Enhanced sensitivity to conformation in various proteins. Vibrational circular dichroism results.
Enhanced sensitivity to conformation in various proteins. Vibrational circular dichroism results.
复制标题
对各种蛋白质构象的敏感性增强。
DOI：
10.1021/bi00440a031
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发表时间：
1989
期刊：
影响因子：
2.9
通讯作者：
Keiderling,TA
中科院分区：
文献类型：
--
作者：
Pancoska,P;Yasui,SC;Keiderling,TA
伊利诺伊大学芝加哥分校化学系，Box 4348，芝加哥，伊利诺伊州60680接收于1988年12月21日;修订的Mandarin pt接收于1989年3月7日摘要：介绍了几种溶于D20的球状蛋白质的振动圆二色性（VCD）光谱，并与传统的UV-CD结果进行了比较。可以看出，对于Levitt和Chothia [（1976）Nature 261，552]的、λ和α + λ类别，VCD证明了比UV-CD大得多的带形变化，包括符号改变。在模型多肽中发现的-螺旋的VCD和肌红蛋白的酰胺V VCD之间可以看到直接的平行。由于蛋白质的所有结构方面对VCD的贡献大致相等，胰凝乳蛋白酶酰胺V VCD与0-折叠模型的类似相关性并不清楚。此外，“随机卷曲”型蛋白质的VCD被发现与“随机卷曲”多肽的VCD结果明显相关。最后，模拟假设预期的VCD蛋白质结构具有构象之间的限制性情况下讨论。
Department of Chemistry, University of Illinois at Chicago, Box 4348, Chicago, Illinois 60680 Received December 21, 1988; Revised Manuscript Received March 7, 1989 abstract: Vibrational circular dichroism (VCD) spectra of several globular proteinsdissolved in D20 are presented and compared to conventional UV-CD results. It can be seen that, for the, ß, and a+ ß categories of Levitt and Chothia [(1976) Nature 261, 552], VCD evidences much larger band shape variations, including sign alteration, than does UV-CD. A direct parallel is seen between the VCD of the-helix found in model polypeptides and the amide V VCD of myoglobin. Since allstructural aspects of the protein contribute to the VCD on a roughly equal footing, a similar correlation of the chymotrypsin amide V VCD with that of 0-sheet models is not as clear. In addition, the VCD of “random-coil”-type proteins is found to be clearly related to VCD results from “random-coil” polypeptides. Finally, simulations are presented to postulate the expected VCD for protein structures having conformations that lie between the limiting cases discussed here.