Functional modulation of a protein folding landscape via side-chain distortion - Test2 - elhamkhani - TriplyDB

Functional modulation of a protein folding landscape via side-chain distortion

Functional modulation of a protein folding landscape via side-chain distortion

http://www.wikidata.org/entity/Q27679315

about

Keep on moving: discovering and perturbing the conformational dynamics of enzymes Conserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states.

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P2860

Functional modulation of a protein folding landscape via side-chain distortion

http://www.wikidata.org/entity/Q27679315

description

2012 nî lūn-bûn

@nan

2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Functional modulation of a protein folding landscape via side-chain distortion

@ast

Functional modulation of a protein folding landscape via side-chain distortion

@en

Functional modulation of a protein folding landscape via side-chain distortion

@nl

type

label

Functional modulation of a protein folding landscape via side-chain distortion

@ast

Functional modulation of a protein folding landscape via side-chain distortion

@en

Functional modulation of a protein folding landscape via side-chain distortion

@nl

prefLabel

Functional modulation of a protein folding landscape via side-chain distortion

@ast

Functional modulation of a protein folding landscape via side-chain distortion

@en

Functional modulation of a protein folding landscape via side-chain distortion

@nl

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PNAS.1119274109

P1433

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

P1476

Functional modulation of a protein folding landscape via side-chain distortion

@en

P2093

Brian A Kelch

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

David A Agard

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

Neema L Salimi

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

P2860

Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Unfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable alpha-lytic protease

Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei

Conformational strain in the hydrophobic core and its implications for protein folding and design

Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior

Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability

Distortion of flavin geometry is linked to ligand binding in cholesterol oxidase

1.2A-resolution crystal structures reveal the second tetrahedral intermediates of streptogrisin B (SGPB)

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9414-9

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scholarly article

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10.1073/PNAS.1119274109

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24

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109

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2012-06-12T00:00:00Z

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225064625

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22635267

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P921

protein folding

P932

3386061

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