Does liquid-liquid phase separation drive peptide folding?
Does liquid-liquid phase separation drive peptide folding?
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液 - 液相分离会驱动肽折叠吗?
DOI:
10.1039/d0sc04993j
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发表时间:
2020-12-29
期刊:
影响因子:
8.4
通讯作者:
Serrano AL
中科院分区:
文献类型:
--
作者:
Edun DN;Flanagan MR;Serrano AL
Proline–arginine (PR) dipeptide repeats have been shown to undergo liquid–liquid phase separation and are an example of a growing number of intrinsically disordered proteins that can assemble into membraneless organelles. These structures have been posited as nucleation sites for pathogenic protein aggregation. As such, a better understanding of the effects that the increased local concentration and volumetric crowding within droplets have on peptide secondary structure is necessary. Herein we use Fourier transform infrared (FTIR) and two-dimensional infrared (2DIR) spectroscopy to show that formation of droplets by PR20 accompanies changes in the amide-I spectra consistent with folding into poly-proline helical structures. Two-dimensional infrared spectroscopy reveals folding of an intrinsically disordered peptide when sequestered into a model “membrane-less” organelle.
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影响因子:
3.3
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通讯作者:
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DOI:
10.1073/pnas.1706197114
发表时间:
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影响因子:
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Vendruscolo M