A Nuclear‐Magnetic‐Resonance Study of the Globular Structure of the H5 Histone

Authors:
Publisher website
Google Scholar
Abstract
The structure of the globular region of the chicken erythrocyte H5 histone was studied by 270 MHz proton NMR. The aromatic resonances were partially assigned by a combination of selective deuteration and iodination with the NMR spectroscopy. Detailed titration studies revealed interactions between residues in the structure. A technique involving measurement of small nuclear Overhauser effects permitted the assignment of 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 permitted a partial assignment of shifted methyl resonances. The histone H5 globular structure is apparently different from that of the homologous histone H1 molecule.

This publication has 16 references indexed in Scilit: