Zarbock J, Clore G M, Gronenborn A M
Proc Natl Acad Sci U S A. 1986 Oct;83(20):7628-32. doi: 10.1073/pnas.83.20.7628.
A 1H NMR study of the 79-residue globular domain of chicken erythrocyte histone H5 (GH5) is presented. Using a combination of two-dimensional NMR techniques to demonstrate through-bond and through-space (less than 5 A) connectivities, the resonances of GH5 are assigned in a sequential manner. From a qualitative interpretation of the short-range nuclear Overhauser effects (NOEs) involving the NH and C alpha H protons, it is shown that GH5 has four alpha-helices. The approximate spatial relationship of three of these four helices relative to each other is deduced from the observation of a number of long-range NOEs. The peptide chain outside the helices appears to have little regular secondary structure and no NOEs characteristic of beta-sheets are apparent.
本文介绍了对鸡红细胞组蛋白H5(GH5)79个残基球状结构域的1H NMR研究。通过结合二维NMR技术来证明键间和空间(小于5埃)连接性,以序列方式对GH5的共振进行了归属。通过对涉及NH和CαH质子的短程核Overhauser效应(NOE)的定性解释,表明GH5有四个α螺旋。从一些长程NOE的观察中推断出这四个螺旋中三个彼此之间的近似空间关系。螺旋外的肽链似乎几乎没有规则的二级结构,也没有明显的β折叠特征的NOE。