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Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET.

William N Zagotta1, Eric G B Evans1,2, Pierce Eggan1

  • 1Department of Physiology and Biophysics, University of Washington, Seattle, Washington 98195.

Biorxiv : the Preprint Server for Biology
|October 24, 2023
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Summary

We developed time-resolved transition metal Förster resonance energy transfer (tmFRET) to study protein allostery. This method accurately measures protein distance distributions and conformational heterogeneity, advancing our understanding of biological regulation.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Proteins undergo conformational changes crucial for biological functions.
  • Protein allostery involves ligand-induced rearrangements.
  • Transition metal Förster resonance energy transfer (tmFRET) probes protein dynamics.

Conclusions:

  • Time-resolved tmFRET is a versatile tool for studying protein allostery and dynamics.
  • The approach provides insights into conformational landscapes and regulatory mechanisms.
  • Metal-bipyridyl compounds offer a robust method for biophysical studies.