Defining a length scale for millisecond-timescale protein conformational exchange

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

Volumn 110, Issue 28, 2013, Pages 11391-11396

  Sekhar, Ashok ^a,b   Vallurupalli, Pramodh ^a,b   Kaya, Lewis E ^a,b,c  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

CPMG NMR; Excited protein states; Hydrophobic hydration; Protein folding

Indexed keywords

AMINO ACID; WATER;

ARTICLE; HYDRODYNAMICS; HYDROGEN BOND; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE;

CPMG NMR; EXCITED PROTEIN STATES; HYDROPHOBIC HYDRATION; PROTEIN FOLDING;

MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEINS;

EID: 84879993654     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1303273110     Document Type: Article

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