Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer

European Journal of Biochemistry

Volumn 271, Issue 18, 2004, Pages 3794-3803

  Konno, Michiko ^a   Sano, Yumi ^a   Okudaira, Kayoko ^a   Kawaguchi, Yoko ^a   Yamagishi Ohmori, Yoko ^a   Fushinobu, Shinya ^b   Matsuzawa, Hiroshi ^b  

^a OCHANOMIZU UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

Cyclophilin; Isozyme; Peptide binding; Peptidyl prolyl cis trans isomerase; Refolding

Indexed keywords

ALANINE; AMIDE; ARGININE; CYCLOPHILIN A; CYCLOPHILIN B; HISTIDINE; NITROGEN; PEPTIDE; PROLINE;

AMINO ACID SEQUENCE; ARTICLE; ATOM; CIS ISOMER; CONTROLLED STUDY; ESCHERICHIA COLI; HYDROGEN BOND; ISOMER; ISOMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON TRANSPORT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CRYSTALLIZATION; CYCLOPHILINS; ESCHERICHIA COLI; HYDROGEN BONDING; ISOMERISM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PEPTIDYLPROLYL ISOMERASE; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; THREONINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 4544282646     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04321.x     Document Type: Article

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