The importance of slow motions for protein functional loops. - Wikidata - awgldk - TriplyDB

The importance of slow motions for protein functional loops.

The importance of slow motions for protein functional loops.

http://www.wikidata.org/entity/Q37198485

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Structural and functional analysis of Hikeshi, a new nuclear transport receptor of Hsp70s Elastic network normal modes provide a basis for protein structure refinement ClustENM: ENM-Based Sampling of Essential Conformational Space at Full Atomic Resolution.Coupling between catalytic loop motions and enzyme global dynamics Common functionally important motions of the nucleotide-binding domain of Hsp70 Similarity in Shape Dictates Signature Intrinsic Dynamics Despite No Functional Conservation in TIM Barrel Enzymes.How an Inhibitor Bound to Subunit Interface Alters Triosephosphate Isomerase Dynamics Detecting transitions in protein dynamics using a recurrence quantification analysis based bootstrap method.The adaptive nature of protein residue networks.

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The importance of slow motions for protein functional loops.

http://www.wikidata.org/entity/Q37198485

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article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on 07 February 2012

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

The importance of slow motions for protein functional loops.

@en

The importance of slow motions for protein functional loops.

@nl

type

label

The importance of slow motions for protein functional loops.

@en

The importance of slow motions for protein functional loops.

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prefLabel

The importance of slow motions for protein functional loops.

@en

The importance of slow motions for protein functional loops.

@nl

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Physical Biology

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The importance of slow motions for protein functional loops.

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Andrzej Kloczkowski

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Aris Skliros

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Ataur R Katebi

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Debkanta Chakraborty

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Michael T Zimmermann

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Robert L Jernigan

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Saras Saraswathi

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Sumudu P Leelananda

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P2860

Advances in Homology Protein Structure Modeling

Structural similarity of loops in protein families: toward the understanding of protein evolution

Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins

High-resolution design of a protein loop

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase

Conformational changes in protein loops and helices induced by post-translational phosphorylation.

Modeling of loops in protein structures

A large data set comparison of protein structures determined by crystallography and NMR: statistical test for structural differences and the effect of crystal packing.

Modeling protein loops with knowledge-based prediction of sequence-structure alignment.

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10.1088/1478-3975/9/1/014001

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1

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2012-02-07T00:00:00Z

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22314977

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3783528

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