A residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical φ{symbol}-value

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 5, 2012, Pages 1343-1349

  Zarrine Afsar, Arash ^a   Dahesh, Samira ^a   Davidson, Alan R ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

value analysis; bulge; Folding transition state; Local structure propensity; Non native interaction

Indexed keywords

MUTANT PROTEIN; PROTEIN KINASE FYN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; CANONICAL PHI VALUE; CHEMICAL PARAMETERS; CONTROLLED STUDY; ENZYME STABILITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN UNFOLDING; WILD TYPE;

KINETICS; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; PROTO-ONCOGENE PROTEINS C-FYN; SRC HOMOLOGY DOMAINS; THERMODYNAMICS;

EID: 84859444101     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24030     Document Type: Article

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