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ABSTRACT On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the
central domain (∼80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the
flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule. Access through your institution Buy or subscribe This is a preview of
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ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS MULTIFUNCTIONAL HISTONE
VARIANTS IN GENOME FUNCTION Article 13 August 2024 HISTONES AND HISTONE VARIANT FAMILIES IN PROKARYOTES Article Open access 11 September 2024 ACETYL-METHYLLYSINE MARKS CHROMATIN AT ACTIVE
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Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Biophysics Laboratories, King's College, London, WC2B 5RL, UK J. Allan * Biophysics Laboratories, Portsmouth
Polytechnic, Portsmouth, PO1 2QQ, UK P. G. Hartman & C. Crane-Robinson * Department of Biochemistry, Autonomous University, Barcelona, Spain F. X. Aviles Authors * J. Allan View author
publications You can also search for this author inPubMed Google Scholar * P. G. Hartman View author publications You can also search for this author inPubMed Google Scholar * C.
Crane-Robinson View author publications You can also search for this author inPubMed Google Scholar * F. X. Aviles View author publications You can also search for this author inPubMed
Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Allan, J., Hartman, P., Crane-Robinson, C. _et al._ The structure of histone H1 and its
location in chromatin. _Nature_ 288, 675–679 (1980). https://doi.org/10.1038/288675a0 Download citation * Received: 17 July 1980 * Accepted: 08 October 1980 * Issue Date: 18 December 1980 *
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