Allostery in the ferredoxin protein motif does not involve a conformational switch - Test2 - elhamkhani - TriplyDB

Allostery in the ferredoxin protein motif does not involve a conformational switch

Allostery in the ferredoxin protein motif does not involve a conformational switch

http://www.wikidata.org/entity/Q27666732

about

Allosteric control in a metalloprotein dramatically alters function.Two-step mechanism for modifier of transcription 1 (Mot1) enzyme-catalyzed displacement of TATA-binding protein (TBP) from DNA.The dominant folding route minimizes backbone distortion in SH3.One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?Native structure-based modeling and simulation of biomolecular systems per mouse click.Analysis of the interaction interfaces of the N-terminal domain from Pseudomonas aeruginosa MutL The role of atomic level steric effects and attractive forces in protein folding Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles.The shadow map: a general contact definition for capturing the dynamics of biomolecular folding and function Molecular Dynamics Simulations of the [2Fe-2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release.The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.

P2860

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P2860

Allostery in the ferredoxin protein motif does not involve a conformational switch

http://www.wikidata.org/entity/Q27666732

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Allostery in the ferredoxin protein motif does not involve a conformational switch

@ast

Allostery in the ferredoxin protein motif does not involve a conformational switch

@en

Allostery in the ferredoxin protein motif does not involve a conformational switch

@nl

type

label

Allostery in the ferredoxin protein motif does not involve a conformational switch

@ast

Allostery in the ferredoxin protein motif does not involve a conformational switch

@en

Allostery in the ferredoxin protein motif does not involve a conformational switch

@nl

prefLabel

Allostery in the ferredoxin protein motif does not involve a conformational switch

@ast

Allostery in the ferredoxin protein motif does not involve a conformational switch

@en

Allostery in the ferredoxin protein motif does not involve a conformational switch

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PNAS.1019502108

P1433

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

P1476

Allostery in the ferredoxin protein motif does not involve a conformational switch

@en

P2093

Alex Fish

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

Alexander Schug

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Dominique T Capraro

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Dorit Michaeli

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Heiko Lammert

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John A Zuris

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Maria A Luca

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Melinda Roy

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

Oded Livnah

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

Odelia Shimshon

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P2860

Conformational transitions of adenylate kinase: switching by cracking

Improved methods for building protein models in electron density maps and the location of errors in these models

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure determination at 1.4 A resolution of ferredoxin from the green alga Chlorella fusca

Structure of the carboxyl-terminal Src kinase, Csk

The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation

Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120

Asymmetric dimeric structure of ferredoxin-NAD(P)+ oxidoreductase from the green sulfur bacterium Chlorobaculum tepidum: implications for binding ferredoxin and NADP+

Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites

Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 A resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis

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2240-5

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scholarly article

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10.1073/PNAS.1019502108

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6

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108

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Rachel Nechushtai

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2011-02-08T00:00:00Z

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49785011

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21266547

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3038707

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