The loss of tryptophan 194 in antichymotrypsin lowers the kinetic barrier to misfolding

FEBS Journal

Volumn 274, Issue 14, 2007, Pages 3622-3632

  Pearce, Mary C ^a   Cabrita, Lisa D ^a   Ellisdon, Andrew M ^a   Bottomley, Stephen P ^a  

^a MONASH UNIVERSITY   (Australia)

Author keywords

Antichymotrypsin; Protein aggregation; Protein misfolding; Serpin; Stability

Indexed keywords

CHYMOTRYPSIN; CHYMOTRYPSIN INHIBITOR; PHENYLALANINE; SERINE PROTEINASE INHIBITOR; TRYPTOPHAN;

ARTICLE; FLUORESCENCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN POLYMERIZATION; PROTEIN STABILITY; TRANSMISSION ELECTRON MICROSCOPY; WILD TYPE;

ALPHA 1-ANTITRYPSIN; CHYMOTRYPSIN; CRYSTALLOGRAPHY, X-RAY; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS; STRUCTURAL HOMOLOGY, PROTEIN; TRYPTOPHAN;

EID: 34447312857     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05897.x     Document Type: Article

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