AN INVESTIGATION OF CONFORMATIONAL CHANGES OF HISTONES F1 AND F2A1 BY PROTON MAGNETIC RESONANCE SPECTROSCOPY
AN INVESTIGATION OF CONFORMATIONAL CHANGES OF HISTONES F1 AND F2A1 BY PROTON MAGNETIC RESONANCE SPECTROSCOPY
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DOI：
10.1111/j.1432-1033.1970.tb00315.x
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发表时间：
1970-01-01
期刊：
影响因子：
--
通讯作者：
CRANEROB.C
中科院分区：
文献类型：
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作者：
BOUBLIK, M;BRADBURY, EM;CRANEROB.C
利用高分辨核磁共振波谱研究了组蛋白组分F2a1和F1在水溶液离子强度升高时的构象变化。某些共振峰的线宽增加，特别是非极性和芳香族氨基酸的共振峰，以及序列数据导致F2a1的C末端一半和F1的中心部分参与构象变化的结论。纳入二级结构的氨基酸残基的比例（如旋光色散所示）小于核磁共振结果所示的构象变化所涉及的比例。因此，假设分子间相互作用来解释这种差异，并且这些相互作用是特异性的，因为它们仅涉及组蛋白分子的一部分，并且包括具有二级结构形成的高潜力的链区域。
High resolution nuclear magnetic resonance spectroscopy is used to study conformational changes in histone fractions F2a1and 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 F2a1and 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.