The oxidised histone octamer does not form a H3 disulphide bond

Histone H3 Glutathionylation in Proliferating Mammalian Cells Destabilizes Nucleosomal Structure

“…Wood et al proposed disulfide bond formation between two histone H3 molecules in oxidant conditions. However, crystal structure analyses did not show the existence of disulphide bounds between H3 histone in this situation (65). Similar results could be deduced after evaluation of H3 amounts (in monomer or dimer forms) in our GSNO experiments (Fig.…”

Bioorganic/inorganic hybrid composition of sponge spicules: Matrix of the giant spicules and of the comitalia of the deep sea hexactinellid Monorhaphis

“…These protein aggregates were analyzed by NaDodSO 4 -PAGE and found to be only slightly soluble in low-strength buffer. For the solubilization of the proteinaceous aggregates we used high concentration of the chaotropic agent urea (6 M), which disrupts the noncovalent forces; in addition, b-mercaptoethanol (10%) was used to cleave potential disulfide bonds (see e.g., Wood et al, 2006). Applying this procedure we succeeded to demonstrate that the proteinaceous matrix in the lamellar zone is a 27-kDa polypeptide.…”

A Study of Protein Secondary Structure Hydrogen Bonds under Oxidizing Conditions

“…The development of the oxidized histone octamer (GHO) and its unoxidized variant (HO) are detailed in previous work [15]. To investigate a reduction in the caxis parameter of the GHO as compared to the HO, the present work combines energy analysis of secondary structure hydrogen bonds with circular dichroism (CD) spectroscopy.…”