Identification of residual structure within denatured antichymotrypsin: Implications for serpin folding and misfolding

Biochemical and Biophysical Research Communications

Volumn 324, Issue 2, 2004, Pages 729-735

  Pearce, Mary C ^a   Cabrita, Lisa D ^a   Rubin, Harvey ^b   Gore, Michael G ^c   Bottomley, Stephen P ^a  

^a MONASH UNIVERSITY   (Australia)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

Aggregation; Antichymotrypsin; Antitrypsin; Conformational disease; Protein folding; Protein misfolding; Residual structure; Serpin

Indexed keywords

CHYMOTRYPSIN INHIBITOR; GUANIDINE; GUANIDINE THIOCYANATE; SERINE PROTEINASE INHIBITOR; THIOCYANIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONCENTRATION RESPONSE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; THERMODYNAMICS;

EID: 5144224143     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.105     Document Type: Article

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