Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan-synthase β chain

Protein Science

Volumn 6, Issue 12, 1997, Pages 2578-2588

  Gast, Klaus ^a   Chaffotte, Alain F ^b   Zirwer, Dietrich ^c   Guillou, Yvonne ^b   Mueller Frohne, Marlies ^a   Cadieux, Céline ^b   Hodges, Maria ^b   Damaschun, Gregor ^c   Goldberg, Michel E ^b  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b INSTITUT PASTEUR   (France)

^c HUMBOLDT UNIVERSITY   (Germany)

Author keywords

Collapse; Folding intermediate; Secondary structure; Solvent perturbations; Tryptophan synthase

Indexed keywords

BACTERIAL ENZYME; POLYPEPTIDE; SOLVENT; TRIFLUOROETHANOL; TRYPTOPHAN SYNTHASE;

ARTICLE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; COLLAPSE; ENVIRONMENTAL FACTOR; ENZYME SUBUNIT; ESCHERICHIA COLI; MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TEMPERATURE DEPENDENCE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0031452282     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061210     Document Type: Article

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