Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy. Curr Opin Struct Biol 2025 Aug;93:103073
Date
06/11/2025Pubmed ID
40494166Pubmed Central ID
PMC12279019DOI
10.1016/j.sbi.2025.103073Scopus ID
2-s2.0-105007473032 (requires institutional sign-in at Scopus site) 2 CitationsAbstract
In the current age of protein structure prediction and determination, resolving the time dependence of structural transitions represents an exciting frontier. Time-resolved biophysical techniques possess the capability to directly observe dynamic structural changes of biomolecules in real time. Here, we review applications of site-directed spin labeling (SDSL) coupled with electron paramagnetic resonance (EPR) spectroscopy that cover a broad range of protein dynamics, from backbone fluctuations on the ps-ns timescale to protein complex assembly formation on the ms-s timescale. Recent developments in SDSL EPR methods allow for direct investigation of protein conformational exchange kinetics on the important μs-ms timescale, providing the time axis for structural transitions needed to define molecular mechanisms of complex biological phenomena.
Author List
Brennan PC, Grosskopf JD, Garces AM, Trier CL, Lerch MTAuthors
Alexander M. Garces Postdoctoral Researcher in the Biophysics department at Medical College of WisconsinMichael Lerch PhD Associate Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Electron Spin Resonance SpectroscopyKinetics
Protein Conformation
Proteins
Spin Labels
