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Volumn 267, Issue 19, 2000, Pages 5891-5899
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Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2
a b a a a b c a,d a |
Author keywords
Activation domain; Calorimetry; Denaturation; Folding; Stability
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Indexed keywords
CARBOXYPEPTIDASE;
ENZYME PRECURSOR;
ARTICLE;
CALORIMETRY;
DIFFERENTIAL SCANNING CALORIMETRY;
ENZYME ACTIVATION;
HUMAN;
PRIORITY JOURNAL;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
THERMODYNAMICS;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
CALORIMETRY, DIFFERENTIAL SCANNING;
CARBOXYPEPTIDASES;
CIRCULAR DICHROISM;
COMPARATIVE STUDY;
ENZYME ACTIVATION;
ENZYME PRECURSORS;
HUMAN;
HYDROGEN-ION CONCENTRATION;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN RENATURATION;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
SUPPORT, NON-U.S. GOV'T;
THERMODYNAMICS;
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EID: 0033807148
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1432-1327.2000.01638.x Document Type: Article |
Times cited : (12)
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References (36)
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