From protein denaturant to protectant: Comparative molecular dynamics study of alcoholprotein interactions
文献类型：期刊论文
| 作者 | Shao, Qiang1,2 ; Fan, Yubo3; Yang, Lijiang1; Qin Gao, Yi1
|
| 刊名 | Journal of Chemical Physics
 |
| 出版日期 | 2012-03-21 |
| 卷号 | 136期号:11 |
| ISSN号 | 00219606 |
| DOI | 10.1063/1.3692801 |
| 文献子类 | Article |
| 英文摘要 | It is well known that alcohols can have strong effects on protein structures. For example, monohydric methanol and ethanol normally denature, whereas polyhydric glycol and glycerol protect, protein structures. In a recent combined theoretical and NMR experimental study, we showed that molecular dynamics simulations can be effectively used to understand the molecular mechanism of methanol denaturing protein. In this study, we used molecular dynamics simulations to investigate how alcohols with varied hydrophobicity and different numbers of hydrophilic groups (hydroxyl groups) exert effects on the structure of the model polypeptide, BBA5. First, we showed that methanol and trifluoroethanol (TFE) but not glycol or glycerol disrupt hydrophobic interactions. The latter two alcohols instead protect the assembly of the - and β-domains of the polypeptide. Second, all four alcohols were shown to generally increase the stability of secondary structures, as revealed by the increased number of backbone hydrogen bonds formed in alcoholwater solutions compared to that in pure water, although individual hydrogen bonds can be weakened by certain alcohols, such as TFE. The two monohydric alcohols, methanol and TFE, display apparently different sequence-dependence in affecting the backbone hydrogen bond stability: methanol tends to enhance the stability of backbone hydrogen bonds of which the carbonyl groups are from polar residues, whereas TFE tends to stabilize those involving non-polar residues. These results demonstrated that subtle differences in the solution environment could have distinct consequences on protein structures. |
| 语种 | 英语 |
| 出版者 | American Institute of Physics Inc. |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/266954]  |
| 专题 | 药物发现与设计中心 |
| 通讯作者 | Qin Gao, Yi |
| 作者单位 | 1.Beijing National Laboratory of Molecular Sciences, Institute of Theoretical and Computational Chemistry, Peking University, Beijing 100871, China; 2.Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Shanghai 201203, China 3.Bioinformatics and Bioengineering Program, Methodist Hospital Research Institute, Weill Cornell Medical College, Houston, TX 77030, United States; |
| 推荐引用方式 GB/T 7714 | Shao, Qiang,Fan, Yubo,Yang, Lijiang,et al. From protein denaturant to protectant: Comparative molecular dynamics study of alcoholprotein interactions[J]. Journal of Chemical Physics,2012,136(11). |
| APA | Shao, Qiang,Fan, Yubo,Yang, Lijiang,&Qin Gao, Yi.(2012).From protein denaturant to protectant: Comparative molecular dynamics study of alcoholprotein interactions.Journal of Chemical Physics,136(11). |
| MLA | Shao, Qiang,et al."From protein denaturant to protectant: Comparative molecular dynamics study of alcoholprotein interactions".Journal of Chemical Physics 136.11(2012). |
入库方式： OAI收割
来源：上海药物研究所
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