Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion

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

Volumn 109, Issue 47, 2012, Pages 19268-19273

  Sekhar, Ashok ^a   Vallurupalli, Pramodh ^a   Kay, Lewis E ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

Compact states; Excited protein states; Nmr relaxation dispersion

Indexed keywords

GLYCEROL; POLYMER; PROTEIN; SOLVENT; WATER;

ARTICLE; FRICTION; HETERONUCLEAR SINGLE QUANTUM COHERENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; VISCOSITY;

DATABASES, PROTEIN; FRICTION; GLYCEROL; MOTION; MUTANT PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; THERMODYNAMICS; VISCOSITY; WATER;

EID: 84869764877     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212036109     Document Type: Article

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