[Conformational peculiarity of H1 histones of calf thymus and sea urchin sperm].
The secondary structure, sizes and form of H1 histone molecules of calf thymus (H1-T) and sea urchin sperm (H1-S) were studied by circular dichroism, sedimentation and diffusion. An increase in the ionic strength of solution is shown to result in the formation of alpha-helical parts in H1-T and both alpha-helical and beta-structural parts of H1-S. An analysis of amino acid composition of histones and their compaction under these conditions enables a conclusion that the resulting B-structure is antiparallel and intramolecular. The above properties of H1-S can result in a more dense compactness of the sea urchin sperm chromatin.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006657:Histones / Q000302:isolation & purification; D008297:Male; D011487:Protein Conformation; D012617:Sea Urchins; D013094:Spermatozoa / Q000032:analysis*; D013950:Thymus Gland / Q000032:analysis*
D006657:Histones
Konformatsionnye osobennosti gistonov H1 iz timusa telenka i spermiev morskogo ezha.