TY - JOUR
T1 - A Nuclear‐Magnetic‐Resonance Study of the Globular Structure of the H5 Histone
AU - CHAPMAN, George E.
AU - AVILES, Francisco J.
AU - CRANE‐ROBINSON, Colyn
AU - BRADBURY, E. Morton
PY - 1978/1/1
Y1 - 1978/1/1
N2 - 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. Copyright © 1978, Wiley Blackwell. All rights reserved
AB - 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. Copyright © 1978, Wiley Blackwell. All rights reserved
UR - https://www.scopus.com/pages/publications/0018127241
U2 - 10.1111/j.1432-1033.1978.tb12602.x
DO - 10.1111/j.1432-1033.1978.tb12602.x
M3 - Article
SN - 0014-2956
VL - 90
SP - 287
EP - 296
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 2
ER -