利用拉曼光谱对微管蛋白和微管进行二级结构分析。

Secondary structure analysis of tubulin and microtubules with Raman spectroscopy.

作者信息

Audenaert R, Heremans L, Heremans K, Engelborghs Y

机构信息

Laboratory of Chemical and Biological Dynamics, University of Leuven, Belgium

出版信息

Biochim Biophys Acta. 1989 Jun 13;996(1-2):110-5. doi: 10.1016/0167-4838(89)90102-7.

DOI:10.1016/0167-4838(89)90102-7

PMID:2736254

Abstract

Raman spectroscopy is used to study the secondary structure of tubulin in the assembled and the dissociated states from the analysis of the amide-I band. Essentially two states are recognized: the GTP- and the GDP-bound state, differing in alpha-helix and antiparallel beta-sheet content. Microtubules give a spectrum which is very similar to the GDP-bound state. MAPs and temperature have minor effects, while increasing the pH up to 8 causes a reduction in alpha-helix content and a increase in antiparallel beta-sheet. The binding of demecolcine also induces structural changes which are similar to the GDP-bound state.

摘要

通过对酰胺-I带的分析，拉曼光谱用于研究组装态和解离态微管蛋白的二级结构。本质上可识别出两种状态：结合GTP和结合GDP的状态，它们在α-螺旋和反平行β-折叠含量上有所不同。微管给出的光谱与结合GDP的状态非常相似。微管相关蛋白（MAPs）和温度的影响较小，而将pH值提高到8会导致α-螺旋含量减少，反平行β-折叠增加。秋水仙碱的结合也会诱导与结合GDP状态相似的结构变化。