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

Volumn 98, Issue 8, 2001, Pages 4349-4354

Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution

(6) Kazmirski, Steven L a,b Wong, Kam Bo a,b,c Freund, Stefan M V b Tan, Yee Joo b Fersht, Alan R b Daggett, Valerie a

a UNIVERSITY OF WASHINGTON (United States)

b UNIVERSITY OF CAMBRIDGE (United Kingdom)

c CHINESE UNIVERSITY OF HONG KONG (Hong Kong)

Author keywords

CI2; Conformational transitions; Molecular dynamics simulations; Nuclear magnetic resonance; Nucleation condensation

Indexed keywords

CHYMOTRYPSIN INHIBITOR;

ALPHA HELIX; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 0035836687 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.071054398 Document Type: Article

Times cited : (158)

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