J
Junmei Wang
Researcher at University of Pittsburgh
Publications - 189
Citations - 37934
Junmei Wang is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 52, co-authored 162 publications receiving 31230 citations. Previous affiliations of Junmei Wang include University of California, San Francisco & University of California, San Diego.
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Development and testing of a general amber force field.
TL;DR: A general Amber force field for organic molecules is described, designed to be compatible with existing Amber force fields for proteins and nucleic acids, and has parameters for most organic and pharmaceutical molecules that are composed of H, C, N, O, S, P, and halogens.
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A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations.
Yong Duan,Chun Wu,Shibasish Chowdhury,Mathew C. Lee,Guoming Xiong,Wei Zhang,Rong Yang,Piotr Cieplak,Piotr Cieplak,Ray Luo,Tai-Sung Lee,Tai-Sung Lee,James W. Caldwell,Junmei Wang,Peter A. Kollman +14 more
TL;DR: A third‐generation point‐charge all‐atom force field for proteins is developed and initial tests on peptides demonstrated a high‐degree of similarity between the calculated and the statistically measured Ramanchandran maps for both Ace‐Gly‐nme and Ace‐Ala‐Nme di‐peptides.
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Automatic atom type and bond type perception in molecular mechanical calculations.
TL;DR: Anautomatic algorithm of perceiving atom types that are defined in a description table, and an automatic algorithm of assigning bond types just based on atomic connectivity are presented.
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How Well Does a Restrained Electrostatic Potential (RESP) Model Perform in Calculating Conformational Energies of Organic and Biological Molecules
TL;DR: In this paper, the authors present conformational energies for a molecular mechanical model (Parm99) developed for organic and biological molecules using the restrained electrostatic potential (RESP) approach to derive the partial charges.
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Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations.
TL;DR: An extensive study of 59 ligands interacting with six different proteins finds that MM/PBSA can serve as a powerful tool in drug design, where correct ranking of inhibitors is often emphasized, and the accuracy of the binding free energies calculated by three Generalized Born (GB) models is evaluated.