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| DOI | 10.1126/science.aba3854 |
| Disordered proteins follow diverse transition paths as they fold and bind to a partner | |
| Kim J.-Y.; Chung H.S. | |
| 发表日期 | 2020 |
| ISSN | 0036-8075 |
| 起始页码 | 1253 |
| 结束页码 | 1257 |
| 卷号 | 368期号:6496 |
| 英文摘要 | Transition paths of macromolecular conformational changes such as protein folding are predicted to be heterogeneous. However, experimental characterization of the diversity of transition paths is extremely challenging because it requires measuring more than one distance during individual transitions. In this work, we used fast three-color single-molecule Förster resonance energy transfer spectroscopy to obtain the distribution of binding transition paths of a disordered protein. About half of the transitions follow a path involving strong non-native electrostatic interactions, resulting in a transition time of 300 to 800 microseconds. The remaining half follow more diverse paths characterized by weaker electrostatic interactions and more than 10 times shorter transition path times. The chain flexibility and non-native interactions make diverse binding pathways possible, allowing disordered proteins to bind faster than folded proteins. © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. |
| 关键词 | intrinsically disordered proteinprotein bindingchemistryfluorescence resonance energy transferproceduresprotein conformationprotein foldingsingle molecule imagingstatic electricityFluorescence Resonance Energy TransferIntrinsically Disordered ProteinsProtein BindingProtein ConformationProtein FoldingSingle Molecule ImagingStatic Electricity |
| 语种 | 英语 |
| 来源机构 | Science |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/133437 |
| 推荐引用方式 GB/T 7714 | Kim J.-Y.,Chung H.S.. Disordered proteins follow diverse transition paths as they fold and bind to a partner[J]. Science,2020,368(6496). |
| APA | Kim J.-Y.,&Chung H.S..(2020).Disordered proteins follow diverse transition paths as they fold and bind to a partner.,368(6496). |
| MLA | Kim J.-Y.,et al."Disordered proteins follow diverse transition paths as they fold and bind to a partner".368.6496(2020). |
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