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Modulation of frustration in folding by sequence permutation.

Modulation of frustration in folding by sequence permutation.

http://www.wikidata.org/entity/Q33971729

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MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling The Structure of a Thermophilic Kinase Shapes Fitness upon Random Circular Permutation Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY.Folding of proteins with a flavodoxin-like architecture.Sequence-, structure-, and dynamics-based comparisons of structurally homologous CheY-like proteins.Progress in small-angle scattering from biological solutions at high-brilliance synchrotrons.Frustration, function and folding.The binding mechanism of a novel nicotinamide isostere inhibiting with TNKSs: a molecular dynamic simulation and binding free energy calculation.

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Modulation of frustration in folding by sequence permutation.

http://www.wikidata.org/entity/Q33971729

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2014 nî lūn-bûn

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2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

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name

Modulation of frustration in folding by sequence permutation.

@ast

Modulation of frustration in folding by sequence permutation.

@en

type

label

Modulation of frustration in folding by sequence permutation.

@ast

Modulation of frustration in folding by sequence permutation.

@en

prefLabel

Modulation of frustration in folding by sequence permutation.

@ast

Modulation of frustration in folding by sequence permutation.

@en

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PNAS.1324230111

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Proceedings of the National Academy of Sciences of the United States of America

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Modulation of frustration in folding by sequence permutation

@en

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C Robert Matthews

http://www.w3.org/2001/XMLSchema#string

Charles L Brooks

http://www.w3.org/2001/XMLSchema#string

Karunesh Arora

http://www.w3.org/2001/XMLSchema#string

Liang Guo

http://www.w3.org/2001/XMLSchema#string

Osman Bilsel

http://www.w3.org/2001/XMLSchema#string

R Paul Nobrega

http://www.w3.org/2001/XMLSchema#string

Raul A Barrea

http://www.w3.org/2001/XMLSchema#string

Sagar V Kathuria

http://www.w3.org/2001/XMLSchema#string

Srinivas Chakravarthy

http://www.w3.org/2001/XMLSchema#string

Thomas C Irving

http://www.w3.org/2001/XMLSchema#string

P2860

CHARMM: the biomolecular simulation program

Crystal structure of Escherichia coli CheY refined at 1.7-A resolution

Determination and analysis of urea and guanidine hydrochloride denaturation curves

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

Prediction of folding mechanism for circular-permuted proteins.

Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.

Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics.

The protein folding 'speed limit'.

Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediates

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