Journal
CHEMICAL SCIENCE
Volume 12, Issue 7, Pages 2474-2479Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0sc04993j
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Funding
- College of Science at the University of Notre Dame
- Notre Dame IBMS program
- Dana Wilson Quintero Memorial Graduate Fellowship
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Proline-arginine (PR) dipeptide repeats can undergo liquid-liquid phase separation, forming membraneless organelles and potentially serving as nucleation sites for pathogenic protein aggregation. Studies have shown that increased local concentration and volumetric crowding within droplets can impact peptide secondary structure.
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.
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