Conformational studies on modified proteins and peptides. Artificial myoglobins prepared with modified and metalloporphyrins.
Conformational studies on modified proteins and peptides. Artificial myoglobins prepared with modified and metalloporphyrins.
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修饰蛋白质和肽的构象研究。
DOI：
10.1021/bi00813a007
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发表时间：
1970
期刊：
影响因子：
2.9
通讯作者：
M. Atassi
中科院分区：
文献类型：
--
作者：
S. Andres;M. Atassi
人工肌红蛋白已制备与铜或锌金属卟啉或与血红素衍生物硝化的乙烯基侧链和它们的构象研究旋光色散和圆二色性和免疫化学方法。天然肌红蛋白（Mb）、Fe-Mb和Cu-Mb在233 µ的负最小值和199 µ的正最大值处显示出相同的旋转。这些衍生物在221和208 µ的负圆二色谱带处的约化摩尔椭圆率的测量结果与旋光度测量结果一致。这些结果表明，这三种衍生物具有相同的构象。另一方面，Nheme-Mb显示出小的构象变化，而Zn-Mb显示出明显程度的展开。因此，Zn-Mb和Nheme-Mb中螺旋结构的贡献低于天然肌红蛋白、Fe-Mb或Cu-Mb中的贡献。此外，研究变化
Artificial myoglobins have been prepared with Cu-or Zn-metalloporphyrins or with a heme derivative nitrated at the vinyl side chains and their conformations investigated by optical rotatory dispersion and circular dichroism and by immunochemical methods. Native myo-globin (Mb), Fe-Mb, and Cu-Mb exhibit identical rotations at the negative minima at 233 µ and at the positive maxima at 199 µ. Measurements of the reduced molar ellipticities of these derivatives at the negative circular dichroism bands at 221 and 208 µ were in agreement with optical rotation measurements. These results suggest that the three derivatives possess identical conformations. On the other hand, Nheme-Mb shows a small conformational change while Zn-Mb shows an appreciable degree of unfolding. A lower contribution of helical structure was, therefore, present in Zn-Mb and Nheme-Mb than thatfound in native myoglobin, Fe-Mb, or Cu-Mb. Furthermore, studies of the changes