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Volumn 39, Issue 46, 2000, Pages 14292-14304
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pH dependence of stability of staphylococcal nuclease: Evidence of substantial electrostatic interactions in the denatured state
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Author keywords
[No Author keywords available]
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Indexed keywords
NUCLEASE;
ARTICLE;
ENZYME CONFORMATION;
ENZYME DENATURATION;
ENZYME STABILITY;
ENZYME STRUCTURE;
MOLECULAR INTERACTION;
NONHUMAN;
PH;
PKA;
PRIORITY JOURNAL;
STAPHYLOCOCCUS;
THERMODYNAMICS;
ACIDS;
BINDING SITES;
ELECTROSTATICS;
ENZYME STABILITY;
GUANIDINE;
HYDROGEN-ION CONCENTRATION;
MICROCOCCAL NUCLEASE;
MODELS, CHEMICAL;
POTASSIUM CHLORIDE;
POTENTIOMETRY;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTONS;
SPECTROMETRY, FLUORESCENCE;
TEMPERATURE;
THERMODYNAMICS;
UREA;
BACTERIA (MICROORGANISMS);
STAPHYLOCOCCUS;
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EID: 0034700307
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi001015c Document Type: Article |
Times cited : (117)
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References (42)
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