Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains

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

Volumn 109, Issue 44, 2012, Pages 17795-17799

  Wensley, Beth G ^a   Kwa, Lee Gyan ^a   Shammas, Sarah L ^a   Rogers, Joseph M ^a   Browning, Stuart ^a   Yang, Ziqi ^a   Clarke, Jane ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Free energy landscape; Frustration; Phi value; Protein folding

Indexed keywords

GLUCOSE; SPECTRIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; ENERGY; FRICTION; GENE MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SURFACE PROPERTY; WILD TYPE;

AMINO ACID SEQUENCE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SPECTRIN;

EID: 84867092008     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201793109     Document Type: Article

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