Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 49, 2009, Pages 20711-20716

  Wani, Ajazul Hamid ^a   Udgaonkar, Jayant B ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

Hydrogen exchange; Mass spectrometry; Native state exchange; Partially unfolded conformation; Protein unfolding

Indexed keywords

GUANIDINE; HYDROGEN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SH3;

ARTICLE; DENATURATION; ELECTROSPRAY MASS SPECTROMETRY; ENZYME STRUCTURE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING;

1-PHOSPHATIDYLINOSITOL 3-KINASE; DEUTERIUM; DEUTERIUM EXCHANGE MEASUREMENT; ENZYME STABILITY; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MASS SPECTROMETRY; MOLECULAR WEIGHT; PEPTIDES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SRC HOMOLOGY DOMAINS; THERMODYNAMICS;

EID: 73949098098     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0908617106     Document Type: Article

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