Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins. - Test2 - elhamkhani - TriplyDB

Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.

Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.

http://www.wikidata.org/entity/Q30157912

about

Cavities determine the pressure unfolding of proteins Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motions Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations.Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.Extracting function from a beta-trefoil folding motif Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.

P2860

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P2860

Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.

http://www.wikidata.org/entity/Q30157912

description

2007 nî lūn-bûn

@nan

2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հուլիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

@zh-hk

2007年論文

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2007年論文

@zh-tw

2007年论文

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name

Partially folded states of sta ...... hierarchy of OB-fold proteins.

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Partially folded states of sta ...... hierarchy of OB-fold proteins.

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type

label

Partially folded states of sta ...... hierarchy of OB-fold proteins.

@ast

Partially folded states of sta ...... hierarchy of OB-fold proteins.

@en

prefLabel

Partially folded states of sta ...... hierarchy of OB-fold proteins.

@ast

Partially folded states of sta ...... hierarchy of OB-fold proteins.

@en

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Partially folded states of sta ...... hierarchy of OB-fold proteins.

@en

P2093

Andrei T Alexandrescu

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

Emma Watson

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

Evelyn L Irimies

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

William M Matousek

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

P2860

Functional evolution of two subtly different (similar) folds

Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability

Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus

Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys)

One-step evolution of a dimer from a monomeric protein

NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease

Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site

SCOP: a structural classification of proteins database for the investigation of sequences and structures

Protein structure prediction and structural genomics

Principles that govern the folding of protein chains

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9484-9494

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scholarly article

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10.1021/BI700532J

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33

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46

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2007-07-28T00:00:00Z

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6178475

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17661445

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P921

OB-fold nucleic acid binding domain

protein folding

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2128864

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