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Volumn 752, Issue , 2011, Pages 73-96

Distance Measurements by Continuous Wave EPR Spectroscopy to Monitor Protein Folding

Author keywords

Continu ous wave EPR spectroscopy; Dipolar interaction; Electron paramagnetic resonance; Interspin distances; Protein folding; Site directed mutagenesis; Site directed spin labeling

Indexed keywords

NITROGEN OXIDE; NITROXYL; PROTEIN;

EID: 79960980463     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-60327-223-0_6     Document Type: Chapter
Times cited : (15)

References (45)
  • 1
    • 0028108981 scopus 로고
    • Investigation of structure and dynamics in membrane proteins using site-directed spin labeling
    • Hubbell, W. L., and Altenbach, C. (1994) Investigation of structure and dynamics in membrane proteins using site-directed spin labeling. Curr Opin Struct Biol. 4, 566–573.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 566-573
    • Hubbell, W.L.1    Altenbach, C.2
  • 2
  • 3
    • 0030586056 scopus 로고    scopus 로고
    • Watching proteins move using site-directed spin labeling
    • Hubbell, W. L., McHaourab, H. S., Altenbach, C., and Lietzow, M. A. (1996) Watching proteins move using site-directed spin labeling. Structure. 4, 779–783.
    • (1996) Structure , vol.4 , pp. 779-783
    • Hubbell, W.L.1    McHaourab, H.S.2    Altenbach, C.3    Lietzow, M.A.4
  • 4
    • 0030693909 scopus 로고    scopus 로고
    • Mapping of the residues involved in a proposed beta-strand located in the ferric enterobactin receptor FepA using site-directed spin-labeling
    • Klug, C. S., Su, W., and Feix, J. B. (1997) Mapping of the residues involved in a proposed beta-strand located in the ferric enterobactin receptor FepA using site-directed spin-labeling. Biochemistry. 36, 13027–13033.
    • (1997) Biochemistry , vol.36 , pp. 13027-13033
    • Klug, C.S.1    Su, W.2    Feix, J.B.3
  • 5
    • 0036606899 scopus 로고    scopus 로고
    • A new spin on protein dynamics
    • Columbus, L., and Hubbell, W. L. (2002) A new spin on protein dynamics. Trends Biochem Sci. 27, 288–295.
    • (2002) Trends Biochem Sci , vol.27 , pp. 288-295
    • Columbus, L.1    Hubbell, W.L.2
  • 6
    • 35648987515 scopus 로고    scopus 로고
    • Practical Pulsed Dipolar ESR (DEER), in Biological Magnetic Resonance (Hemminga, M., and Berliner, L
    • Springer, New York
    • Fajer, P., Brown, L., and Song, L. (2007) Practical Pulsed Dipolar ESR (DEER), in Biological Magnetic Resonance (Hemminga, M., and Berliner, L., Eds.), Vol. 27, Springer, New York, pp. 95–128.
    • (2007) Eds.) , vol.27 , pp. 95-128
    • Fajer, P.1    Brown, L.2    Song, L.3
  • 7
    • 34447305495 scopus 로고    scopus 로고
    • Attaching a spin to a protein-site-directed spin labeling in structural biology
    • Czogalla, A., Pieciul, A., Jezierski, A., and Sikorski, A. F. (2007) Attaching a spin to a protein-site-directed spin labeling in structural biology. Acta Biochim Pol. 54, 235–244.
    • (2007) Acta Biochim Pol , vol.54 , pp. 235-244
    • Czogalla, A.1    Pieciul, A.2    Jezierski, A.3    Sikorski, A.F.4
  • 8
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in biomacromolecules by EPR spectroscopy
    • Schiemann, O., and Prisner, T. F. (2007) Long-range distance determinations in biomacromolecules by EPR spectroscopy. Q Rev Biophys. 40, 1–53.
    • (2007) Q Rev Biophys , vol.40 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 9
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci, G. E., and Cafiso, D. S. (2006) Recent advances and applications of site-directed spin labeling. Curr Opin Struct Biol. 16, 644–653.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 10
    • 8344224484 scopus 로고    scopus 로고
    • Inter-and intramolecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction
    • Steinhoff, H. J. (2004) Inter-and intramolecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction. Biol Chem. 385, 913–920.
    • (2004) Biol Chem , vol.385 , pp. 913-920
    • Steinhoff, H.J.1
  • 12
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol. 7, 735–739.
    • (2000) Nat Struct Biol , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 13
    • 0032985839 scopus 로고    scopus 로고
    • Nitroxide spin–spin interactions: Applications to protein structure and dynamics
    • Hustedt, E. J., and Beth, A. H. (1999) Nitroxide spin–spin interactions: applications to protein structure and dynamics. Annu Rev Biophys Biomol Struct. 28, 129–153.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 129-153
    • Hustedt, E.J.1    Beth, A.H.2
  • 14
    • 0033516494 scopus 로고    scopus 로고
    • Structural rearrangements underlying K+−channel activation gating
    • Perozo, E., Cortes, D. M., and Cuello, L. G. (1999) Structural rearrangements underlying K+−channel activation gating. Science. 285, 73–78.
    • (1999) Science , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 15
    • 34548729760 scopus 로고    scopus 로고
    • Nanometer distance measurements in RNA using site-directed spin labeling
    • Cai, Q., Kusnetzow, A. K., Hideg, K., Price, E. A., Haworth, I. S., and Qin, P. Z. (2007) Nanometer distance measurements in RNA using site-directed spin labeling. Biophys J. 93, 2110–2117.
    • (2007) Biophys J , vol.93 , pp. 2110-2117
    • Cai, Q.1    Kusnetzow, A.K.2    Hideg, K.3    Price, E.A.4    Haworth, I.S.5    Qin, P.Z.6
  • 16
    • 0036789941 scopus 로고    scopus 로고
    • Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance
    • Brown, L. J., Sale, K. L., Hills, R., Rouviere, C., Song, L., Zhang, X., and Fajer, P. G. (2002) Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance. Proc Natl Acad Sci U S A. 99, 12765–12770.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12765-12770
    • Brown, L.J.1    Sale, K.L.2    Hills, R.3    Rouviere, C.4    Song, L.5    Zhang, X.6    Fajer, P.G.7
  • 17
    • 0035066645 scopus 로고    scopus 로고
    • The neuronal t-SNARE complex is a parallel four-helix bundle
    • Xiao, W., Poirier, M. A., Bennett, M. K., and Shin, Y. K. (2001) The neuronal t-SNARE complex is a parallel four-helix bundle. Nat Struct Biol. 8, 308–311.
    • (2001) Nat Struct Biol , vol.8 , pp. 308-311
    • Xiao, W.1    Poirier, M.A.2    Bennett, M.K.3    Shin, Y.K.4
  • 18
    • 34548359337 scopus 로고    scopus 로고
    • Investigation of alpha-synuclein fibril structure by site-directed spin labeling
    • Chen, M., Margittai, M., Chen, J., and Langen, R. (2007) Investigation of alpha-synuclein fibril structure by site-directed spin labeling. J Biol Chem. 282, 24970–24979.
    • (2007) J Biol Chem , vol.282 , pp. 24970-24979
    • Chen, M.1    Margittai, M.2    Chen, J.3    Langen, R.4
  • 19
    • 33646942808 scopus 로고    scopus 로고
    • Visual arrestin binding to microtubules involves a distinct conformational change
    • Hanson, S. M., Francis, D. J., Vishnivetskiy, S. A., Klug, C. S., and Gurevich, V. V. (2006) Visual arrestin binding to microtubules involves a distinct conformational change. J Biol Chem. 281, 9765–9772.
    • (2006) J Biol Chem , vol.281 , pp. 9765-9772
    • Hanson, S.M.1    Francis, D.J.2    Vishnivetskiy, S.A.3    Klug, C.S.4    Gurevich, V.V.5
  • 20
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • Radzwill, N., Gerwert, K., and Steinhoff, H. J. (2001) Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin. Biophys J. 80, 2856–2866.
    • (2001) Biophys J , vol.80 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.J.3
  • 21
    • 0034671339 scopus 로고    scopus 로고
    • Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin
    • Xiao, W., Brown, L. S., Needleman, R., Lanyi, J. K., and Shin, Y. K. (2000) Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin. J Mol Biol. 304, 715–721.
    • (2000) J Mol Biol , vol.304 , pp. 715-721
    • Xiao, W.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4    Shin, Y.K.5
  • 22
    • 33646127590 scopus 로고    scopus 로고
    • Dipolar coupling between nitroxide spin labels: The development and application of a tether-in-a-cone model
    • Hustedt, E. J., Stein, R. A., Sethaphong, L., Brandon, S., Zhou, Z., and Desensi, S. C. (2006) Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model. Biophys J. 90, 340–356.
    • (2006) Biophys J , vol.90 , pp. 340-356
    • Hustedt, E.J.1    Stein, R.A.2    Sethaphong, L.3    Brandon, S.4    Zhou, Z.5    Desensi, S.C.6
  • 23
    • 21644446664 scopus 로고    scopus 로고
    • Explicit Treatment of Spin Labels in Modeling of Distance Constraints from Dipolar EPR and DEER
    • Sale, K., Song, L., Liu, Y. S., Perozo, E., and Fajer, P. (2005) Explicit Treatment of Spin Labels in Modeling of Distance Constraints from Dipolar EPR and DEER. J Am Chem Soc. 127, 9334–9335.
    • (2005) J am Chem Soc , vol.127 , pp. 9334-9335
    • Sale, K.1    Song, L.2    Liu, Y.S.3    Perozo, E.4    Fajer, P.5
  • 24
    • 67649392930 scopus 로고    scopus 로고
    • SDS Polyacrylamide Gel Electrophoresis of Proteins
    • Walker, J. M., Ed.), Humana, Totowa, NJ
    • Walker, J. M. (2002) SDS Polyacrylamide Gel Electrophoresis of Proteins, in The Protein Protocols Handbook (Walker, J. M., Ed.), Humana, Totowa, NJ, pp. 61–67.
    • (2002) The Protein Protocols Handbook , pp. 61-67
    • Walker, J.M.1
  • 25
    • 0035951097 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306–319 at the cytoplasmic end of helix TM7 and in helix H8
    • Altenbach, C., Cai, K., Klein-Seetharaman, J., Khorana, H. G., and Hubbell, W. L. (2001) Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306–319 at the cytoplasmic end of helix TM7 and in helix H8. Biochemistry. 40, 15483–15492.
    • (2001) Biochemistry , vol.40 , pp. 15483-15492
    • Altenbach, C.1    Cai, K.2    Klein-Seetharaman, J.3    Khorana, H.G.4    Hubbell, W.L.5
  • 26
    • 0032575512 scopus 로고    scopus 로고
    • Membrane-mediated assembly of annexins studied by site-directed spin labeling
    • Langen, R., Isas, J. M., Luecke, H., Haigler, H. T., and Hubbell, W. L. (1998) Membrane-mediated assembly of annexins studied by site-directed spin labeling. J Biol Chem. 273, 22453–22457.
    • (1998) J Biol Chem , vol.273 , pp. 22453-22457
    • Langen, R.1    Isas, J.M.2    Luecke, H.3    Haigler, H.T.4    Hubbell, W.L.5
  • 27
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: Implications for the interpretation of EPR spectra in terms of structure
    • Langen, R., Oh, K. J., Cascio, D., and Hubbell, W. L. (2000) Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. Biochemistry. 39, 8396–8405.
    • (2000) Biochemistry , vol.39 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4
  • 28
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • McHaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry. 35, 7692–7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • McHaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 29
    • 2642701712 scopus 로고    scopus 로고
    • Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy
    • Perozo, E., Cortes, D. M., and Cuello, L. G. (1998) Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy. Nat Struct Biol. 5, 459–469.
    • (1998) Nat Struct Biol , vol.5 , pp. 459-469
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 30
    • 0012382504 scopus 로고    scopus 로고
    • Protein Determination by UV Absorption
    • Walker, J. M., Ed.), Humana, Totowa, NJ
    • Aitken, A., and Learmonth, M. P. (2002) Protein Determination by UV Absorption, in The Protein Protocols Handbook (Walker, J. M., Ed.), Humana, Totowa, NJ, pp. 3–6.
    • (2002) The Protein Protocols Handbook , pp. 3-6
    • Aitken, A.1    Learmonth, M.P.2
  • 31
    • 0001824671 scopus 로고    scopus 로고
    • The Lowry Method for Protein Quantitation
    • Walker, J. M., Ed.), Humana, Totowa, NJ
    • Waterborg, J. H. (2002) The Lowry Method for Protein Quantitation, in The Protein Protocols Handbook (Walker, J. M., Ed.), Humana, Totowa, NJ, pp. 7–9.
    • (2002) The Protein Protocols Handbook , pp. 7-9
    • Waterborg, J.H.1
  • 32
    • 0042926861 scopus 로고    scopus 로고
    • The Bicinchoninic Acid (BCA) Assay for Protein Quantitation
    • Walker, J. M., Ed.), Humana, Totowa, NJ
    • Walker, J. M. (2002) The Bicinchoninic Acid (BCA) Assay for Protein Quantitation, in The Protein Protocols Handbook (Walker, J. M., Ed.), Humana, Totowa, NJ, pp. 11–14.
    • (2002) The Protein Protocols Handbook , pp. 11-14
    • Walker, J.M.1
  • 33
    • 0002043677 scopus 로고    scopus 로고
    • The Bradford Method for Protein Quantitation
    • Walker, J. M., Ed.), Humana, Totowa, NJ
    • Kruger, N. J. (2002) The Bradford Method for Protein Quantitation, in The Protein Protocols Handbook (Walker, J. M., Ed.), Humana, Totowa, NJ, pp. 15–21.
    • (2002) The Protein Protocols Handbook , pp. 15-21
    • Kruger, N.J.1
  • 34
    • 0030950516 scopus 로고    scopus 로고
    • Molecular distances from dipolar coupled spin-labels: The global analysis of multifrequency continuous wave electron paramagnetic resonance data
    • Hustedt, E. J., Smirnov, A. I., Laub, C. F., Cobb, C. E., and Beth, A. H. (1997) Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data. Biophys J. 72, 1861–1877.
    • (1997) Biophys J , vol.72 , pp. 1861-1877
    • Hustedt, E.J.1    Smirnov, A.I.2    Laub, C.F.3    Cobb, C.E.4    Beth, A.H.5
  • 35
    • 0030781782 scopus 로고    scopus 로고
    • Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the X-ray structure
    • Steinhoff, H. J., Radzwill, N., Thevis, W., Lenz, V., Brandenburg, D., Antson, A., Dodson, G., and Wollmer, A. (1997) Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure. Biophys J. 73, 3287–3298.
    • (1997) Biophys J , vol.73 , pp. 3287-3298
    • Steinhoff, H.J.1    Radzwill, N.2    Thevis, W.3    Lenz, V.4    Brandenburg, D.5    Antson, A.6    Dodson, G.7    Wollmer, A.8
  • 36
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein, M. D., and Shin, Y. K. (1995) Determination of the distance between two spin labels attached to a macromolecule. Proc Natl Acad Sci U S A. 92, 8239–8243.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 37
    • 0037025372 scopus 로고    scopus 로고
    • The four-helix bundle of the neuronal target membrane SNARE complex is neither disordered in the middle nor uncoiled at the C-terminal region
    • Zhang, F., Chen, Y., Kweon, D. H., Kim, C. S., and Shin, Y. K. (2002) The four-helix bundle of the neuronal target membrane SNARE complex is neither disordered in the middle nor uncoiled at the C-terminal region. J Biol Chem. 277, 24294–24298.
    • (2002) J Biol Chem , vol.277 , pp. 24294-24298
    • Zhang, F.1    Chen, Y.2    Kweon, D.H.3    Kim, C.S.4    Shin, Y.K.5
  • 38
    • 0035951101 scopus 로고    scopus 로고
    • Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations
    • Altenbach, C., Oh, K. J., Trabanino, R. J., Hideg, K., and Hubbell, W. L. (2001) Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. Biochemistry. 40, 15471–15482.
    • (2001) Biochemistry , vol.40 , pp. 15471-15482
    • Altenbach, C.1    Oh, K.J.2    Trabanino, R.J.3    Hideg, K.4    Hubbell, W.L.5
  • 39
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • McHaourab, H. S., Oh, K. J., Fang, C. J., and Hubbell, W. L. (1997) Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry. 36, 307–316.
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • McHaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 40
    • 0006568240 scopus 로고    scopus 로고
    • EPR Spectroscopic Ruler: The Deconvolution Method and its Applications, in Biological Magnetic Resonance: Distance Measurements in Biological Systems by EPR (Berliner, L. J., Eaton, S. S., and Eaton, G. R
    • Kluwer Academic/Plenum Publishers, New York
    • Xiao, W., and Shin, Y.-K. (2000) EPR Spectroscopic Ruler: The Deconvolution Method and its Applications, in Biological Magnetic Resonance: Distance Measurements in Biological Systems by EPR (Berliner, L. J., Eaton, S. S., and Eaton, G. R., Eds.), Vol. 19, Kluwer Academic/Plenum Publishers, New York, pp. 249–276.
    • (2000) Eds.) , vol.19 , pp. 249-276
    • Xiao, W.1    Shin, Y.-K.2
  • 41
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • Perozo, E., Cortes, D. M., Sompornpisut, P., Kloda, A., and Martinac, B. (2002) Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature. 418, 942–948.
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 42
    • 0034998819 scopus 로고    scopus 로고
    • Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II
    • Persson, M., Harbridge, J. R., Hammarstrom, P., Mitri, R., Martensson, L. G., Carlsson, U., Eaton, G. R., and Eaton, S. S. (2001) Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II. Biophys J. 80, 2886–2897.
    • (2001) Biophys J , vol.80 , pp. 2886-2897
    • Persson, M.1    Harbridge, J.R.2    Hammarstrom, P.3    Mitri, R.4    Martensson, L.G.5    Carlsson, U.6    Eaton, G.R.7    Eaton, S.S.8
  • 44
    • 0030732692 scopus 로고    scopus 로고
    • Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the alpha-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface
    • McHaourab, H. S., Berengian, A. R., and Koteiche, H. A. (1997) Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the alpha-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface. Biochemistry. 36, 14627–14634.
    • (1997) Biochemistry , vol.36 , pp. 14627-14634
    • McHaourab, H.S.1    Berengian, A.R.2    Koteiche, H.A.3
  • 45
    • 24144471057 scopus 로고    scopus 로고
    • Site directed spin labelling and pulsed dipolar electron paramagnetic resonance (double electron-electron resonance) of force activation in muscle
    • Fajer, P. G. (2005) Site directed spin labelling and pulsed dipolar electron paramagnetic resonance (double electron-electron resonance) of force activation in muscle. J Phys Condens Matter. 17, S1459–S1469.
    • (2005) J Phys Condens Matter , vol.17 , pp. S1459-S1469
    • Fajer, P.G.1


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