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X‐ray diffraction study of the interaction of the amino terminal half‐molecule of histone H4 with duplex DNA
Author(s) -
Wachtel E. J.,
Sperling R.
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220143
Subject(s) - chemistry , fiber diffraction , dna , molecule , crystallography , diffraction , histone , peptide , histone h4 , duplex (building) , stereochemistry , x ray crystallography , biochemistry , optics , physics , organic chemistry
The interaction of the amino terminal half‐molecule of histone H4 with duplex DNA has been studied by fiber x‐ray diffraction. Changes induced in the diffraction pattern of B‐DNA by the presence of the bound peptide have been Fourier‐analyzed and the results presented in terms of a deweighted radial projection of the electron density. We conclude that the peptide binds on the major groove side of the sugar–phosphate chain.