A K52Q substitution in the globular domain of histone H1t modulates its nucleosome binding properties.
Ramesh, Sneha
A K52Q substitution in the globular domain of histone H1t modulates its nucleosome binding properties. [electronic resource] - FEBS letters Oct 2006 - 5999-6006 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-5793
10.1016/j.febslet.2006.09.061 doi
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites--genetics
Histones--chemistry
Hydrogen Bonding
In Vitro Techniques
Kinetics
Male
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Nucleosomes--metabolism
Protein Binding
Protein Structure, Tertiary
Rats
Recombinant Proteins--chemistry
Sequence Homology, Amino Acid
Testis--metabolism
A K52Q substitution in the globular domain of histone H1t modulates its nucleosome binding properties. [electronic resource] - FEBS letters Oct 2006 - 5999-6006 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-5793
10.1016/j.febslet.2006.09.061 doi
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites--genetics
Histones--chemistry
Hydrogen Bonding
In Vitro Techniques
Kinetics
Male
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Nucleosomes--metabolism
Protein Binding
Protein Structure, Tertiary
Rats
Recombinant Proteins--chemistry
Sequence Homology, Amino Acid
Testis--metabolism