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通过振动和光学活动来研究聚,蛋白质和病毒中的α螺旋体水合

Iain H McColl¹, Ewan W Blanch, Lutz Hecht

¹Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom.

Journal of the American Chemical Society

|July 1, 2004

概括

振动拉曼光学活动 (ROA) 根据它们的水化情况区分了两种类型的右手阿尔法螺旋. 没有水的螺旋显示带接近1300厘米(-1),而水的螺旋显示带接近1340厘米(-1).

科学领域:

生物物理学的生物物理.
频谱学是一种光谱学.
结构生物学结构生物学

背景情况:

阿尔法螺旋是蛋白质的基本二次结构.
区分不同的α螺旋形状对于理解蛋白质功能至关重要.
振动拉曼光学活性 (ROA) 是一种对分子性敏感的光谱技术.

研究的目的:

调查ROA光谱的潜力,以区分不同的类型的右手阿尔法螺旋.
为了将特定的ROA光谱特征与阿尔法螺旋体的水化状态和构造性质相关联.

主要方法:

使用振动拉曼光学活动 (ROA) 光谱.
综合蛋白X射线晶体结构数据用于结构洞察.
在扩展的胺基III区域分析的ROA光谱 (约. 1300-1340厘米 (((-1))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))))

主要成果:

在胺III区域确定了两个不同的ROA波段,与右侧的α螺旋相关.
在~1300厘米的正ROA波段与无水化,正规的alpha (c) 螺旋相对应,在疏水环境中普遍存在.
一个正的ROA波段在~1340cm(-1) 与水合,开放的alpha(o) 螺旋相对应,在水友环境中由水或侧链相互作用稳定.

结论:

ROA光谱学可以有效地区分无水化 (alpha ((c)) 和水化 (alpha ((o)) 右侧的α螺旋形状.
补水状态和特定的侧链特征显著影响alpha-helix形状及其ROA签名.
聚乙L-酸) 存在于一个左侧螺旋状状态,类似于水合的αo) 形状.

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