consuming computation because of their slow convergence in simulation space, which approximately take up 80% of the total simulation time. P. Hünenberger, Simulation and Theory of Electrostatic Interactions in Solution: Computational Chemistry, Biophysics and Aqueous Solution (American Institute of Physics, New York, USA, ). Google Scholar; S. Boresch and O. Steinhauser, J. Chem. Phys. , (). , Google Scholar Scitation, ISI, CAS; B. A. Solution: These are both ions at intermediate distances, so their electrostatic interaction can be approximated using Coulomb's law. The charge-charge distance is given (5 Å). The charges, q A and q B, are the elementary charge of a proton/electron for the Na+ cation and the Cl- anion, respectively. The intermolecular interactions between cellobiose/cellobiose monoacetoacetate and water molecules were calculated, and comparison of hydroxyl-water and acetoacetate ester-water interactions was made in terms of average non-covalent interaction (aNCI) and the electrostatic potential (ESP) analyses.