title: The histone H1 globular region. A possible supersecondary structure from spectroscopic and statistical studies.
abstract: The central region of the basic nuclear protein, histone H1, has a highly conserved amino acid sequence and a globular structure which is still not known at atomic resolution. A possible secondary and supersecondary structure was predicted by combining experimental measurements of circular dichroism and NMR spectroscopy with a statistical method based on the amino acid sequence. Our results showed the protein fragment as being highly structured and having a total alpha-helix content of about 40%.
authors.affiliation: Institute of Biophysics, School of Medicine, University of Genova, Italy.
authors.forename: I
authors.initials: I
authors.lastname: Pepe
authors.forename: P
authors.initials: P
authors.lastname: Catasti
authors.forename: G
authors.initials: G
authors.lastname: Rauch
authors.forename: M
authors.initials: M
authors.lastname: Nizzari
authors.forename: C
authors.initials: C
authors.lastname: Nicolini
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006657:Histones / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D014357:Trypsin
chemical_list: D006657:Histones; D010446:Peptide Fragments; D014357:Trypsin