Native state energetics of the Src SH2 domain: Evidence for a partially structured state in the denatured ensemble

Protein Science

Volumn 15, Issue 7, 2006, Pages 1769-1779

  Wildes, David ^a   Anderson, L Meadow ^a   Sabogal, Alex ^a   Marqusee, Susan ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Hydrogen exchange; Protein folding; Protein stability; Proteolysis; SH2 domain; Unfolded state

Indexed keywords

PROTEIN SH2;

ARTICLE; BEHAVIOR; DEUTERIUM HYDROGEN EXCHANGE; ENERGY TRANSFER; EQUILIBRIUM DIALYSIS; FLUORESCENCE ANALYSIS; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ANIMALS; CHICKENS; DEUTERIUM EXCHANGE MEASUREMENT; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN-TYROSINE KINASES; SPECTROMETRY, FLUORESCENCE; SRC HOMOLOGY DOMAINS; THERMODYNAMICS; TRYPTOPHAN; UREA;

EID: 33745684203     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062136006     Document Type: Article

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