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DOI | 10.1126/science.aan5774 |
Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water | |
Riback, Joshua A.1; Bowman, Micayla A.2; Zmyslowski, Adam M.3; Knoverek, Catherine R.2; Jumper, John M.3,4,5; Hinshaw, James R.4,5; Kaye, Emily B.2; Freed, Karl F.4,5; Clark, Patricia L.2; Sosnick, Tobin R.3,6 | |
2017-10-13 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 358期号:6360页码:238-241 |
文章类型 | Article |
语种 | 英语 |
国家 | USA |
英文摘要 | A substantial fraction of the proteome is intrinsically disordered, and even well-folded proteins adopt non-native geometries during synthesis, folding, transport, and turnover. Characterization of intrinsically disordered proteins (IDPs) is challenging, in part because of a lack of accurate physical models and the difficulty of interpreting experimental results. We have developed a general method to extract the dimensions and solvent quality (self-interactions) of IDPs from a single small-angle x-ray scattering measurement. We applied this procedure to a variety of IDPs and found that even IDPs with low net charge and high hydrophobicity remain highly expanded in water, contrary to the general expectation that protein-like sequences collapse in water. Our results suggest that the unfolded state of most foldable sequences is expanded; we conjecture that this property was selected by evolution to minimize misfolding and aggregation. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000412841500052 |
WOS关键词 | X-RAY-SCATTERING ; MOLECULE FRET SPECTROSCOPY ; REDUCED RIBONUCLEASE-A ; UNFOLDED-STATE ; CHAIN COLLAPSE ; SIMULATIONS ; DIMENSIONS ; DYNAMICS ; PHASE ; STEP |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/197095 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Chicago, Grad Program Biophys Sci, Chicago, IL 60637 USA; 2.Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA; 3.Univ Chicago, Dept Biochem & Mol Biol, 920 E 58Th St, Chicago, IL 60637 USA; 4.Univ Chicago, Dept Chem, 5735 S Ellis Ave, Chicago, IL 60637 USA; 5.Univ Chicago, James Franck Inst, 5640 S Ellis Ave, Chicago, IL 60637 USA; 6.Univ Chicago, Inst Biophys Dynam, Chicago, IL 60637 USA |
推荐引用方式 GB/T 7714 | Riback, Joshua A.,Bowman, Micayla A.,Zmyslowski, Adam M.,et al. Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water[J]. SCIENCE,2017,358(6360):238-241. |
APA | Riback, Joshua A..,Bowman, Micayla A..,Zmyslowski, Adam M..,Knoverek, Catherine R..,Jumper, John M..,...&Sosnick, Tobin R..(2017).Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water.SCIENCE,358(6360),238-241. |
MLA | Riback, Joshua A.,et al."Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".SCIENCE 358.6360(2017):238-241. |
条目包含的文件 | 条目无相关文件。 |
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