Correlation of binding-loop internal dynamics with stability and function in potato I inhibitor family: Relative contributions of Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V as studied by site-directed mutagenesis and NMR spectroscopy

Biochemistry

Volumn 41, Issue 30, 2002, Pages 9572-9579

  Cai, Mengli ^a,b   Gong, Yu Xi ^a   Wen, Lisa ^c   Krishnamoorthi, Ramaswamy ^a  

^a KANSAS STATE UNIVERSITY   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c WESTERN ILLINOIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING-LOOP FLEXIBILITY;

AMINO ACIDS; FREE ENERGY; HYDROGEN BONDS; HYDROLYSIS; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; PLANTS (BOTANY);

PROTEINS;

ARGININE; HYDROGEN; NITROGEN; TRYPSIN INHIBITOR;

ARTICLE; HYDROGEN BOND; KINETICS; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE; REACTION ANALYSIS; RELAXATION TIME; SITE DIRECTED MUTAGENESIS; SQUASH; THREE DIMENSIONAL IMAGING;

ARGININE; CATALYSIS; CUCURBITA; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; TRYPSIN; TRYPSIN INHIBITORS;

CUCURBITA; CUCURBITA MAXIMA; SOLANUM TUBEROSUM;

EID: 0037199462     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0258952     Document Type: Article

References (35)