Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition

Biochemistry

Volumn 43, Issue 30, 2004, Pages 9834-9839

  Cabrita, Lisa D ^a   Dai, Weiwen ^a   Bottomley, Stephen P ^a  

^a MONASH UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ENZYMES; HYDROGEN BONDS; HYDROPHOBICITY; POLYMERIZATION; THERMODYNAMIC STABILITY;

CONFORMATIONAL CHANGES; HYDROPHOBIC RESIDUES; INACTIVE POLYMERS;

BIOCHEMISTRY;

POLYMER; PROTEINASE; SERINE PROTEINASE INHIBITOR;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; ENZYME INHIBITION; F HELIX; HYDROGEN BOND; HYDROPHOBICITY; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN POLYMERIZATION; PROTEIN STABILITY; STOICHIOMETRY; THERMODYNAMICS;

ALPHA 1-ANTITRYPSIN; HUMANS; ISOLEUCINE; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; POLYMERS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SERINE PROTEINASE INHIBITORS; SERPINS; THERMODYNAMICS; VALINE;

EID: 3342889562     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0491346     Document Type: Article

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