典型蛋白质折叠中阳离子-<em>π</em>相互作用的特异性

引用本文: 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 shu

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

典型蛋白质折叠中阳离子-π相互作用的特异性

基金项目:
国家自然科学基金(30570427) 和北京市自然科学基金(4092008) 资助项目 (30570427) 和北京市自然科学基金(4092008)

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:

English

Specificity of Cation-π Interactions in Typical Protein Folds

1.
School of Life Science and Bioengineering, Beijing University of Technology, Beijing 100124, P. R. China
Received Date: 29 April 2010
Available Online: 27 September 2010
Fund Project:
国家自然科学基金(30570427) 和北京市自然科学基金(4092008) 资助项目

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:

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沈阳化工大学材料科学与工程学院沈阳 110142

典型蛋白质折叠中阳离子-π相互作用的特异性

English

Specificity of Cation-π Interactions in Typical Protein Folds

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