protocolforanalyzingproteinensemblestructuresfromchemicalcrosslinksusingdynaxl
文献类型：期刊论文
| 作者 | Gong Zhou1; Liu Zhu2; Dong Xu1; Ding Yuehe3; Dong Mengqiu4; Tang Chun1 |
| 刊名 | biophysicsreports
 |
| 出版日期 | 2017 |
| 卷号 | 3期号:4/6页码:100 |
| ISSN号 | 2364-3439 |
| 英文摘要 | Chemical cross-linking coupled with mass spectroscopy (CXMS) is a powerful technique for investigating protein structures. CXMS has been mostly used to characterize the predominant structure for a protein, whereas cross-links incompatible with a unique structure of a protein or a protein complex are often discarded. We have recently shown that the so-called over-length cross-links actually contain protein dynamics information. We have thus established a method called DynaXL, which allow us to extract the information from the over-length cross-links and to visualize protein ensemble structures. In this protocol, we present the detailed procedure for using DynaXL, which comprises five steps. They are identification of highly confident cross-links, delineation of protein domains/subunits, ensemble rigid-body refinement, and final validation/assessment. The DynaXL method is generally applicable for analyzing the ensemble structures of multi-domain proteins and protein-protein complexes, and is freely available at www.tanglab.org/resources. |
| 语种 | 英语 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/19482]  |
| 专题 | 中国科学院武汉物理与数学研究所 |
| 作者单位 | 1.中国科学院武汉物理与数学研究所 2.中国科学院上海生命科学研究院神经科学研究所 3.马萨诸塞大学 4.National Institute of Biological Sciences |
| 推荐引用方式 GB/T 7714 | Gong Zhou,Liu Zhu,Dong Xu,et al. protocolforanalyzingproteinensemblestructuresfromchemicalcrosslinksusingdynaxl[J]. biophysicsreports,2017,3(4/6):100. |
| APA | Gong Zhou,Liu Zhu,Dong Xu,Ding Yuehe,Dong Mengqiu,&Tang Chun.(2017).protocolforanalyzingproteinensemblestructuresfromchemicalcrosslinksusingdynaxl.biophysicsreports,3(4/6),100. |
| MLA | Gong Zhou,et al."protocolforanalyzingproteinensemblestructuresfromchemicalcrosslinksusingdynaxl".biophysicsreports 3.4/6(2017):100. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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。