EPR in protein science : intrinsically disordered proteins - PubMed

Review

EPR in protein science : intrinsically disordered proteins

Malte Drescher. Top Curr Chem. 2012.

Abstract

Intrinsically disordered proteins (IDPs) form a unique protein category characterized by the absence of a well-defined structure and by remarkable conformational flexibility. Electron Paramagnetic Resonance (EPR) spectroscopy combined with site-directed spin labeling (SDSL) is amongst the most suitable methods to unravel their structure and dynamics. This review summarizes the tremendous methodological developments in the area of SDSL EPR and its applications in protein research. Recent results on the intrinsically disordered Parkinson's disease protein α-synuclein illustrate that the method has gained increasing attention in IDP research. SDSL EPR has now reached a level where broad application in this rapidly advancing field is feasible.

Similar articles

• Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy.

  Longhi S, Belle V, Fournel A, Guigliarelli B, Carrière F. Longhi S, et al. J Pept Sci. 2011 May;17(5):315-28. doi: 10.1002/psc.1344. Epub 2011 Feb 24. J Pept Sci. 2011. PMID: 21351321 Review.

• Methods and applications of site-directed spin labeling EPR spectroscopy.

  Klug CS, Feix JB. Klug CS, et al. Methods Cell Biol. 2008;84:617-58. doi: 10.1016/S0091-679X(07)84020-9. Methods Cell Biol. 2008. PMID: 17964945

• Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR Spectroscopy.

  Martinho M, Allegro D, Etienne E, Lohberger C, Bonucci A, Belle V, Barbier P. Martinho M, et al. Methods Mol Biol. 2024;2754:55-75. doi: 10.1007/978-1-0716-3629-9_3. Methods Mol Biol. 2024. PMID: 38512660

• Site-directed spin labeling EPR spectroscopy in protein research.

  Klare JP. Klare JP. Biol Chem. 2013 Oct;394(10):1281-300. doi: 10.1515/hsz-2013-0155. Biol Chem. 2013. PMID: 23912220 Review.

• Combining high-field EPR with site-directed spin labeling reveals unique information on proteins in action.

  Möbius K, Savitsky A, Wegener C, Plato M, Fuchs M, Schnegg A, Dubinskii AA, Grishin YA, Grigor'ev IA, Kühn M, Duché D, Zimmermann H, Steinhoff HJ. Möbius K, et al. Magn Reson Chem. 2005 Nov;43 Spec no.:S4-S19. doi: 10.1002/mrc.1690. Magn Reson Chem. 2005. PMID: 16235212

Cited by

• Advances in studying protein disorder with solid-state NMR.

  Siemer AB. Siemer AB. Solid State Nucl Magn Reson. 2020 Apr;106:101643. doi: 10.1016/j.ssnmr.2020.101643. Epub 2020 Jan 12. Solid State Nucl Magn Reson. 2020. PMID: 31972419 Free PMC article. Review.

• Digested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013).

  Uversky VN. Uversky VN. Intrinsically Disord Proteins. 2013 Apr 1;1(1):e25496. doi: 10.4161/idp.25496. eCollection 2013 Jan-Dec. Intrinsically Disord Proteins. 2013. PMID: 28516015 Free PMC article. Review.

• Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin.

  Kurzbach D, Platzer G, Schwarz TC, Henen MA, Konrat R, Hinderberger D. Kurzbach D, et al. Biochemistry. 2013 Aug 6;52(31):5167-75. doi: 10.1021/bi400502c. Epub 2013 Jul 24. Biochemistry. 2013. PMID: 23848319 Free PMC article.

• Alpha-synuclein fragments trigger distinct aggregation pathways.

  Chakroun T, Evsyukov V, Nykänen NP, Höllerhage M, Schmidt A, Kamp F, Ruf VC, Wurst W, Rösler TW, Höglinger GU. Chakroun T, et al. Cell Death Dis. 2020 Feb 3;11(2):84. doi: 10.1038/s41419-020-2285-7. Cell Death Dis. 2020. PMID: 32015326 Free PMC article.

• α-Synuclein and biological membranes: the danger of loving too much.

  Mansueto S, Fusco G, De Simone A. Mansueto S, et al. Chem Commun (Camb). 2023 Jul 13;59(57):8769-8778. doi: 10.1039/d3cc01682j. Chem Commun (Camb). 2023. PMID: 37345454 Free PMC article. Review.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Springer