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Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET. | LitMetric

AI Article Synopsis

  • PELDOR/DEER and smFRET are techniques used to study the structure and conformational changes in biological molecules by measuring distances between probes.
  • This research compares the accuracy of these two methods using four proteins that change shape when binding to ligands, following standard experimental and data analysis protocols.
  • While both methods show overall accurate distance measurements, some discrepancies were found, likely due to cryoprotectants in PELDOR/DEER and interactions between labels and proteins in smFRET, revealing the unique strengths and limitations of each technique in structural biology.

Article Abstract

Pulsed electron-electron double resonance spectroscopy (PELDOR/DEER) and single-molecule Förster resonance energy transfer spectroscopy (smFRET) are frequently used to determine conformational changes, structural heterogeneity, and inter probe distances in biological macromolecules. They provide qualitative information that facilitates mechanistic understanding of biochemical processes and quantitative data for structural modelling. To provide a comprehensive comparison of the accuracy of PELDOR/DEER and smFRET, we use a library of double cysteine variants of four proteins that undergo large-scale conformational changes upon ligand binding. With either method, we use established standard experimental protocols and data analysis routines to determine inter-probe distances in the presence and absence of ligands. The results are compared to distance predictions from structural models. Despite an overall satisfying and similar distance accuracy, some inconsistencies are identified, which we attribute to the use of cryoprotectants for PELDOR/DEER and label-protein interactions for smFRET. This large-scale cross-validation of PELDOR/DEER and smFRET highlights the strengths, weaknesses, and synergies of these two important and complementary tools in integrative structural biology.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9338047PMC
http://dx.doi.org/10.1038/s41467-022-31945-6DOI Listing

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