R
Robert B. Best
Researcher at National Institutes of Health
Publications - 188
Citations - 19728
Robert B. Best is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Protein folding & Intrinsically disordered proteins. The author has an hindex of 63, co-authored 187 publications receiving 16085 citations. Previous affiliations of Robert B. Best include Medical Research Council & Center for Information Technology.
Papers
More filters
Journal ArticleDOI
Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ(1) and χ(2) dihedral angles.
Robert B. Best,Xiao Zhu,Jihyun Shim,Pedro E. M. Lopes,Jeetain Mittal,Michael Feig,Alexander D. MacKerell +6 more
TL;DR: The results indicate that the revised CHARMM 36 parameters represent an improved model for the modeling and simulation studies of proteins, including studies of protein folding, assembly and functionally relevant conformational changes.
Journal ArticleDOI
Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides.
Robert B. Best,Gerhard Hummer +1 more
TL;DR: Simple backbone energy corrections are determined for two force fields to reproduce the fraction of helix measured in short peptides at 300 K, showing that the dependence of the helix content on temperature is too weak, a problem shared with other force fields.
Journal ArticleDOI
Simultaneous determination of protein structure and dynamics
Kresten Lindorff-Larsen,Kresten Lindorff-Larsen,Robert B. Best,Robert B. Best,Mark A. DePristo,Mark A. DePristo,Christopher M. Dobson,Michele Vendruscolo +7 more
TL;DR: The procedure combines the strengths of nuclear magnetic resonance spectroscopy—for obtaining experimental information at the atomic level about the structural and dynamical features of proteins—with the ability of molecular dynamics simulations to explore a wide range of protein conformations.
Journal ArticleDOI
Balanced Protein–Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association
TL;DR: It is found that a modest strengthening of protein–water interactions is sufficient to recover the correct dimensions of intrinsically disordered or unfolded proteins, as determined by direct comparison with small-angle X-ray scattering and Förster resonance energy transfer data.
Journal ArticleDOI
Polarizable Atomic Multipole-Based AMOEBA Force Field for Proteins
TL;DR: Initial results suggest the AMOEBA polarizable multipole force field is able to describe the structure and energetics of peptides and proteins, in both gas-phase and solution environments.