Prediction of folding transition-state position (βT) of small, two-state proteins from local secondary structure content

Proteins: Structure, Function and Genetics

Volumn 68, Issue 1, 2007, Pages 218-222

  Huang, Ji Tao ^a,b   Cheng, Jin Pei ^a  

^a NANKAI UNIVERSITY   (China)

^b TIANJIN UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Content of helix; Local secondary structure content; Position of folding transition state on reaction pathway; Protein folding mechanism; Solvent accessibility of the transition states

Indexed keywords

PROLINE; PROTEIN;

ALPHA HELIX; ARTICLE; COMPUTER PROGRAM; COMPUTER SIMULATION; CONFORMATIONAL TRANSITION; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

COMPUTATIONAL BIOLOGY; DATABASES, PROTEIN; KINETICS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SOLVENTS;

EID: 34249904688     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21411     Document Type: Article

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