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Does Liquid-Liquid Phase Separation Drive Peptide Folding?

preprint
submitted on 07.09.2020 and posted on 07.09.2020 by Dean N. Edun, Meredith R. Flanagan, Arnaldo Serrano

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 a nucleation site for pathogenic protein aggregation. As such, a better understanding of the effects that the increased local concentration and volumetric crowding within droplets has 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 accompany changes in the Amide-I spectra consistent with folding into poly-proline helical structures.

History

Email Address of Submitting Author

arnaldo.serrano@nd.edu

Institution

University of Notre Dame

Country

United States

ORCID For Submitting Author

https://orcid.org/0000-0002-7268-1306

Declaration of Conflict of Interest

We declare no conflicts of interest.

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