在阿尔法螺旋和蛋白质中,芳香和基本侧链之间的稳定相互作用. 氨酸对螺旋形圆形二元体的影响
Charles D Andrew1, Samita Bhattacharjee, Nicoleta Kokkoni
1Department of Biomolecular Sciences, UMIST, P.O. Box 88, Manchester M60 1QD, UK.
Journal of the American Chemical Society
|October 24, 2002
概括
芳香和基本的氨基酸,如氨酸和氨酸稳定阿尔法螺旋. 这些相互作用主要是疏水的,而不是阴离子-pi键,影响蛋白质结构.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 蛋白质科学 蛋白质科学
背景情况:
- 氨基酸相互作用驱动蛋白质折叠和稳定性.
- 了解阿尔法螺旋体中的侧链能量对于预测蛋白质结构至关重要.
研究的目的:
- 为了研究阿尔法螺旋体中芳香基氨基酸相互作用的能量.
- 为了澄清这些相互作用的性质 (疏水性与阴离子-pi).
主要方法:
- 循环二重化 (CD) 光谱法用于测量螺旋性.
- 基于Lifson-Roig的螺旋/线圈理论用于数据解释.
- 计算氨酸对CD光谱的影响.
主要成果:
- 芳香基对 (Phe-Lys,Lys-Phe,Phe-Arg,Arg-Phe,Tyr-Lys) 正在稳定 (-0.10 到 -0.18 千卡/mol).
- 铁素的螺旋偏好被改进为0.35.
- 蛋白质结构分析显示主要是疏水性相互作用.
结论:
- 阿尔法螺旋体中的芳香和基本氨基酸相互作用正在稳定.
- 这些相互作用主要是由疏水性接触驱动的,而不是阴离子-pi键.
- 这些发现完善了对蛋白质中螺旋稳定性和氨基酸相互作用的理解.
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