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Probing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment

View ORCID ProfileDavid Moses, View ORCID ProfileFeng Yu, Garrett M. Ginell, Nora M. Shamoon, Patrick S. Koenig, View ORCID ProfileAlex S. Holehouse, View ORCID ProfileShahar Sukenik
doi: https://doi.org/10.1101/2020.08.17.252478
David Moses
aChemistry and Chemical Biology Program, University of California, Merced, CA
bCenter for Cellular and Biomolecular Machines (CCBM), University of California, Merced, CA
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Feng Yu
bCenter for Cellular and Biomolecular Machines (CCBM), University of California, Merced, CA
cQuantitative Systems Biology Program, University of California, Merced, CA
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Garrett M. Ginell
dDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO
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Nora M. Shamoon
eCalifornia State University Stanislaus, Turlock, CA
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Patrick S. Koenig
cQuantitative Systems Biology Program, University of California, Merced, CA
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Alex S. Holehouse
dDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO
fCenter for Science and Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO
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Shahar Sukenik
aChemistry and Chemical Biology Program, University of California, Merced, CA
bCenter for Cellular and Biomolecular Machines (CCBM), University of California, Merced, CA
cQuantitative Systems Biology Program, University of California, Merced, CA
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  • For correspondence: ssukenik@ucmerced.edu
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Abstract

Intrinsically disordered proteins and protein-regions (IDRs) make up roughly 30% of the human proteome and play vital roles in a wide variety of biological processes. Given a lack of persistent tertiary structure, all of the residues in an IDR are, to some extent, solvent exposed. This extensive surface area, coupled with the absence of strong intramolecular contacts, makes IDRs inherently sensitive to their chemical environment. Despite this sensitivity, our understanding of how IDR structural ensembles are influenced by changes in their chemical environment is limited. This is particularly relevant given a growing body of evidence showing that IDR function is linked to the underlying structural ensemble. We develop and use a combined experimental, computational, and analytical framework for high-throughput characterization of IDR sensitivity we call solution space scanning. Our framework reveals that IDRs show sequence-dependent sensitivity to solution chemistry, with complex behavior that can be interpreted through relatively simple polymer models. Our results imply that solution-responsive IDRs are ubiquitous and can provide an additional layer of biological regulation.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted August 18, 2020.
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Probing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment
David Moses, Feng Yu, Garrett M. Ginell, Nora M. Shamoon, Patrick S. Koenig, Alex S. Holehouse, Shahar Sukenik
bioRxiv 2020.08.17.252478; doi: https://doi.org/10.1101/2020.08.17.252478
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Probing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment
David Moses, Feng Yu, Garrett M. Ginell, Nora M. Shamoon, Patrick S. Koenig, Alex S. Holehouse, Shahar Sukenik
bioRxiv 2020.08.17.252478; doi: https://doi.org/10.1101/2020.08.17.252478

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