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Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins

View ORCID ProfileDinesh Sundaravadivelu Devarajan, Shiv Rekhi, Arash Nikoubashman, Young C. Kim, View ORCID ProfileMichael P. Howard, View ORCID ProfileJeetain Mittal
doi: https://doi.org/10.1101/2022.07.04.498718
Dinesh Sundaravadivelu Devarajan
†Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX 77843, United States
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  • ORCID record for Dinesh Sundaravadivelu Devarajan
Shiv Rekhi
†Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX 77843, United States
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Arash Nikoubashman
‡Institute of Physics, Johannes Gutenberg University Mainz, Staudingerweg 7, 55128 Mainz, Germany
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Young C. Kim
¶Center for Materials Physics and Technology, Naval Research Laboratory, Washington, DC 20375, United States
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Michael P. Howard
§Department of Chemical Engineering, Auburn University, Auburn, AL 36849, United States
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Jeetain Mittal
†Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX 77843, United States
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  • For correspondence: jeetain@tamu.edu
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Abstract

The stability and physiological function of many biomolecular coacervates depend on the structure and dynamics of intrinsically disordered proteins (IDPs) that typically contain a significant fraction of charged residues. Although the effect of relative arrangement of charged residues on IDP conformation is a well-studied problem, the associated changes in dynamics are far less understood. In this work, we systematically interrogate the effects of charge distribution on the chain-level and segmental dynamics of polyampholytic IDPs in dilute solutions. We study a coarse-grained model polyampholyte consisting of an equal fraction of two oppositely charged residues (glutamic acid and lysine) that undergoes a transition from an ideal chain-like conformation for uniformly charge-patterned sequences to a semi-compact conformation for highly charge-segregated sequences. Changes in the chain-level dynamics with increasing charge segregation correlate with changes in conformation. The chain-level and segmental dynamics conform to simple homopolymer models for uniformly charge-patterned sequences but deviate with increasing charge segregation, both in the presence and absence of hydrodynamic interactions. We discuss the significance of these findings, obtained for a model polyampholyte, in the context of a charge-rich intrinsically disordered region of the naturally occurring protein LAF-1. Our findings have important implications for understanding the effects of charge patterning on the dynamics of polyampholytic IDPs in dilute conditions using polymer scaling theories.

Competing Interest Statement

The authors have declared no competing interest.

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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 July 04, 2022.
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Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins
Dinesh Sundaravadivelu Devarajan, Shiv Rekhi, Arash Nikoubashman, Young C. Kim, Michael P. Howard, Jeetain Mittal
bioRxiv 2022.07.04.498718; doi: https://doi.org/10.1101/2022.07.04.498718
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Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins
Dinesh Sundaravadivelu Devarajan, Shiv Rekhi, Arash Nikoubashman, Young C. Kim, Michael P. Howard, Jeetain Mittal
bioRxiv 2022.07.04.498718; doi: https://doi.org/10.1101/2022.07.04.498718

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