Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding

Nature Structural Biology

Volumn 6, Issue 11, 1999, Pages 1005-1009

  Chiti, Fabrizio ^a   Taddei, Niccolo ^b   White, Paul M ^a   Bucciantini, Monica ^b   Magherini, Francesca ^b   Stefani, Massimo ^b   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPHOSPHATASE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; GENE MUTATION; KINETICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ACID ANHYDRIDE HYDROLASES; BINDING SITES; CARBOXYPEPTIDASES; CARBOXYPEPTIDASES A; ENZYME PRECURSORS; ENZYME STABILITY; HUMANS; KINETICS; MODELS, MOLECULAR; MUSCLES; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; THERMODYNAMICS;

EID: 0032708771     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/14890     Document Type: Article

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