The H2A.Z/H2B dimer is unstable compared to the dimer containing the major H2A isoform

Protein Science

Volumn 14, Issue 2, 2005, Pages 514-522

  Placek, Brandon J ^a   Nicole Harrison, L ^a   Villers, Brooke M ^a   Gloss, Lisa M ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

Chemical denaturation; Circular dichroism; Fluorescence; Histone variant; Thermodynamics

Indexed keywords

DIMER; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; ISOPROTEIN; TETRAMER; TRIMETHYLAMINE OXIDE; TYROSINE; UREA;

ANISOTROPY; ARTICLE; BIOPHYSICS; CHROMATIN; CIRCULAR DICHROISM; DNA REPLICATION; DNA TRANSCRIPTION; ENERGY; EQUILIBRIUM CONSTANT; FLUORESCENCE; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN VARIANT; THERMODYNAMICS;

ANIMALS; ANISOTROPY; CIRCULAR DICHROISM; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; HISTONES; MACROMOLECULAR SUBSTANCES; MICE; NUCLEOSOMES; PROMOTER REGIONS (GENETICS); PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; RECOMBINANT PROTEINS; THERMODYNAMICS; TIME FACTORS; UREA; XENOPUS LAEVIS;

EUKARYOTA;

EID: 13244256813     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041026405     Document Type: Article

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