Development of Enzymatic Activity during Protein Folding - Wikidata - awgldk - TriplyDB

Development of Enzymatic Activity during Protein Folding

Development of Enzymatic Activity during Protein Folding

http://www.wikidata.org/entity/Q57957851

about

Integrating folding kinetics and protein function: biphasic kinetics and dual binding specificity in a WW domain.Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.

P2860

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P2860

Development of Enzymatic Activity during Protein Folding

http://www.wikidata.org/entity/Q57957851

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im Juli 1999 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в липні 1999

@uk

name

Development of Enzymatic Activity during Protein Folding

@en

Development of Enzymatic Activity during Protein Folding

@nl

type

label

Development of Enzymatic Activity during Protein Folding

@en

Development of Enzymatic Activity during Protein Folding

@nl

prefLabel

Development of Enzymatic Activity during Protein Folding

@en

Development of Enzymatic Activity during Protein Folding

@nl

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JBC.274.29.20151

P1433

Journal of Biological Chemistry

P1476

Development of enzymatic activ ...... iate of muscle acylphosphatase

@en

P2093

C M Dobson

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

F Chiti

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

G Ramponi

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

N A van Nuland

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

P2860

Crystal structure of common type acylphosphatase from bovine testis

Mapping the transition state and pathway of protein folding by protein engineering

From Levinthal to pathways to funnels

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.

The folding kinetics and thermodynamics of the Fyn-SH3 domain.

Slow folding of muscle acylphosphatase in the absence of intermediates.

Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues.

Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilization.

Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42, and Thr46.

P304

20151-20158

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

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scholarly article

P356

10.1074/JBC.274.29.20151

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P407

P433

29

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P478

274

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1999-07-01T00:00:00Z

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10400629

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P921

protein folding