Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding

Proceedings of the National Academy of Sciences of the United States of America

Volumn 91, Issue 22, 1994, Pages 10422-10425

  Otzen, Daniel E ^a   Itzhaki, Laura S ^a   Elmasry, Nadia F ^a   Jackson, Sophie E ^a   Fersht, Alan R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

protein engineering

Indexed keywords

CHYMOTRYPSIN INHIBITOR;

ARTICLE; BARLEY; ENZYME CONFORMATION; ENZYME KINETICS; GENETIC ENGINEERING; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS;

CHYMOTRYPSIN; HORDEUM; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PLANT PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLUTIONS; SUPPORT, NON-U.S. GOV'T;

HORDEUM VULGARE SUBSP. VULGARE;

EID: 0027948175     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.91.22.10422     Document Type: Article

References (40)