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Related Experiment Video

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Polymer effects modulate binding affinities in disordered proteins.

Renee Vancraenenbroeck1, Yair S Harel1, Wenwei Zheng2

  • 1Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|September 7, 2019
PubMed
Summary
This summary is machine-generated.

Ionic strength affects disordered proteins by altering their structure and increasing binding affinity. This sensitivity allows protein networks to maintain robust function in changing cellular conditions.

Keywords:
collapseintrinsically disordered proteinprotein foldingprotein networksingle-molecule FRET

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Systems Biology

Background:

  • Intrinsically disordered proteins (IDPs) are crucial in regulatory networks but sensitive to environmental changes.
  • The impact of solution conditions on IDP folding-binding coupling remains unclear.

Purpose of the Study:

  • Investigate how salt concentration influences the polymer properties and binding affinities of disordered proteins.
  • Determine the functional relevance of disordered protein states in fluctuating cellular environments.

Main Methods:

  • Single-molecule Förster resonance energy transfer (smFRET) experiments.
  • Theoretical polymer physics modeling.
  • All-atom molecular dynamics simulations.

Main Results:

  • Increasing ionic strength causes surveyed disordered proteins to expand due to Debye-Hückel charge screening.
  • Pairwise protein affinities increase significantly (order of magnitude) within physiological salt ranges.
  • Changes in the disordered state account for 50% of the observed binding affinity enhancement.

Conclusions:

  • Disordered protein states possess functional relevance, impacting binding affinities.
  • Networks of homologous disordered proteins exhibit robustness in variable cellular environments.
  • Understanding IDP sensitivity to ionic strength is key for predicting network behavior.