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Electron paramagnetic resonance spectroscopy

Biological applications

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Abstract

Recently, electron paramagnetic resonance (EPR) spectroscopy has emerged as a powerful tool to study the structure and dynamics of biological macromolecules such as proteins, protein aggregates, RNA and DNA. It is used in combination with molecular modelling to study complex systems such as soluble proteins, membrane proteins and protein aggregates like amyloid fibrils and oligomers. This article describes how the EPR technique can be used to elucidate the structural reorganization taking place in a membrane-bound protein by taking a few examples from the literature including some of the earlier works of the author.

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Suggested Reading

  1. W L Hubbell, A Gross, R Langen and M A Lietzow, Recent advances in site-directed spin labelling of proteins, Curr. Opin. Struct. Biol., Vol.8, pp.649–56, 1998.

    Article  Google Scholar 

  2. M Margittai and R Langen, Spin labelling analysis of amyloids and other protein aggregates, Methods in Enzymology, Vol.43, pp.123–139, 2006.

    Google Scholar 

  3. W L Hubbell, H. S Mchaourab, C Altenbach and M A Lietzow, Watching proteins move using site-directed spin labelling, Structure, Vol.4, pp.779–783, 1996.

    Article  Google Scholar 

  4. C Altenbach, D A Greenhalgh, H G Khorana and W L Hubbell, A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin, Proc Natl Acad Sci USA, Vol.91, No.5, pp.1667–1671, 1994.

    Article  Google Scholar 

  5. B G Hegde, J M Isas, G Zampighi, H T Haigler, and R Langen, A novel calcium-independent peripheral membrane-bound form of annexin B12, Biochemistry, Vol.45, pp.934–942, 2006.

    Article  Google Scholar 

  6. M D Rabenstein and Y K Shin, Determination of the distance between two spin labels attached to a macromolecule, Proc. Natl Acad. Sci. USA Vol.92, pp.8239–43, 1995.

    Article  Google Scholar 

  7. C Altenbach, K J Oh, R J Trabanino, K Hideg and WL Hubbell, Estimation of inter-residue distances in spin labelled proteins at physiological temperatures: Experimental strategies and practical limitations, Biochemistry, Vol.40, pp.5471–15482, 2001.

    Google Scholar 

  8. G Jeschke and Y Polyhach, Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance, Phys. Chem. Chem. Phys., Vol.9, pp.895–1910, 2007.

    Article  Google Scholar 

  9. M Pannier, S Veit, A Godt, G Jeschke and H W Spiess Dead-time free measurement of dipole–dipole interactions between electron spins, J. Magn. Reson. Vol.142 pp.331–340, 2000.

    Article  Google Scholar 

  10. H T McMahon and J L Gallop, Membrane curvature and mechanisms of dynamic cell membrane remodelling, Nature, Vol.38, pp.590–596, 2005.

    Article  Google Scholar 

  11. J Zimmerberg and M M Kozlov, How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. Vo.7, pp9–19, 2006.

    Article  Google Scholar 

  12. J L Gallop and H T McMahon, BAR domains and membrane curvature: bringing your curves to the BAR, Biochem. Soc. Symp., Vol.72, pp.223–231, 2005.

    Article  Google Scholar 

  13. J L Gallop, C C Jao, M H Kent, P J Butler, P R Evans, R Langen and H T McMahon, Mechanism of endophilin N-BAR domain mediated membrane curvature, EMBO J., Vol.25, pp.2898–2910, 2006.

    Article  Google Scholar 

  14. C C Jao, B GHegde, J L Gallop, P B Hegde, H T McMahon, I S Haworth and R Langen, Roles of amphipathic helices and BAR domain of endophilin in membrane curvature generation, J Biol Chem., Vol.285, pp.20164–70, 2010.

    Article  Google Scholar 

  15. M Ambroso, B G Hegde and R Langen, Endophilin A1 induces different membrane shapes using a conformational switch that is regulated by phosphorylation, Proc. Natl. Acad. Sci., USA, Vol.111(19), pp.6982–6987, 2014.

    Article  Google Scholar 

  16. G Jeschke, V Chechik, P Ionita, A Godt, H Zimmermann, J Banham, C R Timmel, D Hilger and H Jung, DeerAnalysis 2006 - AComprehensive Software Package for Analyzing Pulsed ELDOR Data, Appl. Magn. Reson., Vol.30, pp.473–498, 2006.

    Article  Google Scholar 

  17. S Bedrood, Y Li, JM Isas, B GHegde, U Baxa, I S Haworth and R Langen, Fibril Structure of Human Islet Amyloid Polypeptide. J Biol Chem., Vol.287, pp. 5235–41, 2012.

    Article  Google Scholar 

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Authors and Affiliations

  1. Department of Physics, Rani Channamma University, Vidyasangama, PBNH-4, Belagavi Karnataka, 591 156, India

    B. G. Hegde

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  1. B. G. Hegde
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Correspondence to B. G. Hegde.

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B G Hegde is an Associate Professor in the Department of Physics, Rani Channamma University, Belagavi, Karnataka. His research interests are peptide membrane interaction studies using biophysical techniques and study of colossal magnetoresistance (CMR) properties in manganite nanoparticles.

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Hegde, B.G. Electron paramagnetic resonance spectroscopy. Reson 20, 1017–1032 (2015). https://doi.org/10.1007/s12045-015-0270-8

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  • DOI: https://doi.org/10.1007/s12045-015-0270-8

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