Chapman G E, Aviles F J, Crane-Robinson C, Bradbury E M
Eur J Biochem. 1978 Oct;90(2):287-96. doi: 10.1111/j.1432-1033.1978.tb12602.x.
The structure of the globular region of the chicken erythrocyte H5 histone has been studied by 270-MHz proton magnetic resonance. The aromatic resonances have been partially assigned by a combination of selective deuteration and iodination with the nuclear magnetic resonance spectroscopy. Detailed titration studies have revealed interactions between residues in the structure. A technique involving the measurement of small nuclear Overhauser effects has enabled the assignment of the aromatic residues causing the perturbation of the ring-current-shifted methyl resonances occurring in the upfield region of the spectrum. Spin-decoupling experiments on these peaks has enabled a partial assignment of shifted methyl resonances. The results support the notion that the histone H5 globular structure is different from that of the homologous histone H1 molecule.
利用270兆赫质子磁共振研究了鸡红细胞H5组蛋白球状区域的结构。通过选择性氘代和碘化结合核磁共振光谱法，已部分确定了芳香族共振峰。详细的滴定研究揭示了该结构中残基之间的相互作用。一种涉及测量小核Overhauser效应的技术，已能够确定导致光谱高场区域出现环电流位移甲基共振峰发生扰动的芳香族残基。对这些峰进行的自旋去耦实验，已能够部分确定位移甲基共振峰。结果支持了组蛋白H5球状结构不同于同源组蛋白H1分子结构这一观点。
