1. Structural Studies of Chicken Erythrocyte Histone H5
- Author
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Madeleine Champagne, Anne-Marie Kovacs, S E Danby, Michel Daune, Annie Garel, E. Morton Bradbury, and Colyn Crane-Robinson
- Subjects
Protein Denaturation ,Circular dichroism ,Erythrocytes ,Magnetic Resonance Spectroscopy ,Spectrophotometry, Infrared ,Protein Conformation ,Chemistry ,Circular Dichroism ,Osmolar Concentration ,Temperature ,Beta sheet ,Nuclear magnetic resonance spectroscopy ,Biochemistry ,Peptide Fragments ,Histones ,Crystallography ,Protein structure ,Histone H1 ,Animals ,Histone octamer ,Globular Region ,Alpha helix - Abstract
Spectroscopic studies (nuclear magnetic resonance, circular dichroism and infrared) have been carried out on chicken erythrocyte histone H5 and on three peptides cleaved therefrom: 1-31, 32-197 and 58-197. It is shown that at ionic strengths above o.1M part of the H5 molecule takes up a globular conformation containing 14% alpha helix but no beta sheet structure. Several details of the circular dichroism and nuclear magnetic resonace spectra indicate that the globular region is located in the N-terminal half of the molecule and this proposal is supported by the observation that the peptide 32-197 is largely incapable of folding and the peptide 59-197 is completely incapable of folding. Structural similarities and differences between histone H5 and histone H1 are discussed.
- Published
- 1976
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