An Investigation of the Conformational Changes of Histones F1 and F2a1 by Proton Magnetic Resonance Spectroscopy

作者：Miloslav Boublík, E. Morton Bradbury, Colyn Crane‐Robinson · 发表于：European Journal of Biochemistry · 年份：1970 · DOI：10.1111/j.1432-1033.1970.tb00315.x · 被引用次数：102 · 研究领域：Electron Spin Resonance Studies、Advanced NMR Techniques and Applications、DNA and Nucleic Acid Chemistry

High resolution nuclear magnetic resonance spectroscopy is used to study conformational changes in histone fractions F2a1 and F1 when the ionic strength of aqueous solutions is raised. Increasing line widths of certain resonance peaks, in particular those of apolar and aromatic amino acids, together with sequence data lead to the conclusion that the C‐terminal half of F2a1 and a central portion of F1 are involved in the conformational changes. The proportion of amino acid residues incorporated into secondary structure (as indicated by optical rotatory dispersion) is less than that involved in the conformational changes indicated by the nuclear magnetic resonance results. Intermolecular interactions are therefore postulated to explain this difference and these are specific in as much as they involve only a part of the histone molecule and include the regions of the chain having high potential for secondary structure formation.