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

Acta Phys. -Chim. Sin. ›› 2010, Vol. 26 ›› Issue (10): 2828-2832.doi: 10.3866/PKU.WHXB20100939

• BIOPHYSICAL CHEMISTRY • Previous Articles Next Articles

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).

Abstract

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

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

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Specificity of Cation-π Interactions in Typical Protein Folds

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