Why and how does native topology dictate the folding speed of a protein?

Journal of Chemical Physics

Volumn 137, Issue 20, 2012, Pages

  Rustad, Mark ^a   Ghosh, Kingshuk ^a  

^a UNIVERSITY OF DENVER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONTACT ORDERS; CORRECTION TERMS; ENTROPY LOSS; FIRST ORDER; FIRST PRINCIPLE CALCULATIONS; FIT PARAMETERS; GAUSSIAN CHAINS; GAUSSIAN POLYMERS; HELICAL PROTEINS; METRIC COMBINING; MONOMERIC PROTEINS; MULTI-STATE; NATIVE TOPOLOGY; PERTURBATIVE CALCULATIONS; POLYMER PHYSICS; PROTEIN DATA BANK; PROTEIN FOLDING KINETICS; RANDOM SYSTEMS; SECOND ORDERS; SPEED DEPENDENCE; SPEED LIMIT; TOPOLOGICAL METRICS; TRANSITION STATE; TWO-STATE; UNIVERSAL MECHANISMS;

AMINO ACIDS; ARTIFICIAL INTELLIGENCE; ENTROPY; PROTEIN FOLDING; RNA; SEPARATION; SPEED; TOPOLOGY;

PROTEINS;

PROTEIN;

ARTICLE; BIOLOGICAL MODEL; CHEMISTRY; PROTEIN FOLDING; SURFACE PROPERTY; THERMODYNAMICS; TIME;

MODELS, BIOLOGICAL; PROTEIN FOLDING; PROTEINS; SURFACE PROPERTIES; THERMODYNAMICS; TIME FACTORS;

EID: 84870535360     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.4767567     Document Type: Article

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