Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications

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

Volumn 92, Issue 24, 1995, Pages 10869-10873

  Fersht, Alan R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

computer simulation; denatured state; evolution; fragments; intermediates

Indexed keywords

CHYMOTRYPSIN INHIBITOR;

ARTICLE; BARLEY; CHROMOSOME CONDENSATION; COMPUTER SIMULATION; PREDICTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

CHYMOTRYPSIN; COMPUTER SIMULATION; HORDEUM; KINETICS; PEPTIDES; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SERINE PROTEINASE INHIBITORS; THERMODYNAMICS;

HORDEUM VULGARE SUBSP. VULGARE;

EID: 0028856785     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.92.24.10869     Document Type: Article

References (66)