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Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule

Lydia H Manger1, Alexander K Foote1, Sharla L Wood1

  • 1Department of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI, 53706, USA.

Angewandte Chemie (International Ed. in English)
|October 25, 2017
PubMed
Summary

Intrinsically disordered proteins like tau can adopt diverse structures. Using an anti-Brownian electrokinetic (ABEL) trap, researchers observed distinct conformational states in single tau proteins, revealing insights into their flexibility.

Keywords:
biophysicsfluorescence spectroscopymicrofluidicsprotein structuressingle-molecule studies

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Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs), including tau protein, exhibit dynamic conformational heterogeneity in solution.
  • This conformational diversity poses challenges for traditional solution-phase structural characterization.

Purpose of the Study:

  • To investigate the conformational landscape of single tau proteins in solution.
  • To overcome limitations in studying dynamic protein structures using advanced single-molecule techniques.

Main Methods:

  • Utilized an anti-Brownian electrokinetic (ABEL) trap to immobilize and prolong observation of single tau proteins.
  • Employed fluorescence anisotropy measurements to probe the conformational states of trapped tau molecules.
  • Performed time-resolved fluorescence anisotropy to elucidate the origins of observed conformational distributions.

Main Results:

  • The fluorescence anisotropy distribution for single tau proteins was distinctly bimodal.
  • In contrast, globular proteins and individual fluorophores exhibited unimodal anisotropy distributions.
  • Time-resolved measurements indicated the bimodal distribution arises from two distinct families of tau conformations with differing compaction states.

Conclusions:

  • The anti-Brownian electrokinetic (ABEL) trap enables detailed analysis of single intrinsically disordered protein conformations.
  • Tau protein exists in at least two distinct conformational states in solution, characterized by different degrees of compaction.
  • This study provides a novel approach for characterizing the structural dynamics of IDPs.