An investigation of the conformational and self-aggregational processes of histones using 1H and 13C nuclear magnetic resonance.
Histone self-aggregation processes have been studied by 13C and 1H nuclear magnetic resonance (NMR) as a function of ionic strength and protein concentration. Thus has led to a model involving apolar aggregation between structured regions of these molecules. This analysis supports the validity of the acquistion of conformational data on histones by the simulation of 13C NMR spectra at high concentration. Solution conformations for histones F2B and F3 are presented.
D000818:Animals; D002247:Carbon Isotopes; D002417:Cattle; D003201:Computers; D006657:Histones; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009994:Osmolar Concentration; D011487:Protein Conformation; D012965:Sodium Chloride; D013950:Thymus Gland
D002247:Carbon Isotopes; D006657:Histones; D012965:Sodium Chloride; D006859:Hydrogen