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Volumn 40, Issue 43, 2001, Pages 13114-13123
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Thermodynamic studies of the core histones: Stability of the octamer subunits is not altered by removal of their terminal Domains
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Author keywords
[No Author keywords available]
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Indexed keywords
CORE HISTONES;
DIFFERENTIAL SCANNING CALORIMETRY;
DIMERS;
ENTHALPY;
IONIC STRENGTH;
MONOMERS;
PH EFFECTS;
PROTEINS;
SPECTROSCOPIC ANALYSIS;
THERMODYNAMIC STABILITY;
BIOCHEMISTRY;
HISTONE;
ANIMAL CELL;
ARTICLE;
CHICKEN;
CIRCULAR DICHROISM;
ENTHALPY;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DENATURATION;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN STABILITY;
THERMODYNAMICS;
ANIMALS;
CALORIMETRY, DIFFERENTIAL SCANNING;
CIRCULAR DICHROISM;
DIMERIZATION;
DOSE-RESPONSE RELATIONSHIP, DRUG;
HISTONES;
HYDROGEN-ION CONCENTRATION;
KINETICS;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
SALTS;
SODIUM CHLORIDE;
TEMPERATURE;
THERMODYNAMICS;
TRYPSIN;
ULTRAVIOLET RAYS;
UREA;
ANIMALIA;
GALLUS GALLUS;
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EID: 0035980285
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0110140 Document Type: Article |
Times cited : (27)
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References (70)
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