Counterion Effects on the Denaturing Activity of Guanidinium Cation to Protein
文献类型：期刊论文
| 作者 | Shao, Qiang2,3 ; Fan, Yubo1; Yang, Lijiang3; Gao, Yi Qin3
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| 刊名 | JOURNAL OF CHEMICAL THEORY AND COMPUTATION
 |
| 出版日期 | 2012-11 |
| 卷号 | 8期号:11页码:4364-4373 |
| ISSN号 | 1549-9618 |
| DOI | 10.1021/ct3002267 |
| 文献子类 | Article |
| 英文摘要 | The denaturation of a three-alpha-helix bundle, the B domain of protein A, by guanidinium is studied by molecular dynamics simulations. The simulation results showed that in GdmCl solution, guanidinium cations accumulate around the protein surface, whereas chloride anions are expelled from the protein. In contrast, in GdmSCN solution, both cations and anions accumulate around the protein surface and the degree of Gdm(+) accumulation. is higher. than that in GdmCl, suggesting the cooperativity between the cations and anions in preferential binding. Moreover, the accumulation of guanidinium around the protein surface is not uniform, and it prefers to populate near residues With negatively Charged or planar side chains On the Other hand, guanidinium participates in direct hydrogen bonding with backbone carbonyl groups Meanwhile, guanidinium also promotes the hydrogen bonding Of Water to a backbone carbonyl group by changing the hydrogen bonding network within solvent Therefore, the attack from both water and guanidinium breaks backbone hydrogen bonds and results in the destruction of secondary structures of the protein. The stronger accumulation of guanidinium and more hydrogen bonding from guanidinium in GdmSCN leads to the increase of its denaturing efficiency compared to GdmCl. In the latter solution, the ion pairing between Cl- and guanidinium limits the approach of guanidinium to protein and the hydrogen bonding between guanidinium and protein, and the main denaturing contributor is the hydrogen bonding from water. |
| WOS关键词 | KIRKWOOD-BUFF THEORY ; PREFERENTIAL INTERACTION PARAMETERS ; MOLECULAR-DYNAMICS SIMULATION ; TRIMETHYLAMINE N-OXIDE ; WATER-STRUCTURE ; B-DOMAIN ; CHLORIDE SOLUTIONS ; EQUILIBRIUM INTERMEDIATE ; BIOCHEMICAL REACTIONS ; POTENTIAL FUNCTIONS |
| 资助项目 | National Natural Science Foundation of China[91027044] ; National Natural Science Foundation of China[21125311] ; National Natural Science Foundation of China[21003003] ; Texas Advanced Computing Center (TACC) at The University of Texas at Austin[TG-MCB110130] |
| WOS研究方向 | Chemistry ; Physics |
| 语种 | 英语 |
| WOS记录号 | WOS:000311191900038 |
| 出版者 | AMER CHEMICAL SOC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/277885]  |
| 专题 | 药物发现与设计中心 |
| 通讯作者 | Gao, Yi Qin |
| 作者单位 | 1.Methodist Hosp, Bioinformat & Bioengn Program, Res Inst, Weill Cornell Med Coll, Houston, TX 77030 USA 2.Chinese Acad Sci, Drug Discovery & Design Ctr, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China; 3.Peking Univ, Inst Theoret & Computat Chem, Coll Chem & Mol Engn, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Shao, Qiang,Fan, Yubo,Yang, Lijiang,et al. Counterion Effects on the Denaturing Activity of Guanidinium Cation to Protein[J]. JOURNAL OF CHEMICAL THEORY AND COMPUTATION,2012,8(11):4364-4373. |
| APA | Shao, Qiang,Fan, Yubo,Yang, Lijiang,&Gao, Yi Qin.(2012).Counterion Effects on the Denaturing Activity of Guanidinium Cation to Protein.JOURNAL OF CHEMICAL THEORY AND COMPUTATION,8(11),4364-4373. |
| MLA | Shao, Qiang,et al."Counterion Effects on the Denaturing Activity of Guanidinium Cation to Protein".JOURNAL OF CHEMICAL THEORY AND COMPUTATION 8.11(2012):4364-4373. |
入库方式： OAI收割
来源：上海药物研究所
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