The carboxyâterminal domain (residues 121â248) of sea urchin spermâspecific H1 is not random coil but partly alphaâhelical, even in 1 mM sodium phosphate, pH 7. The helix resides in a 57 residue prolineâfree segment which, in the intact histone, immediately abuts the central globular domain. The prolineâfree region, which is rich in lysine and alanine, is relatively resistant to tryptic digestion when the carboxyâterminal domain is bound to DNA. Two (overlapping) resistant peptides are shown by circular dichroism measurements to be substantially alphaâhelical in 1 mM sodium phosphate and to increase in helix content to approximately 70% in 1 M NaCLO4. Tryptic digestion of chromatin gives resistant fragments containing both the globular domain and the contiguous prolineâfree segment, strongly suggesting that the alphaâhelical segment also exists in chromatin, where it would be ideally placed to direct the path of the linker DNA entering or leaving the nucleosome. The linker in sea urchin sperm chromatin is long (approximately 74 bp), and the unusually long alphaâhelical segment in the carboxyâterminal tail of sperm H1 which has amphipathic character due to the alanine distribution, and is likely to be curved, may be a special feature tailored to organize it.