Force-field dependence of chignolin folding and misfolding: comparison with experiment and redesign.
about
Gaussian Accelerated Molecular Dynamics: Unconstrained Enhanced Sampling and Free Energy CalculationEnhanced, targeted sampling of high-dimensional free-energy landscapes using variationally enhanced sampling, with an application to chignolinComparing molecular dynamics force fields in the essential subspace.Starting-structure dependence of nanosecond timescale intersubstate transitions and reproducibility of MD-derived order parameters.Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein AssociationA study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamicsDependence of internal friction on folding mechanism.Accelerated molecular dynamics simulations of protein folding.Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formationSimple few-state models reveal hidden complexity in protein folding.ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB.Simple, yet powerful methodologies for conformational sampling of proteins.Relaxation mode analysis and Markov state relaxation mode analysis for chignolin in aqueous solution near a transition temperature.Communication: Multiple atomistic force fields in a single enhanced sampling simulation.The universality of β-hairpin misfolding indicated by molecular dynamics simulations.Efficient conformational sampling of peptides adsorbed onto inorganic surfaces: insights from a quartz binding peptide.Comparison of the structural characteristics of Cu(2+)-bound and unbound α-syn12 peptide obtained in simulations using different force fields.Application of reference-modified density functional theory: Temperature and pressure dependences of solvation free energy.Accelerated weight histogram method for exploring free energy landscapes.Enhanced conformational sampling method for proteins based on the TaBoo SeArch algorithm: application to the folding of a mini-protein, chignolin.Relaxation mode analysis for molecular dynamics simulations of proteins.
P2860
Q27301372-687A1302-89ED-4535-8077-EFA065C97F57Q28601123-75C46F3E-DEF1-4C53-8963-66BBE2CBAC06Q30373070-AC7DB186-3B75-47B2-A166-CD9FC5F54E98Q30577861-7759BFA0-823A-4FF5-B9C0-72E382821D14Q34503099-71958010-CFA0-40CD-B0B4-196DE0DFEC90Q34553763-B0E76D4B-F3F7-4D20-A29A-8740A7527BD1Q35233778-C1599AFA-6D44-43A0-BE39-73DBB1DBF452Q35804657-1862FA2A-7FA9-4331-9F50-842C6E88EAD4Q36207942-F640D82A-3EBF-4975-A0D1-8519DBA4E801Q36397878-F30E3BAD-A5BF-4413-9CBB-7724F6A8629CQ36766916-39A70DC2-FE59-4FC3-A60E-3E9473AEB7E8Q38346856-45C09C26-7BAD-4D5F-B1CD-2C3AF3C060CCQ40475576-E9E7E83A-E77B-4132-AE03-254F79A9C5C8Q44858542-29ABAD2C-F813-4898-8EE6-0DB6BCA557F6Q44873453-3AB78308-359C-43F3-B244-2E1515A39559Q44989862-73B50CB6-DBEB-47BF-ABAD-F5A0FE4BA294Q46066811-03A7C606-7D72-4E94-9933-E17A5B0617BEQ47425338-E4252073-5ACE-4FA9-8FAB-E496CF941796Q47445087-C7A134D5-323D-48DE-A49A-8AA6B8FC3444Q50957837-C5835903-9F49-44F3-B614-830ABEC1E199Q55130435-5E69A674-0665-4BC8-A033-29CAC56BF90D
P2860
Force-field dependence of chignolin folding and misfolding: comparison with experiment and redesign.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Force-field dependence of chig ...... with experiment and redesign.
@en
type
label
Force-field dependence of chig ...... with experiment and redesign.
@en
prefLabel
Force-field dependence of chig ...... with experiment and redesign.
@en
P2860
P1433
P1476
Force-field dependence of chig ...... with experiment and redesign.
@en
P2093
Alfonso De Simone
Petra Kührová
P2860
P304
P356
10.1016/J.BPJ.2012.03.024
P407
P577
2012-04-01T00:00:00Z