Nuclear magnetic resonance studies of histone IV solution conformation.
The 220-MHz high-resolution proton magnetic resonance (PMR) spectrum of histone IV has been examined as a function of histone concentration, salt concentration, and pD. The hydrophobic C-terminal portion of the histone IV monomer appears to be largely PMR "invisible" indicating that this region of the polypeptide contains rigid secondary structure. Further loss of PMR resonance areas with increased histone IV concentration in neat D2O has been attributed to self-aggregation involving a monomer-dimer equilibrium. An equilibrium between the monomer and large aggregates, on the other hand, appears to dominate at NaCl concentrations above 0.01 M. pD studies reveal an abrupt increase in histone IV aggregation at pD smaller than 0.8 and precipitation of histone IV at pD values in the neighborhood of its isoelectric point, pD similar to 11.
D000818:Animals; D002417:Cattle; D003903:Deuterium; D006657:Histones; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D009994:Osmolar Concentration; D011487:Protein Conformation; D011522:Protons; D012965:Sodium Chloride; D012996:Solutions; D013950:Thymus Gland / Q000032:analysis
D006657:Histones; D011522:Protons; D012996:Solutions; D012965:Sodium Chloride; D003903:Deuterium