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CW ESR spectroscopy and protein spin labeling in membrane biology.

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Title: CW ESR spectroscopy and protein spin labeling in membrane biology.
Authors: Ishola O; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States of America., Ogunbowale A; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States of America., Abdul-Rahman E; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States of America., Starr K; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States of America., Zhu P; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States of America., Borbat PP; Department of Chemistry and Chemical Biology and ACERT, Cornell University, Ithaca, NY 14853, United States of America., Georgieva ER; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States of America.
Source: Physical biology [Phys Biol] 2025 Dec 30; Vol. 23 (1). Date of Electronic Publication: 2025 Dec 30.
Publication Type: Journal Article; Review; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural
Language: English
Journal Info: Publisher: Institute of Physics Pub Country of Publication: England NLM ID: 101197454 Publication Model: Electronic Cited Medium: Internet ISSN: 1478-3975 (Electronic) Linking ISSN: 14783967 NLM ISO Abbreviation: Phys Biol Subsets: MEDLINE
Imprint Name(s): Original Publication: Bristol, UK : Institute of Physics Pub., c2004-
MeSH Terms: Membrane Proteins*/chemistry , Membrane Proteins*/metabolism , Spin Labels*, Electron Spin Resonance Spectroscopy/methods ; Lipid Bilayers/chemistry ; Humans ; Protein Conformation
Abstract: Biological membranes define cellular and organelle boundaries, and perform vital functions, providing transport, recognition, signaling, and interaction with other cells. These membranes are majorly composed of lipid bilayers and membrane proteins. Membrane proteins perform most membrane functions. Based on their localization, they are classified as integral and peripheral proteins. In this overview, we provide basic information about membrane proteins structure, conformational dynamics, and functions, and outline the methodologies used to produce highly-pure functional membrane proteins forin vitrobiophysical characterizations based on selected examples. To this end, expression of membrane proteins in a host, their extraction, purification and reconstitution in model lipid bilayers are described. Further, biophysical approaches play key role in elucidation of the structure and function of membrane proteins. Our focus here is on the technique of continuous wave electron paramagnetic/spin resonance (CW ESR) spectroscopy applied to spin-labeled membrane proteins. We describe the basic principles of membrane proteins labeling with nitroxide spin labels (paramagnetic tags) and how the CW ESR can be successfully used in elucidating the conformational dynamics of such proteins. We describe the basic principles of the CW ESR technique. The capability of this technique to characterize physiologically relevant conformational dynamics of proteins is demonstrated using two examples of CW ESR studies on spin-labeled human Tau and influenza A M2 proteins. The method is highly suitable to study physiological structure-function relationships of a broad range of proteins, and to explain the malfunctional states of proteins linked to diseases. This review is directed to the broader biophysical community with interest in molecular biophysics of biological membranes.
(Creative Commons Attribution license.)
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Grant Information: R24 GM146107 United States GM NIGMS NIH HHS
Contributed Indexing: Keywords: continuous wave electron spin resonance (CW ESR); membrane protein conformational dynamics; membrane proteins; protein spin labeling; study of membrane protein by CW ESR
Substance Nomenclature: 0 (Spin Labels)
0 (Membrane Proteins)
0 (Lipid Bilayers)
Entry Date(s): Date Created: 20251216 Date Completed: 20251230 Latest Revision: 20260816
Update Code: 20260816
PubMed Central ID: PMC13470987
DOI: 10.1088/1478-3975/ae2db1
PMID: 41401506
Database: MEDLINE
Description
ISSN:1478-3975
DOI:10.1088/1478-3975/ae2db1