Molecular insights into the mechanisms of cation-type specific stability and denaturation of poly-l-glutamate: a simulation study | |
Shen, Hao1,2; Shen, Xin1,2; Cheng, Wei1,2; Zhang, Feng-Shou1,2,3 | |
刊名 | MOLECULAR SIMULATION
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2013-09 | |
卷号 | 39页码:842-847 |
关键词 | poly-l-glutamate cations conformation changes free-energy landscape |
ISSN号 | 0892-7022 |
DOI | 10.1080/08927022.2013.773630 |
英文摘要 | Cation-induced conformational changes of peptide as a guide to developing insights into human diseases-related proteins have received a lot of attention. The interactions between poly-l-glutamate (PGA) and different cations, including Na+, K+ and Mg2+, respectively, are studied in solvent at a concentration of 1M, and the behaviours of peptide with different cations are investigated. For Na+, an oscillatory stabilising process to -helix PGA is found, in accordance with the uniform free-energy landscape, whereas for K+, an extended -helix structure is formed by the terminal turns, suggesting a weaker attraction to charged head groups. For Mg2+, the bridged charged side chains are responsible for the maximum probability of helix state. These distinct structural changes can be attributed to the different interactions between charged head groups and cations. Both Na+ and K+ are mainly attracted around head groups by direct ion binding while Mg2+ is centrally trapped among adjacent charged head groups. In addition, a surprising shift of the backbone hydrogen bond, from intact state to intermediate state, is observed. This is opposite to the stabilising effect of Na+ around negatively charged head groups. |
资助项目 | National Basic Research Programme of China[2010CB832903] |
WOS关键词 | COIL-HELIX TRANSITION ; CONFORMATIONAL TRANSITION ; DYNAMICS SIMULATIONS ; HOFMEISTER-SERIES ; ENERGY LANDSCAPE ; AMINO-ACID ; SALT ; PROTEINS ; FORCE ; BIOMOLECULES |
WOS研究方向 | Chemistry ; Physics |
语种 | 英语 |
出版者 | TAYLOR & FRANCIS LTD |
WOS记录号 | WOS:000322697300008 |
内容类型 | 期刊论文 |
源URL | [http://119.78.100.186/handle/113462/57135] ![]() |
专题 | 中国科学院近代物理研究所 |
通讯作者 | Zhang, Feng-Shou |
作者单位 | 1.Beijing Normal Univ, Key Lab Beam Technol & Mat Modificat, Minist Educ, Coll Nucl Sci & Technol, Beijing 100875, Peoples R China 2.Beijing Radiat Ctr, Beijing 100875, Peoples R China 3.Ctr Theoret Nucl Phys, Natl Lab Heavy Ion Accelerator Lanzhou, Lanzhou 730000, Peoples R China |
推荐引用方式 GB/T 7714 | Shen, Hao,Shen, Xin,Cheng, Wei,et al. Molecular insights into the mechanisms of cation-type specific stability and denaturation of poly-l-glutamate: a simulation study[J]. MOLECULAR SIMULATION,2013,39:842-847. |
APA | Shen, Hao,Shen, Xin,Cheng, Wei,&Zhang, Feng-Shou.(2013).Molecular insights into the mechanisms of cation-type specific stability and denaturation of poly-l-glutamate: a simulation study.MOLECULAR SIMULATION,39,842-847. |
MLA | Shen, Hao,et al."Molecular insights into the mechanisms of cation-type specific stability and denaturation of poly-l-glutamate: a simulation study".MOLECULAR SIMULATION 39(2013):842-847. |
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