X‐ray diffraction study of the interaction of the amino terminal half‐molecule of histone H4 with duplex DNA

E. J. Wachtel; R. Sperling

doi:10.1002/bip.360220143

X‐ray diffraction study of the interaction of the amino terminal half‐molecule of histone H4 with duplex DNA

E. J. Wachtel^*
, R. Sperling

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	333-339
Number of pages	7
Journal	Biopolymers
Volume	22
Issue number	1
DOIs	https://doi.org/10.1002/bip.360220143
State	Published - Jan 1983

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title = "X‐ray diffraction study of the interaction of the amino terminal half‐molecule of histone H4 with duplex DNA",

abstract = "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.",

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year = "1983",

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N2 - 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.

AB - 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.

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X‐ray diffraction study of the interaction of the amino terminal half‐molecule of histone H4 with duplex DNA

Abstract

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