Puigdoménech P, Daban J R, Palau J, Podo F, Guidoni L, Temussi P A
Biochim Biophys Acta. 1977 May 27;492(1):12-9. doi: 10.1016/0005-2795(77)90209-4.
The behaviour, upon variations in ionic strength, pH and temperature of 19F nuclear nuclear magnetic resonance signals of the trifluoroacetonylated derivative of histone H3 is compared with those of the H3-H4 complex and of the Hv fraction (an equimolar mixture of H2A, H2B, H3 and h4). The line width of the 19F-labelled histone H3 signals increases with ionic strength or pH, an effect consistent with aggregation of the protein. In the case of H3-H4 complex or Hv the line width decreases at intermediate ionic strengths (0.1-0.25 M NaCl). This effect is interpreted as the consequence of the formation of a well defined structure with ionic strength. At high salt concentrations the line width increases as a consequence of the final rigid quaternary structure or of the formation of higher aggregates.
将组蛋白H3的三氟乙酰化衍生物的19F核磁共振信号在离子强度、pH值和温度变化时的行为，与H3-H4复合物和Hv组分（H2A、H2B、H3和H4的等摩尔混合物）的行为进行了比较。19F标记的组蛋白H3信号的线宽随离子强度或pH值增加，这一效应与蛋白质的聚集一致。对于H3-H4复合物或Hv，在中等离子强度（0.1 - 0.25 M NaCl）下线宽减小。这种效应被解释为形成了具有离子强度的明确结构的结果。在高盐浓度下，由于最终的刚性四级结构或更高聚集体的形成，线宽增加。
