A simple measure of native-state topology and chain connectivity predicts the folding rates of two-state proteins with and without crosslinks

Proteins: Structure, Function and Genetics

Volumn 64, Issue 1, 2006, Pages 193-197

  Dixit, Purushottam D ^a,b   Weikl, Thomas R ^a  

^a MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

^b INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Disulfide bonds; Effective contact order; Loop closure entropy; Protein folding kinetics

Indexed keywords

ARTICLE; CORRELATION COEFFICIENT; CROSS LINKING; DISULFIDE BOND; ENTROPY; KINETICS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STRUCTURE;

CARBON MONOXIDE; CROSS-LINKING REAGENTS; DATABASES, PROTEIN; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS;

EID: 33744832626     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20976     Document Type: Article

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