The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones

Protein Science

Volumn 20, Issue 12, 2011, Pages 2060-2073

  Topping, Traci B ^a   Gloss, Lisa M ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

Aggregation; Amyloid; Domain swapping; Oligomeric proteins; Protein folding intermediates

Indexed keywords

AMYLOID; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; HISTONE HMFB; HISTONE HPYA1; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; DIMERIZATION; ELECTRON MICROSCOPY; FIBRIL FORMATION; FLUORESCENCE ANALYSIS; INFRARED SPECTROSCOPY; KINETICS; MOLECULAR DYNAMICS; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STABILITY; ROOM TEMPERATURE; SOLUBILITY; STATIC ELECTRICITY; ULTRAVIOLET SPECTROSCOPY;

AMYLOID; ANIMALS; ARCHAEAL PROTEINS; HISTONES; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY; STATIC ELECTRICITY; XENOPUS LAEVIS;

ARCHAEA; EUKARYOTA;

EID: 81755162784     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.743     Document Type: Article

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