Experimental evaluation of topological parameters determining protein-folding rates.
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Structural and Thermodynamic Analysis of a Conformationally Strained Circular Permutant of Barnase †Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesThe protein folding problemRandom amino acid mutations and protein misfolding lead to Shannon limit in sequence-structure communication.A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins.Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins.Biophysics of protein evolution and evolutionary protein biophysicsThe topomer search model: A simple, quantitative theory of two-state protein folding kinetics.Critical nucleation size in the folding of small apparently two-state proteins.Native and nonnative conformational preferences in the urea-unfolded state of barstar.Knotted and topologically complex proteins as models for studying folding and stability.Perspective: Coarse-grained models for biomolecular systems.How cooperative are protein folding and unfolding transitions?The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.The response of Greek key proteins to changes in connectivity depends on the nature of their secondary structure.Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation.A Ca2+-sensing molecular switch based on alternate frame protein folding.Conservation of inter-residue interactions and prediction of folding rates of domain repeats.Folding mechanism of all-beta globular proteins.Glutamine Hydrolysis by Imidazole Glycerol Phosphate Synthase Displays Temperature Dependent Allosteric Activation.Folding and misfolding in a naturally occurring circularly permuted PDZ domain.
P2860
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P2860
Experimental evaluation of topological parameters determining protein-folding rates.
description
2002 nî lūn-bûn
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2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
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2002年论文
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name
Experimental evaluation of topological parameters determining protein-folding rates.
@ast
Experimental evaluation of topological parameters determining protein-folding rates.
@en
Experimental evaluation of topological parameters determining protein-folding rates.
@nl
type
label
Experimental evaluation of topological parameters determining protein-folding rates.
@ast
Experimental evaluation of topological parameters determining protein-folding rates.
@en
Experimental evaluation of topological parameters determining protein-folding rates.
@nl
prefLabel
Experimental evaluation of topological parameters determining protein-folding rates.
@ast
Experimental evaluation of topological parameters determining protein-folding rates.
@en
Experimental evaluation of topological parameters determining protein-folding rates.
@nl
P2093
P2860
P356
P1476
Experimental evaluation of topological parameters determining protein-folding rates.
@en
P2093
Erik J Miller
Kael F Fischer
Susan Marqusee
P2860
P304
10359-10363
P356
10.1073/PNAS.162219099
P407
P577
2002-07-29T00:00:00Z