Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, Cl-2

Folding and Design

Volumn 1, Issue 1, 1996, Pages 43-55

  López Hernández, Eva ^a   Serrano, Luis ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Energy landscape; Folding kinetics; Folding pathway; Protein engineering; Protein folding; Protein thermodynamics

Indexed keywords

BACILLUS AMYLOLIQUEFACIENS RIBONUCLEASE; BACTERIAL PROTEIN; CHYMOTRYPSIN; CHYMOTRYPSIN INHIBITOR 2; MEMBRANE PROTEIN; METHYL ACCEPTING CHEMOTAXIS PROTEINS; METHYL-ACCEPTING CHEMOTAXIS PROTEINS; PEPTIDE; RIBONUCLEASE; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DRUG ANTAGONISM; ESCHERICHIA COLI; GENETICS; KINETICS; MOLECULAR GENETICS; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CHYMOTRYPSIN; ESCHERICHIA COLI; KINETICS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PLANT PROTEINS; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEASES; THERMODYNAMICS;

EID: 0030334834     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1359-0278(96)00011-9     Document Type: Article

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