Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.
about
Site-specific infrared probes of proteinsContribution of hydrogen bonds to protein stabilityAre current atomistic force fields accurate enough to study proteins in crowded environments?Characterizing a partially ordered miniprotein through folding molecular dynamics simulations: Comparison with the experimental data.Spectroscopic studies of protein folding: linear and nonlinear methodsEster carbonyl vibration as a sensitive probe of protein local electric field.Tackling force-field bias in protein folding simulations: folding of Villin HP35 and Pin WW domains in explicit water.Folding network of villin headpiece subdomain.Challenges in protein folding simulations: Timescale, representation, and analysisMaking connections between ultrafast protein folding kinetics and molecular dynamics simulations.The protein folding network indicates that the ultrafast folding mutant of villin headpiece subdomain has a deeper folding funnelSite-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules.Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulationSequence, structure, and cooperativity in folding of elementary protein structural motifs.Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding.Native state conformational heterogeneity of HP35 revealed by time-resolved FRET.Thermally induced protein unfolding probed by isotope-edited IR spectroscopy.Protein folding kinetics and thermodynamics from atomistic simulationEffect of macromolecular crowding on protein folding dynamics at the secondary structure level.Common structural transitions in explicit-solvent simulations of villin headpiece foldingMeasuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.Forces stabilizing proteinsNon-additive stabilization by halogenated amino acids reveals protein plasticity on a sub-angstrom scale.The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein.Equilibrium kinetic network of the villin headpiece in implicit solvent.Contribution of hydrophobic interactions to protein stability.Hydrophobic core formation and dehydration in protein folding studied by generalized-ensemble simulations.Protein unfolding mechanisms and their effects on folding experiments.Microscopic nucleation and propagation rates of an alanine-based α-helix.
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P2860
Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Probing the folding transition ...... hain and backbone mutagenesis.
@en
Probing the folding transition ...... hain and backbone mutagenesis.
@nl
type
label
Probing the folding transition ...... hain and backbone mutagenesis.
@en
Probing the folding transition ...... hain and backbone mutagenesis.
@nl
prefLabel
Probing the folding transition ...... hain and backbone mutagenesis.
@en
Probing the folding transition ...... hain and backbone mutagenesis.
@nl
P2860
P356
P1476
Probing the folding transition ...... chain and backbone mutagenesis
@en
P2093
Michelle R Bunagan
P2860
P304
P356
10.1021/JA901860F
P407
P577
2009-06-01T00:00:00Z