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Volumn 41, Issue 24, 2002, Pages 7556-7564
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Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
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Author keywords
[No Author keywords available]
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Indexed keywords
THERMAL UNFOLDING;
AMINO ACIDS;
BACTERIA;
DIMERS;
HYDROGEN BONDS;
THERMODYNAMIC STABILITY;
X RAY SCATTERING;
BIOCHEMISTRY;
AMIDE;
AMINO ACID;
DIMER;
GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;
NICOTINAMIDE ADENINE DINUCLEOTIDE;
ARTICLE;
CONTROLLED STUDY;
DIFFERENTIAL SCANNING CALORIMETRY;
ENZYME ACTIVE SITE;
ENZYME BINDING;
ENZYME ISOLATION;
ENZYME STABILITY;
GEOBACILLUS STEAROTHERMOPHILUS;
HEAT TREATMENT;
HYDROGEN BOND;
MUTATION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN PHOSPHORYLATION;
PROTEIN PROTEIN INTERACTION;
RADIATION SCATTERING;
STEREOSPECIFICITY;
THERMAL ANALYSIS;
THERMOSTABILITY;
APOENZYMES;
BACILLUS STEAROTHERMOPHILUS;
CATALYTIC DOMAIN;
DIMERIZATION;
ENZYME STABILITY;
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (PHOSPHORYLATING);
HEAT;
HOLOENZYMES;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE FRAGMENTS;
PROTEIN DENATURATION;
PROTEIN FOLDING;
RECOMBINANT PROTEINS;
BACTERIA (MICROORGANISMS);
GEOBACILLUS STEAROTHERMOPHILUS;
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EID: 0037129983
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi012084+ Document Type: Article |
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Times cited : (12)
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References (25)
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