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Conformational Entropy of Intrinsically Disordered Proteins from Amino Acid TriadsCoupling between properties of the protein shape and the rate of protein folding.In vitro polymerization of a functional Escherichia coli amyloid protein.On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate.Predicting protein folding rates from geometric contact and amino acid sequence.Non-active site mutations disturb the loop dynamics, dimerization, viral budding and egress of VP40 of the Ebola virus.KineticDB: a database of protein folding kinetics.Nucleation-based prediction of the protein folding rate and its correlation with the folding nucleus size.Sequence determinants of protein folding rates: positive correlation between contact energy and contact range indicates selection for fast folding.Molecular Dynamic Simulation of Space and Earth-Grown Crystal Structures of Thermostable T1 Lipase Geobacillus zalihae Revealed a Better Structure.
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P2860
description
im April 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published on 01 April 2006
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в січні 2006
@uk
name
Entropy capacity determines protein folding
@en
Entropy capacity determines protein folding
@nl
type
label
Entropy capacity determines protein folding
@en
Entropy capacity determines protein folding
@nl
prefLabel
Entropy capacity determines protein folding
@en
Entropy capacity determines protein folding
@nl
P921
P356
P1433
P1476
Entropy capacity determines protein folding
@en
P2093
Oxana V Galzitskaya
P2860
P304
P356
10.1002/PROT.20851
P407
P577
2006-04-01T00:00:00Z