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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Translocation of polyampholytes and intrinsically disordered proteins⋆
1Institut Charles Sadron CNRS-Unistra, 6 rue Boussingault, 67083, Strasbourg Cedex, France. albert.johner@ics-cnrs.unistra.fr.
Synthetic polyampholytes and intrinsically disordered proteins exhibit distinct translocation behaviors through pores. Disorder in synthetic polyampholytes slows translocation, while protein translocation depends on the engaged end.
Area of Science:
- Polymer Physics
- Biophysics
- Statistical Mechanics
Background:
- Polyampholytes are polymers with both positive and negative charges.
- Intrinsically disordered proteins (IDPs) can mimic polyampholytes in denatured states.
- Understanding polymer and protein translocation through nanopores is crucial for various applications.
Purpose of the Study:
- To investigate the electric-field-driven translocation of synthetic polyampholytes and IDPs through a pore.
- To analyze the impact of charge sequence disorder on synthetic polyampholytes.
- To examine how the engaged end affects translocation and rejection rates of IDPs.
Main Methods:
- Theoretical modeling and simulation of polymer translocation.
- Analysis of translocation dynamics, including speed, rejection time, and blockade time distributions.
- Comparison between synthetic polyampholytes with random charges and IDPs with defined sequences.
Main Results:
- Charge sequence disorder in synthetic polyampholytes significantly slows down translocation dynamics.
- For IDPs, translocation versus rejection rates are dependent on which terminus enters the pore first.
- Translocation speed and blockade time distributions vary for different IDP lengths and structures.
Conclusions:
- Disordered charge sequences in synthetic polyampholytes impede efficient pore translocation.
- The specific end of an IDP engaging with the pore dictates its translocation outcome.
- IDP translocation is sensitive to sequence length and structural properties, offering insights into biological transport mechanisms.
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