From protein denaturant to protectant: Comparative molecular dynamics study of alcohol/protein interactions
文献类型：期刊论文
| 作者 | Shao, Qiang1; Fan, Yubo2; Yang, Lijiang1; Gao, Yi Qin1 |
| 刊名 | JOURNAL OF CHEMICAL PHYSICS
 |
| 出版日期 | 2012-03-21 |
| 卷号 | 136期号:11 |
| ISSN号 | 0021-9606 |
| DOI | 10.1063/1.3692801 |
| 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 a-and beta-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 alcohol/water 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. (C) 2012 American Institute of Physics. [http://dx.doi.org/10.1063/1.3692801] |
| 语种 | 英语 |
| WOS记录号 | WOS:000302214200057 |
| 出版者 | AMER INST PHYSICS |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/49021]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Gao, Yi Qin |
| 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.Weill Cornell Med Coll, Bioinformat & Bioengn Program, Methodist Hosp Res Inst, Houston, TX 77030 USA |
| 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 alcohol/protein interactions[J]. JOURNAL OF CHEMICAL PHYSICS,2012,136(11). |
| APA | Shao, Qiang,Fan, Yubo,Yang, Lijiang,&Gao, Yi Qin.(2012).From protein denaturant to protectant: Comparative molecular dynamics study of alcohol/protein interactions.JOURNAL OF CHEMICAL PHYSICS,136(11). |
| MLA | Shao, Qiang,et al."From protein denaturant to protectant: Comparative molecular dynamics study of alcohol/protein interactions".JOURNAL OF CHEMICAL PHYSICS 136.11(2012). |
入库方式： OAI收割
来源：化学研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。