Crane-Robinson C, Hayashi H, Cary P D, Briand G, Sautière P, Krieger D, Vidali G, Lewis P N, Tom-Kun J
Eur J Biochem. 1977 Oct 3;79(2):535-48. doi: 10.1111/j.1432-1033.1977.tb11838.x.
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.
通过圆二色光谱、红外光谱和核磁共振光谱，在几种离子强度下对从小牛胸腺组蛋白H4切割得到的总共八条肽段进行了研究，以追踪α螺旋、β结构和自聚集体的形成。将结果与先前在其他三条肽段以及完整分子上获得的数据进行比较，以确定组蛋白H4中二级结构的位置。得出的结论是，有两个α螺旋区，第一个从第55位残基到第67位残基，第二个在第70位残基到第90位残基之间约12个残基的区域。β结构仅在完整H4分子的C端部分形成。对这些肽段的核磁共振研究证明，当分子自聚集时，组蛋白H4的碱性N端区域仍保持游离状态。
