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(III) 结合对β-毛结构的影响
Danny Ramadan1, Daniel J Cline, Shi Bai
1Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716-2522, USA.
Journal of the American Chemical Society
|February 22, 2007
概括
(III) 与蛋白质囊蛋白结合可以改变二次结构. 在β-hairpins中的特定的囊定位增强或破坏β-sheet的含量,影响.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 毒理学 毒理学 毒理学
背景情况:
- (III) 化合物具有显著的毒理和药理作用.
- 的确切作用机制及其对蛋白质的结构影响,特别是基残留物,尚未完全理解.
研究的目的:
- 为了研究与囊结合如何影响模型β-hairpin的二次结构.
- 确定囊定位对结亲和力和结构后果的影响.
主要方法:
- 一个模型单体β-hairpin与工程氨酸对的合成.
- 使用循环二重化 (CD),核磁共振 (NMR),紫外线光谱和快速反应研究进行了表征.
- 使用单甲基酸和p-succinylamidephenyl arsenoxide (PSAO) 的结的分析.
主要成果:
- 定位在同一个面部的β-hairpin上,氨酸增强了β-sheet结构.
- 对面的交叉链囊素仍然紧紧地结合了,并且比β-sheet增加了很少.
- 与非对立的半氨酸结合,或沿着单一链破坏了β-sheet结构.
结论:
- 与蛋白质结合的结构后果在很大程度上取决于乙烯残留物的空间布置.
- 结合可以诱导局部二次蛋白质结构的实质性变化,影响生物活性剂的功能.
- 这些发现提供了对毒性和药理学的基础分子机制的见解.
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