Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding
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Hydration dynamics at fluorinated protein surfacesWater mediation is essential to nucleation of β-turn formation in peptide folding motifs.Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau.Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water.Parallel Generalized Born Implicit Solvent Calculations with NAMD.GPU/CPU Algorithm for Generalized Born/Solvent-Accessible Surface Area Implicit Solvent Calculations.Alteration of water structure by peptide clusters revealed by neutron scattering in the small-angle region (below 1 Å(-1))Recent advances in implicit solvent-based methods for biomolecular simulationsTurn-directed α-β conformational transition of α-syn12 peptide at different pH revealed by unbiased molecular dynamics simulations.Mapping amyloid-β(16-22) nucleation pathways using fluorescence lifetime imaging microscopy.Effects of different force fields and temperatures on the structural character of Abeta (12-28) peptide in aqueous solution.Hydrated and dehydrated tertiary interactions--opening and closing--of a four-helix bundle peptide.An improved coarse-grained model of solvation and the hydrophobic effect.Effects of pH and temperature on the structural and thermodynamic character of alpha-syn12 peptide in aqueous solution.Folding propensity of anoplin: A molecular dynamics study of the native peptide and four mutated isoforms.Structure-based design of broadly protective group a streptococcal M protein-based vaccines.Proceedings of the Seventh Annual UT-ORNL-KBRIN Bioinformatics Summit 2008.Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water.Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides.A comparative study of two different force fields on structural and thermodynamics character of H1 peptide via molecular dynamics simulations.Why the OPLS-AA force field cannot produce the β-hairpin structure of H1 peptide in solution when comparing with the GROMOS 43A1 force field?
P2860
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P2860
Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding
description
2007 nî lūn-bûn
@nan
2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
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2007年學術文章
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2007年學術文章
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2007年學術文章
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name
Dehydration-driven solvent exp ...... iving force in peptide folding
@ast
Dehydration-driven solvent exp ...... iving force in peptide folding
@en
type
label
Dehydration-driven solvent exp ...... iving force in peptide folding
@ast
Dehydration-driven solvent exp ...... iving force in peptide folding
@en
prefLabel
Dehydration-driven solvent exp ...... iving force in peptide folding
@ast
Dehydration-driven solvent exp ...... iving force in peptide folding
@en
P2093
P2860
P356
P1476
Dehydration-driven solvent exp ...... iving force in peptide folding
@en
P2093
Alfredo Di Nola
Andrea Amadei
Isabella Daidone
Jeremy C Smith
Martin B Ulmschneider
P2860
P304
15230-15235
P356
10.1073/PNAS.0701401104
P407
P577
2007-09-19T00:00:00Z