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Volumn 273, Issue 29, 1998, Pages 18052-18059
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Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions
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Author keywords
[No Author keywords available]
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Indexed keywords
TYROSINE TRANSFER RNA LIGASE;
ARTICLE;
CIRCULAR DICHROISM;
ENZYME ANALYSIS;
ENZYME STRUCTURE;
GEL PERMEATION CHROMATOGRAPHY;
GEOBACILLUS STEAROTHERMOPHILUS;
NONHUMAN;
PARTITION COEFFICIENT;
PRIORITY JOURNAL;
PROTEIN FOLDING;
SPECTROFLUOROMETRY;
STEADY STATE;
BACILLUS STEAROTHERMOPHILUS;
CHROMATOGRAPHY, GEL;
CIRCULAR DICHROISM;
DIMERIZATION;
DIPHOSPHATES;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
SPECTROMETRY, FLUORESCENCE;
THERMODYNAMICS;
TYROSINE-TRNA LIGASE;
UREA;
BACTERIA (MICROORGANISMS);
GEOBACILLUS STEAROTHERMOPHILUS;
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EID: 0000022693
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.273.29.18052 Document Type: Article |
Times cited : (43)
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References (35)
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