The prosegment catalyzes pepsin folding to a kinetically trapped native state

Biochemistry

Volumn 49, Issue 2, 2010, Pages 365-371

  Dee, Derek R ^a   Yada, Rickey Y ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PEPTIDASE; COMMON FEATURES; DENATURED STATE; DENATURING CONDITIONS; ENERGY LANDSCAPE; FOLDING TRANSITION STATE; FREE-ENERGY DIFFERENCE; IRREVERSIBLE DENATURATION; KINETIC BARRIER; META-STABLE STATE; NATIVE CONFORMATION; NATIVE STATE; PROTEIN DESIGN; PROTEIN UNFOLDING; THERMODYNAMICALLY STABLE; TRAPPED STATE;

ACTIVATION ENERGY; DENATURATION; FREE ENERGY; PROTEINS;

BIOLOGICAL MATERIALS;

ENZYME PRECURSOR; PEPSIN A; PEPTIDASE; PEPSINOGEN; PEPTIDE FRAGMENT;

ARTICLE; CATALYSIS; COMPARATIVE STUDY; CONFORMATION; ENERGY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STRUCTURE; KINETICS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; THERMODYNAMICS; AMINO ACID SEQUENCE; CALORIMETRY; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; METABOLISM; MOLECULAR GENETICS; PROTEIN DENATURATION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CALORIMETRY; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPSIN A; PEPSINOGEN A; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 75349090412     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9014055     Document Type: Article

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