A K52Q substitution in the globular domain of histone H1t modulates its nucleosome binding properties

FEBS Letters

Volumn 580, Issue 25, 2006, Pages 5999-6006

  Ramesh, Sneha ^a   Bharath, M M Srinivas ^a   Chandra, Nagasuma R ^a   Rao, Manchanahalli R Satyanarayana ^a,b  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH   (India)

Author keywords

Globular domain; Histone H1t; Nucleosome binding property

Indexed keywords

AMINO ACID; CARBONYL DERIVATIVE; DNA; GLUTAMINE; HISTONE H1; LYSINE; METHIONINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA BINDING; HYDROGEN BOND; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PURIFICATION; RAT; STATISTICAL SIGNIFICANCE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; HISTONES; HYDROGEN BONDING; KINETICS; MALE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEOSOMES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TESTIS;

EID: 33750044116     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.09.061     Document Type: Article

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