The N tails of histones H3 and H4 adopt a highly structured conformation in the nucleosome 1 1Edited by T. Richmond
- 1 October 1997
- journal article
- editorial
- Published by Elsevier in Journal of Molecular Biology
- Vol. 273 (3) , 503-508
- https://doi.org/10.1006/jmbi.1997.1297
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The distribution of α‐helix propensity along the polypeptide chain is not conserved in proteins from the same familyProtein Science, 1995
- Evidence Indicating Proximity in the Nucleosome Between the Histone H4 N Termini and the Globular Domain of Histone H1Journal of Molecular Biology, 1994
- Protein Secondary Structure from Circular Dichroism Spectroscopy Combining Variable Selection Principle and Cluster Analysis with Neural Network, Ridge Regression and Self-consistent MethodsJournal of Molecular Biology, 1994
- Poly(Pro)II Helixes in Globular Proteins: Identification and Circular Dichroic AnalysisBiochemistry, 1994
- Use of selectively trypsinized nucleosome core particles to analyze the role of the histone “tails” in the stabilization of the nucleosomeJournal of Molecular Biology, 1989
- Chromatin core particle obtained by selective cleavage of histories H3 and H4 by clostripainJournal of Molecular Biology, 1988
- Structure of the nucleosome core particle at 7 Å resolutionNature, 1984
- High‐Resolution Proton‐Magnetic‐Resonance Studies of Chromatin Core ParticlesEuropean Journal of Biochemistry, 1978
- Kinetic analysis of deoxyribonuclease I cleavages in the nucleosome core: Evidence for a DNA superhelixJournal of Molecular Biology, 1978
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969