Abstract
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 alpha helix, beta 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 alpha-helical sections, the first from residues 55 to 67 and the second of about 12 residues in the region between residues 70 to 90. beta-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.
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