Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics
文献类型：期刊论文
| 作者 | Lu Q ; Lu HP ; Wang J |
| 刊名 | physical review letters
 |
| 出版日期 | 2007 |
| 卷号 | 98期号:12页码:文献编号：128105 |
| 关键词 | ALDRICH-SYNDROME PROTEIN TRANSITION-STATE CONFORMATIONAL DYNAMICS CDC42 BINDING DETERMINES LANDSCAPES DOMAIN |
| ISSN号 | 0031-9007 |
| 通讯作者 | lu q |
| 中文摘要 | combining a single-molecule study of protein binding with a coarse grained molecular dynamics model including solvent (water molecules) effects, we find that biomolecular recognition is determined by flexibilities in addition to structures. our single-molecule study shows that binding of cbd (a fragment of wiskott-aldrich syndrome protein) to cdc42 involves bound and loosely bound states, which can be quantitatively explained in our model as a result of binding with large conformational changes. our model identified certain key residues for binding consistent with mutational experiments. our study reveals the role of flexibility and a new scenario of dimeric binding between the monomers: first bind and then fold. |
| 收录类别 | SCI |
| 语种 | 英语 |
| 公开日期 | 2010-07-13 ; 2011-06-09 |
| 源URL | [http://ir.ciac.jl.cn/handle/322003/14027]  |
| 专题 | 长春应用化学研究所_长春应用化学研究所知识产出_期刊论文 |
| 推荐引用方式 GB/T 7714 | Lu Q,Lu HP,Wang J. Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics[J]. physical review letters,2007,98(12):文献编号：128105. |
| APA | Lu Q,Lu HP,&Wang J.(2007).Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics.physical review letters,98(12),文献编号：128105. |
| MLA | Lu Q,et al."Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics".physical review letters 98.12(2007):文献编号：128105. |
入库方式： OAI收割
来源：长春应用化学研究所
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