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

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 (30570427) 和北京市自然科学基金(4092008)

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.
- Singly wound,
- Doubly wound,
- Cation-π interaction,
- Specificity
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沈阳化工大学材料科学与工程学院沈阳 110142