Phi-value analysis by molecular dynamics simulations of reversible folding.
about
CHARMM: the biomolecular simulation programComparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.On the precision of experimentally determined protein folding rates and phi-valuesAtomic-level characterization of the structural dynamics of proteinsThe redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulationsP versus Q: structural reaction coordinates capture protein folding on smooth landscapes.Ensemble versus single-molecule protein unfolding.Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulationsIndependent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate stateProtein folding kinetics and thermodynamics from atomistic simulationMethods for the accurate estimation of confidence intervals on protein folding phi-valuesProtein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.High temperature unfolding simulations of the TRPZ1 peptide.New insights into the folding of a β-sheet miniprotein in a reduced space of collective hydrogen bond variables: application to a hydrodynamic analysis of the folding flow.One-dimensional barrier-preserving free-energy projections of a beta-sheet miniprotein: new insights into the folding process.How does a simplified-sequence protein fold?First passage analysis of the folding of a β-sheet miniprotein: is it more realistic than the standard equilibrium approach?Some recommendations for the practitioner to improve the precision of experimentally determined protein folding rates and phi values.An error analysis for two-state protein-folding kinetic parameters and phi-values: progress toward precision by exploring pH dependencies on Leffler plots.Characterization of protein folding by a Φ-value calculation with a statistical-mechanical model.Testing simplified proteins models of the hPin1 WW domain.Solvation of the folding-transition state in Pseudomonas aeruginosa azurin is modulated by metal: Solvation of azurin's folding nucleus.Transition states in protein folding kinetics: modeling phi-values of small beta-sheet proteins.C(α) torsion angles as a flexible criterion to extract secrets from a molecular dynamics simulation.Combination of Markov state models and kinetic networks for the analysis of molecular dynamics simulations of peptide folding.
P2860
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P2860
Phi-value analysis by molecular dynamics simulations of reversible folding.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Phi-value analysis by molecular dynamics simulations of reversible folding.
@ast
Phi-value analysis by molecular dynamics simulations of reversible folding.
@en
type
label
Phi-value analysis by molecular dynamics simulations of reversible folding.
@ast
Phi-value analysis by molecular dynamics simulations of reversible folding.
@en
prefLabel
Phi-value analysis by molecular dynamics simulations of reversible folding.
@ast
Phi-value analysis by molecular dynamics simulations of reversible folding.
@en
P2093
P2860
P356
P1476
Phi-value analysis by molecular dynamics simulations of reversible folding.
@en
P2093
Amedeo Caflisch
Francesco Rao
Giovanni Settanni
P2860
P304
P356
10.1073/PNAS.0406754102
P407
P577
2005-01-11T00:00:00Z