Conformation of the primary binding loop folded through an intramolecular interaction contributes to the strong chymotrypsin inhibitory activity of the chymotrypsin inhibitor from Erythrina variegata seeds

Journal of Biochemistry

Volumn 126, Issue 1, 1999, Pages 162-167

  Iwanaga, Shiroh ^a   Nagata, Ruby ^a   Miyamoto, Atsushi ^a   Kouzuma, Yoshiaki ^a   Yamasaki, Nobuyuki ^a   Kimura, Makoto ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

Chymotrypsin inhibitor; Erythrina variegata; Kunitz family proteinase inhibitor; Primary binding loop; Scaffold

Indexed keywords

ALANINE; AMINO ACID; APROTININ; CHIMERIC PROTEIN; CHYMOTRYPSIN; CHYMOTRYPSIN INHIBITOR;

AMINO ACID SUBSTITUTION; ARTICLE; ASSOCIATION; CHIMERA; DISSOCIATION CONSTANT; ERYTHRINA; NONHUMAN; PLANT SEED; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SURFACE PLASMON RESONANCE;

ERYTHRINA VARIEGATA;

EID: 0032820530     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022417     Document Type: Article

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