Open AccessThe Location of Secondary Structure in Histone H4
Author(s) -
CRANEROBINSON Colyn,
HAYASHI Hiroaki,
CARY Peter D.,
BRIAND Gilbert,
SAUTIÈRE Pierre,
KRIEGER David,
VIDALI Giorgio,
LEWIS Peter N.,
TOMKUN Jean
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11838.x
Subject(s) - chemistry , histone , protein secondary structure , molecule , histone h1 , crystallography , peptide , helix (gastropod) , stereochemistry , biophysics , nuclear magnetic resonance , biochemistry , biology , physics , ecology , organic chemistry , snail , gene
A total of eight peptides cleaved from calf thymus histone H4 have been studied at several ionic strengths by circular dichroic, infrared and nuclear magnetic resonance spectroscopies to follow the formation of α helix, β structure and self‐aggregates. The results are compared with data obtained previously on three other peptides and on the intact molecule in order to define the location of secondary structure in histone H4. It is concluded that there are two α‐helical sections, the first from residues 55 to 67 and the second of about 12 residues in the region between residues 70 and 90. β‐Structure formation takes place only in the C‐terminal part of the intact H4 molecule. Nuclear magnetic resonance studies of the peptides prove that it is the basic N‐terminal regions of histone H4 that remain free when the molecule self‐aggregates.