A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome

Journal of Biological Chemistry

Volumn 279, Issue 23, 2004, Pages 24274-24282

  Park, Young Jun ^a   Dyer, Pamela N ^a   Tremethick, David J ^b   Luger, Karolin ^a  

^a Department of Environmental and Radiological Health Sciences   (United States)

^b Biology and Environment   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

DIMERS; DNA; ENERGY TRANSFER; ENZYMES; FLUORESCENCE; IONIC STRENGTH;

MACROMOLECULAR COMPLEXES; NUCLEOSOME STABILITY;

BIOCHEMISTRY;

DNA; HISTONE; HISTONE H2A; HISTONE H2AZ; HISTONE H2B; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DISSOCIATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; IONIC STRENGTH; MACROMOLECULE; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION;

ANIMALS; ANISOTROPY; CYSTAMINE; DIMERIZATION; DNA; DOSE-RESPONSE RELATIONSHIP, DRUG; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; HETEROCHROMATIN; HISTONES; IONS; KINETICS; MODELS, MOLECULAR; MUTATION; NUCLEOSOMES; PROTEIN FOLDING; SODIUM CHLORIDE; SPECTROMETRY, FLUORESCENCE; TYROSINE; XENOPUS LAEVIS;

EID: 2642515598     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M313152200     Document Type: Article

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