Dramatic stabilization of an SH3 domain by a single substitution: Roles of the folded and unfolded states

Journal of Molecular Biology

Volumn 307, Issue 3, 2001, Pages 913-928

  Mok, Yu Keung ^a,b   Elisseeva, Elena L ^a,b   Davidson, Alan R ^c   Forman Kay, Julie D ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Folding kinetics; Non native residual structure; Protein stability; SH3 domain; Unfolded state structure

Indexed keywords

PROTEIN; PROTEIN DRK; THREONINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CORRELATION FUNCTION; DROSOPHILA; ELECTRICITY; KINETICS; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THERMODYNAMICS; ULTRAVIOLET SPECTROSCOPY;

EID: 0035970299     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4521     Document Type: Article

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