典型蛋白质折叠中阳离子-π相互作用的特异性

doi:10.3866/PKU.WHXB20100939

物理化学学报 >> 2010, Vol. 26 >> Issue (10): 2828-2832.doi: 10.3866/PKU.WHXB20100939

典型蛋白质折叠中阳离子-π相互作用的特异性

乔辉, 李晓琴, 徐海松, 孔令强, 彭宇

北京工业大学生命科学与生物工程学院, 北京 100124

收稿日期:2010-04-29 修回日期:2010-06-28 发布日期:2010-09-27
通讯作者: 李晓琴 E-mail:lxq0811@bjut.edu.cn
基金资助:
国家自然科学基金(30570427) 和北京市自然科学基金(4092008) 资助项目

Specificity of Cation-π Interactions in Typical Protein Folds

QIAO Hui, LI Xiao-Qin, XU Hai-Song, KONG Ling-Qiang, PENG Yu

School of Life Science and Bioengineering, Beijing University of Technology, Beijing 100124, P. R. China

Received:2010-04-29 Revised:2010-06-28 Published:2010-09-27
Contact: LI Xiao-Qin E-mail:lxq0811@bjut.edu.cn
Supported by:
The project was supported by the National Natural Science Foundation of China (30570427) and Natural Science Foundation of Beijing, China(4092008).

摘要/Abstract

摘要：

蛋白质中的阳离子-π相互作用是带正电荷的氨基酸(Lys、Arg)和芳香族氨基酸(Phe、Tyr、Trp)之间的一种作用力. 对α/β类蛋白中两种典型折叠类型(单绕和双绕)的研究表明: (1) 单绕结构中阳离子-π相互作用的分布密度大约是双绕结构中的2.6 倍; (2)在单绕结构中, 样本所含氨基酸残基数量与样本中阳离子-π的数量有明显的相关性, 在双绕结构中没有发现类似的相关性; (3) Lys、Arg 与Tyr 在单绕中比在双绕中更容易形成阳离子-π相互作用; (4) Arg-Tyr组合在单绕中出现的几率较大, Arg-Phe 组合在双绕中出现的几率较大; (5) 阳离子-π相互作用在65%的单绕样本中形成阵列或分布在结构的首尾间.

关键词: 单绕, 双绕, 阳离子-π相互作用, 特异性

Abstract:

In proteins, cation-π interactions are formed between positively charged amino acids (Lys, Arg) and aromatic amino acids(Phe, Tyr, Trp). We investigated the cation-π interactions in two typical folding structures of α/β proteins, namely, the singly wound structure and the doubly wound structure. The results reveal that: (1) The distribution density of cation-π interactions in singly wound structures is about 2.6 times as high as that in doubly wound structures; (2) In singly wound structures, a correlation is observed between the amount of residues and their cation-π interactions while no correlation is observed in doubly wound structures; (3) Lys, Arg and Tyr in singly wound structures participate more easily in cation-π interactions than those in doubly wound structures; (4) Arg-Phe pairs are preferred in doubly wound structures while Arg-Tyr pairs are preferred in singly wound structures; (5) In singly wound structures, 65%of the cation-π interactions formarrays or distribute between the starting point and the end point in the structures.

Key words: Singly wound, Doubly wound, Cation-π interaction, Specificity

乔辉, 李晓琴, 徐海松, 孔令强, 彭宇. 典型蛋白质折叠中阳离子-π相互作用的特异性[J]. 物理化学学报, 2010, 26(10), 2828-2832. doi: 10.3866/PKU.WHXB20100939

QIAO Hui, LI Xiao-Qin, XU Hai-Song, KONG Ling-Qiang, PENG Yu. Specificity of Cation-π Interactions in Typical Protein Folds[J]. Acta Phys. -Chim. Sin. 2010, 26(10), 2828-2832. doi: 10.3866/PKU.WHXB20100939

链接本文: https://www.whxb.pku.edu.cn/CN/10.3866/PKU.WHXB20100939

https://www.whxb.pku.edu.cn/CN/Y2010/V26/I10/2828

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典型蛋白质折叠中阳离子-π相互作用的特异性

Specificity of Cation-π Interactions in Typical Protein Folds

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