Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2

Journal of Molecular Biology

Volumn 269, Issue 4, 1997, Pages 611-622

  Tan, Yee Joo ^a,b   Oliveberg, Mikael ^a,c   Otzen, Daniel E ^a,d   Fersht, Alan R ^a  

^a MRC CENTRE FOR PROTEIN ENGINEERING   (United Kingdom)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c CHEMICAL CENTER   (Sweden)

^d NOVO NORDISK A S   (Denmark)

Author keywords

cis trans; Folding; Protein

Indexed keywords

CHYMOTRYPSIN INHIBITOR; PROLINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL BINDING; CONTROLLED STUDY; ISOMERISM; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; TEMPERATURE DEPENDENCE;

EID: 0031580205     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1043     Document Type: Article

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