A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding.
about
Exploring the composition of protein-ligand binding sites on a large scaleGeofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability.Local interactions and the optimization of protein folding.Anti-cooperativity and cooperativity in hydrophobic interactions: Three-body free energy landscapes and comparison with implicit-solvent potential functions for proteins.Potential of mean force of association of large hydrophobic particles: toward the nanoscale limit.Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein GHydration and conformational equilibria of simple hydrophobic and amphiphilic solutesMinimizing frustration by folding in an aqueous environmentHydrophobic interactions in model enclosures from small to large length scales: non-additivity in explicit and implicit solvent models.Effects of lengthscales and attractions on the collapse of hydrophobic polymers in waterThe major transition state in folding need not involve the immobilization of side chainsSimulating the minimum core for hydrophobic collapse in globular proteinsMolecular simulation study of cooperativity in hydrophobic associationProtein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability.The role of surface charge in the desolvation process of gelatin: implications in nanoparticle synthesis and modulation of drug releaseEnergetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding ratesScoring protein interaction decoys using exposed residues (SPIDER): a novel multibody interaction scoring function based on frequent geometric patterns of interfacial residues.Thermodynamic and structural signatures of water-driven methane-methane attraction in coarse-grained mW water.Simple Physics-Based Analytical Formulas for the Potentials of Mean Force of the Interaction of Amino Acid Side Chains in Water. VII. Charged-Hydrophobic/Polar and Polar-Hydrophobic/Polar Side Chains.Shedding light on the hydrophobicity puzzleHydrophobic interactions in the formation of secondary structures in small peptides
P2860
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P2860
A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
A desolvation barrier to hydro ...... iting step in protein folding.
@en
A desolvation barrier to hydro ...... iting step in protein folding.
@nl
type
label
A desolvation barrier to hydro ...... iting step in protein folding.
@en
A desolvation barrier to hydro ...... iting step in protein folding.
@nl
prefLabel
A desolvation barrier to hydro ...... iting step in protein folding.
@en
A desolvation barrier to hydro ...... iting step in protein folding.
@nl
P2860
P356
P1433
P1476
A desolvation barrier to hydro ...... iting step in protein folding.
@en
P2860
P304
P356
10.1002/PRO.5560060210
P577
1997-02-01T00:00:00Z