The folding transition state between SH3 domains is conformationally restricted and evolutionary conserved

Nature Structural Biology

Volumn 6, Issue 11, 1999, Pages 1010-1016

  Martinez, Jose C ^a,b   Serrano, Luis ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF GRANADA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN; PROTEIN TYROSINE KINASE;

AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; GENE MUTATION; GENETIC CONSERVATION; KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SPECTRIN; SRC HOMOLOGY DOMAINS; THERMODYNAMICS;

EID: 0032750509     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/14896     Document Type: Article

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