Abstract
When a nitroxide radical is bound to a protein in solution, the shape of its spectrum and its relaxation properties depend on its interactions with its environment. These “paramagnetic probes” can be used to study structural transitions in proteins, which are very important phenomena which are currently poorly understood. By labelling an appropriately selected site, it is possible, for example, to monitor conformational changes in an enzyme induced by its interaction with its physiological partners. It is also possible to draw a “mobility map” to identify the domain involved in folding of an “intrinsically disordered protein” induced by its interaction with another protein.
Access provided by Autonomous University of Puebla. Download to read the full chapter text
Chapter PDF
Similar content being viewed by others
References
Aloulou A. et al. (2006) Biochimica et Biophysica Acta 1761: 995-1013.
Altenbach C. et al. (1989) Biochemistry 28: 7806-7812.
Altenbach C. et al. (2005) Biophysical Journal 89: 2103-2112.
Altenbach C. et al. (1994) Proceeding of the National Academy of Sciences of the USA 91: 1667-1671.
Altenbach C. et al. (2008) Proceeding of the National Academy of Sciences of the USA 105: 7439-7444.
Altenbach C. et al. (1990) Science 248: 1088-1092.
Barnes J.P. et al. (1999) Biophysical Journal 76: 3298-3306.
Belle V. et al. (2007) Biochemistry 46: 2205-2214.
Belle V. et al. (2008) Proteins: Structure, Function and Bioinformatics 73: 973-988.
Belle V. et al. (2009) « Assessing Structures and Conformations of Intrinsically Disordered Proteins » in Site-directed spin labeling EPR spectroscopy, Uversky V.N. ed., John Wiley and Sons, New Jersey.
Bezzine S. et al. (1999) Biochemistry 38: 5499-5510.
Bourhis J.M. et al. (2006) Virology 344: 94-110.
Bourhis J.M. et al. (2005) Protein Science 14: 1975-1992.
Bridges M.D. et al. (2010) Applied Magnetic Resonance 37: 363-390.
Budil D.E. et al. (1996) Journal of Magnetic Resonance Series A 120: 155-189.
Columbus L. & Hubbell W.L. (2002) Trends in Biochemical Sciences 27: 288-295.
Columbus L. et al. (2001) Biochemistry 40: 3828-3846.
Doebber M. et al. (2008) Journal of Biological Chemistry 283: 28691-28701.
Drescher M. et al. (2008) Journal of the American Chemical Society 130: 7796-7797.
Dunker A.K. et al. (2005) FEBS Journal 272: 5129-5148.
Dyson H.J. & Wright P.E. (2002) Current Opinion in Structural Biology 12: 54-60.
Dyson H.J. & Wright P.E. (2005) Nature Reviews Molecular Cell Biology 6: 197-208.
Fanucci G.E. & Cafiso D.S. (2006) Current Opinion in Structural Biology 16: 644-653.
Fanucci G.E. et al. (2003) Biochemistry 42: 1391-1400.
Fink A.L. (2005) Current Opinion in Structural Biology 15: 35-41.
Fleissner M.R. et al. (2009) Protein Science 18: 893-908.
Freed J.H. (1976) « Theory of slow tumbling ESR spectra for nitroxides » in Spin labeling: theory and applications, Berliner L. J., ed., Academic Press, New York.
Goldman A. et al. (1972) Journal of Chemical Physics 56: 716-735.
Griffith O.H. & McConnell H.M. (1966) Proceeding of the National Academy of Sciences of the USA 55: 8-11.
Guo Z.F. et al. (2008) Protein Science 17: 228-239.
Guo Z.F. et al. (2007) Protein Science 16: 1069-1086.
Haas D.A. et al. (1993) Biophysical Journal 64: 594-604.
Hubbell W.L. et al. (1998) Current Opinion in Structural Biology 8: 649-656.
Hubbell W.L. et al. (1996) Structure 4: 779-783.
Jeschke G. (2002) ChemPhysChem 3: 927-932.
Jeschke G. et al. (2005) Journal of Biological Chemistry 280: 18623-18630.
Jeschke G. et al. (2006) Applied Magnetic Resonance 30: 473-498.
Johansson K. et al. (2003) Journal of Biological Chemistry 278: 44567-44573.
Kaplan R.S. et al. (2000) Biochemistry 39: 9157-9163.
Karlin D. et al. (2002) Virology 302: 420-432.
Kavalenka A. et al. (2010) Biophysical Journal 98: 1055-1064.
Kim M. et al. (2007) Proceeding of the National Academy of Sciences of the USA 104: 11975-11980.
Kingston R.L. et al. (2004) Proceeding of the National Academy of Sciences of the USA 101: 8301-8306.
Klare J.P. & Steinhoff H.J. (2009) Photosynthesis Research 102: 377-390.
Klug C.S. et al. (1998) Biochemistry 37: 9016-9023.
Klug C.S. & Feix J.B. (2008) Biophysical Tools for Biologists Vol 1 in Vitro Techniques 84: 617-658.
Kreimer D.I. et al. (1994) Proceeding of the National Academy of Sciences of the USA 91: 12145-12149.
Langen R. et al. (2000) Biochemistry 39: 8396-8405.
Lin Y. et al. (1998) Science 279: 1925-1929.
Longhi S. et al. (2003) Journal of Biological Chemistry 278: 18638-18648.
Marsh D. et al. (2006) Biophysical Journal 90: 49-51.
Marsh D. et al. (2002) Chemistry and Physics of Lipids 116: 93-114.
Mchaourab H.S. et al. (1996) Biochemistry 35: 7692-7704.
Merianos H.J. et al. (2000) Nature Structural Biology 7: 205-209.
Morin B. et al. (2006) Journal of Physical Chemistry B 110: 20596-20608.
Pannier M. et al. (2000) Journal of Magnetic Resonance 142: 331-340.
Perozo E. et al. (1999) Science 285: 73-78.
Pistolesi S. et al. (2006) Biophysical Chemistry 123: 49-57.
Pyka J. et al. (2005) Biophysical Journal 89: 2059-2068.
Qu K. et al. (1997) Biochemistry 36: 2884-2897.
Rabenstein M.D. & Sgin Y.K. (1995) Proceeding of the National Academy of Sciences of the USA 92: 8239-8243.
Ranaldi S. et al. (2010) Biochemistry 49: 2140-2149.
Ranaldi S. et al. (2009) Biochemistry 48: 630-638.
Steinhoff H.J. et al. (1994) Science 266: 105-107.
Steinhoff H.J. et al. (1997) Biophysical Journal 73: 3287-3298.
Stoll S. & Schweiger A. (2006) Journal of Magnetic Resonance 178: 42-55.
Jones T.J. et al. (1965) Proceeding of the National Academy of Sciences of the USA 54: 1010-1017.
Stopar D. et al. (2005) Journal of Chemical Information and Modeling 45: 1621-1627.
Stopar D. et al. (2006) Biophysical Journal 91: 3341-3348.
Strancar J. et al. (2005) Journal of Chemical Information and Modeling 45: 394-406.
Sugata K. et al. (2009) Journal of Molecular Biology 386: 626-636.
Thirstrup K. et al. (1993) FEBS Letters 327: 79-84.
Thorgeirsson T.E. et al. (1997) Journal of Molecular Biology 273: 951-957.
Timofeev V.P. & Tsetlin V.I. (1983) Biophysics of Structure and Mechanisms 10: 93-108.
Tompa P. (2002) Trends in Biochemical Sciences 27: 527-533.
Tsai C.D. et al. (2001) Critical Reviews in Biochemistry and Molecular Biology 36: 399-433.
Uversky V.N. et al. (2005) Journal of Molecular Recognition 18: 343-384.
van Tilbeurgh H. et al. (1992) Nature 359: 159-162.
van Tilbeurgh H. et al. (1993) Journal of Molecular Biology 229: 552-554.
Volume 1: Bertrand P. (2020) Electron Paramagnetic Resonance Spectroscopy - Fundamentals, Springer, Heidelberg.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2020 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Belle, V., Fournel, A. (2020). Using Paramagnetic Probes to Study Structural Transitions in Proteins. In: Electron Paramagnetic Resonance Spectroscopy. Springer, Cham. https://doi.org/10.1007/978-3-030-39668-8_8
Download citation
DOI: https://doi.org/10.1007/978-3-030-39668-8_8
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-39667-1
Online ISBN: 978-3-030-39668-8
eBook Packages: Physics and AstronomyPhysics and Astronomy (R0)