Open AccessA Nuclear‐Magnetic‐Resonance Study of the Globular Structure of the H5 Histone
Author(s) -
CHAPMAN George E.,
AVILES Francisco J.,
CRANEROBINSON Colyn,
BRADBURY E. Morton
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12602.x
Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , histone h1 , spectroscopy , resonance (particle physics) , molecule , nuclear overhauser effect , crystallography , histone , globular cluster , stereochemistry , physics , atomic physics , biochemistry , dna , organic chemistry , quantum mechanics , galaxy
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.