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烯-芳香序列通过C-H/π相互作用稳定转向,无论是cis-proline还是trans-proline

Himal K Ganguly¹, Michael B Elbaum¹, Neal J Zondlo¹

¹Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States.

|June 18, 2025

概括

蛋白质中的proline-aromatic序列,特别是Pro-Trp,通过C-H/π相互作用稳定局部结构,如转和螺旋. 这些相互作用影响了proline构造和蛋白质折叠动态.

科学领域:

生物化学生物化学
结构生物学结构生物学
计算化学计算化学

背景情况:

蛋白质中的proline-aromatic序列显示出更高频率的cis-proline胺基键.
香环与或骨干残留物之间的拟议的C-H/π相互作用被认为是驱动这种构造的.
之前的研究缺乏芳香环电子和cis-proline群体之间的明显相关性.

研究的目的:

研究芳香残留对林-芳香序列构成的影响.
阐明C-H/π和疏水相互作用在稳定蛋白质结构中的作用.
确定芳香相互作用如何影响cis-proline形成和蛋白质局部结构.

主要方法:

在模型 (Ac-TGPAr-NH2) 上进行NMR光谱学.
在蛋白质数据库 (PDB) 中对林芳香序列的生物信息学分析.
量子计算的调查. 量子计算的调查.

主要成果:

C-H/π 和疏水相互作用稳定了跨-和 cis-两种构造.
相互作用是最强的与托和最弱的与histidine,通过histidine电离调节.
氨酸芳香序列与特定的形状姿势相关,如β转.
在前烯残留物中的C-H/π相互作用稳定了不太有利的构造,包括cis-proline.

结论:

烯芳香序列,特别是Pro-Trp,作为蛋白质二次结构的核化场所.
C-H/π 相互作用在稳定蛋白质局部构造和影响普林异构化方面发挥着至关重要的作用.
了解这些相互作用有助于预测和设计蛋白质结构和功能.

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