Are current atomistic force fields accurate enough to study proteins in crowded environments?
about
Biomolecular interactions modulate macromolecular structure and dynamics in atomistic model of a bacterial cytoplasm.COFFDROP: A Coarse-Grained Nonbonded Force Field for Proteins Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of Amino AcidsBalanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein AssociationCaution is required in interpretation of mutations in the voltage sensing domain of voltage gated channels as evidence for gating mechanismsAssessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding.Quantitative interpretation of FRET experiments via molecular simulation: force field and validation.Transient helicity in intrinsically disordered Axin-1 studied by NMR spectroscopy and molecular dynamics simulations.NANOGOLD decorated by pHLIP peptide: comparative force field study.Temperature-sensitive gating of TRPV1 channel as probed by atomistic simulations of its trans- and juxtamembrane domains.Reparametrization of Protein Force Field Nonbonded Interactions Guided by Osmotic Coefficient Measurements from Molecular Dynamics Simulations.Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.Osmotic Pressure Simulations of Amino Acids and Peptides Highlight Potential Routes to Protein Force Field Parameterization.Residue-Specific Force Field (RSFF2) Improves the Modeling of Conformational Behavior of Peptides and Proteins.Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.Enhanced unbiased sampling of protein dynamics using evolutionary coupling information.Replica exchange molecular dynamics simulation of cross-fibrillation of IAPP and PrP106-126.Effects of force fields on the conformational and dynamic properties of amyloid β(1-40) dimer explored by replica exchange molecular dynamics simulations.Slow-Down in Diffusion in Crowded Protein Solutions Correlates with Transient Cluster Formation.Bead-Level Characterization of Early-Stage Amyloid β42 Aggregates: Nuclei and Ionic Concentration Effects.Specific DNA sequences allosterically enhance protein-protein interaction in a transcription factor through modulation of protein dynamics: implications for specificity of gene regulation.A multi-resolution model to capture both global fluctuations of an enzyme and molecular recognition in the ligand-binding site.Recent advances in automated protein design and its future challenges.New tricks for old dogs: improving the accuracy of biomolecular force fields by pair-specific corrections to non-bonded interactions.Computational close up on protein-protein interactions: how to unravel the invisible using molecular dynamics simulations?Dynamics and Thermodynamics of Transthyretin Association from Molecular Dynamics Simulations.Distribution of dopant ions around poly(3,4-ethylenedioxythiophene) chains: a theoretical study
P2860
Q28109324-1D622492-6BD5-45C4-990F-745AEF95B836Q34503075-9D8A421F-C828-426A-B7D8-2BD89F7751B6Q34503099-28F3CAA3-8373-482C-B50D-A0623E28714BQ35016639-3E7136C5-7556-48F3-979C-D6B34EE3296AQ35663714-7071CB1C-D217-4554-A9CC-F63FC25AC341Q35688357-5F6937A4-09DD-43C9-A675-FD202F90948BQ36326844-941068CF-F3CD-4C85-B264-4F3D422E249BQ41027474-84D9F5BC-4CA7-4472-9CEA-6FEECD8C8630Q41052388-BC5F2E8F-3A1D-4179-9B43-E584A7EB7FA9Q41250855-7FACD963-8C25-4569-9738-75CC2DC0E8B7Q41600734-1104367F-CFD0-4D65-93DB-31DA4974F3D7Q41633141-C74E6C5B-C471-4548-9ADB-1A796CCBDEC7Q41869632-95568BDB-95B2-4E72-8EF4-E4ADFE20BDDDQ42022642-76F21847-276A-49B0-BE88-B765882A0952Q42277476-7BB69009-A965-476F-9215-7991268AC8AAQ46552313-7A08E857-59E1-4C33-86C9-F60431CC0335Q47299318-F7B2E581-A69C-4032-9196-26D53D02847DQ47389171-A1188640-83F9-4E6F-88EF-877C79BCE7ECQ47815180-122BE480-C570-4161-8817-DF83E63058E5Q50620927-5A8FE419-32EB-4822-A26B-48F620C735D9Q51434391-EC9F23D7-A50C-4227-BBA9-47A7352EC554Q52309659-BBC59EB2-3EE3-473E-936A-FE05BA77D9F9Q52353173-A81394B8-2876-48E0-B038-9A3F545EBA4CQ53347950-758EB7FB-FAFF-4419-80DE-6A1ED532ACEFQ55417366-8B884EE2-EAC7-40BA-B855-2876D0891F0AQ58224119-DE50063E-37C7-4FA0-AD84-C370772073D7
P2860
Are current atomistic force fields accurate enough to study proteins in crowded environments?
description
2014 nî lūn-bûn
@nan
2014 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Are current atomistic force fi ...... teins in crowded environments?
@ast
Are current atomistic force fi ...... teins in crowded environments?
@en
type
label
Are current atomistic force fi ...... teins in crowded environments?
@ast
Are current atomistic force fi ...... teins in crowded environments?
@en
prefLabel
Are current atomistic force fi ...... teins in crowded environments?
@ast
Are current atomistic force fi ...... teins in crowded environments?
@en
P2860
P1476
Are current atomistic force fi ...... teins in crowded environments?
@en
P2093
Bojan Zagrovic
P2860
P304
P356
10.1371/JOURNAL.PCBI.1003638
P577
2014-05-22T00:00:00Z