(III) 结合对α-螺旋结构的影响
Daniel J Cline1, Colin Thorpe, Joel P Schneider
1Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716-2522, USA.
Journal of the American Chemical Society
|March 6, 2003
概括
在模型酸中与囊残留物结合的 () 破坏了α-螺旋结构的稳定,改变了蛋白质折叠. 特定的安排,比如i,i+3,可以消除螺旋,而i,i+4安排可以稳定它们.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 化学生物学 化学生物学
背景情况:
- (III) 具有多种不同的细胞效应,但其对蛋白质结构的影响尚不清楚.
- 半氨酸残留物是生物系统中的关键结合点.
研究的目的:
- 为了研究 (III) 与α-螺旋结合的结构后果.
- 确定囊残留物的排列和位置如何影响的结合和结构变化.
主要方法:
- 循环二重化 (CD) 光谱法用于分析的二次结构.
- 合成了具有不同氨酸 (Cys) 残留排列的模型α-螺旋类.
- 测量了结合亲缘关系和关联率常数.
主要成果:
- 当Cys残留物处于i,i+1,i+2或i+3排列的中心或C端位置时, (III) 结合了不稳定的螺旋.
- 与i,i+3位置的Cys残留物结合,消除了螺旋结构,形成了另一个折叠.
- 螺旋稳定发生在具有i,i+4 Cys残留的上,并测量了相互作用能量.
- 在中等稳定的螺旋体中,As(III) 的结合亲和度对Cys的位置大致不敏感.
结论:
- (III) 结合显著调节了阿尔法螺旋二次结构.
- 囊残留物的空间排列决定了结合的结构结果.
- 了解这些相互作用对于理解的细胞机制至关重要.
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