Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway

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

Volumn 94, Issue 25, 1997, Pages 13409-13413

  Bond, Chris J ^b   Wong, Kam Bo ^b   Clarke, Jane ^a   Fersht, Alan R ^a,c   Daggett, Valerie ^b  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

^b UNIVERSITY OF WASHINGTON   (United States)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Molecular dynamics; NMR; Protein folding

Indexed keywords

ENZYME; RIBONUCLEASE;

ALPHA HELIX; ARTICLE; BACILLUS AMYLOLIQUEFACIENS; ENZYME DENATURATION; ENZYME STRUCTURE; HYDROPHOBICITY; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING;

AMINO ACID SEQUENCE; ELECTROSTATICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEASES; TEMPERATURE; THERMODYNAMICS;

BACILLUS AMYLOLIQUEFACIENS;

EID: 0031472252     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.25.13409     Document Type: Article

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