Energy landscapes of functional proteins are inherently risky

Nature Chemical Biology

Volumn 10, Issue 11, 2014, Pages 884-891

  Gershenson, Anne ^a   Gierasch, Lila M ^a   Pastore, Annalisa ^b   Radford, Sheena E ^c  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

^b KING'S COLLEGE LONDON   (United Kingdom)

^c UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 3; SERINE PROTEINASE INHIBITOR; PROTEIN;

CONFORMATIONAL TRANSITION; COVALENT BOND; ENERGY; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR EVOLUTION; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEPLETION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; REVIEW; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PROTEINOSIS; THERMODYNAMICS;

HUMANS; MODELS, MOLECULAR; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; THERMODYNAMICS;

EID: 84924293849     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/NCHEMBIO.1670     Document Type: Review

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