The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state

Protein Science

Volumn 18, Issue 3, 2009, Pages 526-536

  Lin, Sung Lun ^a   Zarrine Afsar, Arash ^a   Davidson, Alan R ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

value analysis; Folding kinetics; Folding transition state; Osmolyte induced stability; Osmolytes; Protein stability; SH3 domains; Trimethylamine N oxide

Indexed keywords

MUTANT PROTEIN; PROTEIN KINASE FYN; TRIMETHYLAMINE OXIDE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENERGY TRANSFER; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; MELTING POINT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; GUANIDINE; KINETICS; METHYLAMINES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTO-ONCOGENE PROTEINS C-FYN; SRC HOMOLOGY DOMAINS; TEMPERATURE; THERMODYNAMICS;

EID: 61449176137     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.52     Document Type: Article

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