Water plays an important role in osmolyte-induced hairpin structure change: A molecular dynamics simulation study
文献类型：期刊论文
| 作者 | Shao, Qiang2 ; Gao, Yi Qin1
|
| 刊名 | JOURNAL OF CHEMICAL PHYSICS
 |
| 出版日期 | 2012-10-14 |
| 卷号 | 137期号:14 |
| 关键词 | biochemistry hydrogen bonds molecular biophysics molecular dynamics method proteins water |
| ISSN号 | 0021-9606 |
| DOI | 10.1063/1.4757419 |
| 文献子类 | Article |
| 英文摘要 | To investigate how solvent (water) and cosolvent (osmolyte) affect protein structure in various osmolyte solutions, in the present study we used GB1p peptide as the model protein to study its folding process in 2,2,2-trifluoroethanol (TFE)/water and denaturation process in GdmSCN/water solutions, respectively. It was observed that TFE moderately enhances the structure stability of native beta-hairpin, consistent with the previous experimental observation that the hairpin conformation population of several polypeptides is increased in TFE/water solution compared to in pure water. More interestingly, the formation of beta-hairpin is significantly accelerated in TFE/water solution. The accelerated folding of beta-hairpin consists of following sequential events: the accumulation of TFE on protein surface -> less water surrounding carbonyl group (easier dehydration of CO) -> the formation of CO-NH backbone hydrogen bond. In contrary, the denaturation of hairpin structure of GB1p peptide in GdmSCN/water solution is induced by the accumulation of Gdm(+) on protein surface and the hydrogen bonding from water as well as Gdm(+). Therefore, this study shows the importance of water in TFE-induced formation and Gdm(+)-induced denaturation of beta-hairpin structure. (C) 2012 American Institute of Physics. [http://dx.doi.org/10.1063/1.4757419] |
| WOS关键词 | BETA-HAIRPIN ; CONFORMATIONAL-CHANGES ; AQUEOUS-SOLUTION ; DENATURED STATE ; PROTEIN-A ; B-DOMAIN ; TRIFLUOROETHANOL ; PEPTIDES ; MECHANISM ; NMR |
| 资助项目 | National Natural Science Foundation of China[21003003] ; National Natural Science Foundation of China[21125311] ; National Natural Science Foundation of China[91027044] ; 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:000310302800035 |
| 出版者 | AMER INST PHYSICS |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/277911]  |
| 专题 | 药物发现与设计中心 |
| 通讯作者 | Shao, Qiang |
| 作者单位 | 1.Peking Univ, Inst Theoret & Computat Chem, Coll Chem & Mol Engn, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China 2.Chinese Acad Sci, Drug Discovery & Design Ctr, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Shao, Qiang,Gao, Yi Qin. Water plays an important role in osmolyte-induced hairpin structure change: A molecular dynamics simulation study[J]. JOURNAL OF CHEMICAL PHYSICS,2012,137(14). |
| APA | Shao, Qiang,&Gao, Yi Qin.(2012).Water plays an important role in osmolyte-induced hairpin structure change: A molecular dynamics simulation study.JOURNAL OF CHEMICAL PHYSICS,137(14). |
| MLA | Shao, Qiang,et al."Water plays an important role in osmolyte-induced hairpin structure change: A molecular dynamics simulation study".JOURNAL OF CHEMICAL PHYSICS 137.14(2012). |
入库方式： OAI收割
来源：上海药物研究所
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