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Volumn 63, Issue , 2012, Pages 419-446

DEER distance measurements on proteins

Author keywords

Electron paramagnetic resonance (EPR); Electron electron double resonance; Macromolecular movements; Membrane proteins; Spin labeling; Structure determination

Indexed keywords

BIOLOGICAL MEMBRANES; ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; PARAMAGNETIC RESONANCE; PARAMAGNETISM;

EID: 84859888767     PISSN: 0066426X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-physchem-032511-143716     Document Type: Review
Times cited : (836)

References (137)
  • 1
    • 0000097324 scopus 로고
    • Experiences de double irradiation en resonance magnetique par laméthode d'impulsions
    • Kaplan DE,Hahn EL. 1958. Experiences de double irradiation en resonance magnetique par laméthode d'impulsions. J. Phys. Rad. 19:821-25
    • (1958) J. Phys. Rad. , vol.19 , pp. 821-825
    • Kaplan, D.E.1    Hahn, E.L.2
  • 2
    • 0000330102 scopus 로고
    • Use of the double resonance in electron spin echo method for the study of paramagnetic center spatial distribution in solids
    • Milov AD, Salikhov KM, Shchirov MD. 1981. Use of the double resonance in electron spin echo method for the study of paramagnetic center spatial distribution in solids. Fiz. Tverd. Tela (Leningrad ) 23:975-82
    • (1981) Fiz. Tverd. Tela (Leningrad ) , vol.23 , pp. 975-982
    • Milov, A.D.1    Salikhov, K.M.2    Shchirov, M.D.3
  • 3
    • 0002279727 scopus 로고
    • Electron-electron double resonance in electron spin echo: Model biradical systems and the sensitized photolysis of decalin
    • Milov AD, Ponomarev AB, Tsvetkov YD. 1984. Electron-electron double resonance in electron spin echo: model biradical systems and the sensitized photolysis of decalin. Chem. Phys. Lett. 110:67-72
    • (1984) Chem. Phys. Lett. , vol.110 , pp. 67-72
    • Milov, A.D.1    Ponomarev, A.B.2    Tsvetkov, Y.D.3
  • 4
    • 0032476844 scopus 로고    scopus 로고
    • Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment
    • Martin RE, Pannier M, Diederich F, Gramlich V, Hubrich M, Spiess HW. 1998. Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment. Angew. Chem. Int. Ed. Engl. 37:2834-37 (Pubitemid 29008565)
    • (1998) Angewandte Chemie - International Edition , vol.37 , Issue.20 , pp. 2834-2837
    • Martin, R.E.1    Pannier, M.2    Diederich, F.3    Gramlich, V.4    Hubrich, M.5    Spiess, H.W.6
  • 5
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier M, Veit S, Godt A, Jeschke G, Spiess HW. 2000. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142:331-40
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 6
    • 34147218123 scopus 로고    scopus 로고
    • Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance
    • Jeschke G, Polyhach Y. 2007. Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance. Phys. Chem. Chem. Phys. 9:1895-910
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 1895-1910
    • Jeschke, G.1    Polyhach, Y.2
  • 7
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in biomacromolecules by EPR spectroscopy
    • DOI 10.1017/S003358350700460X
    • Schiemann O, Prisner TF. 2007. Long-range distance determinations in biomacromolecules by EPR spectroscopy. Q. Rev. Biophys. 40:1-53 (Pubitemid 47343581)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.1 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 8
    • 51649090966 scopus 로고    scopus 로고
    • Pulsed electron-electron double resonance (PELDOR) as EPR spectroscopy in nanometre range
    • Tsvetkov YD, Milov AD, Maryasov AG. 2008. Pulsed electron-electron double resonance (PELDOR) as EPR spectroscopy in nanometre range. Russ. Chem. Rev. 77:487-520
    • (2008) Russ. Chem. Rev. , vol.77 , pp. 487-520
    • Tsvetkov, Y.D.1    Milov, A.D.2    Maryasov, A.G.3
  • 9
    • 0000021813 scopus 로고    scopus 로고
    • The pulsed electron-electron double resonance and "2 + 1" electron spin echo study of the oriented oxygen-evolving and Mn-depleted preparations of photosystem II
    • Astashkin AV, Hara H, Kawamori A. 1998. The pulsed electron-electron double resonance and "2+1" electron spin echo study of the oriented oxygen-evolving and Mn-depleted preparations of photosystem II. J. Chem. Phys. 108:3805-12 (Pubitemid 128602275)
    • (1998) Journal of Chemical Physics , vol.108 , Issue.9 , pp. 3805-3812
    • Astashkin, A.V.1    Hara, H.2    Kawamori, A.3
  • 10
    • 0024809884 scopus 로고
    • Site-directed mutagenesis of colicin E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation
    • DOI 10.1002/prot.340060312
    • Todd AP, Cong J, Levinthal F, Levinthal C, Hubbell WL. 1989. Site-directed mutagenesis of colicin E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation. Proteins Struct. Funct. Genet. 6:294-305 (Pubitemid 20024369)
    • (1989) Proteins: Structure, Function and Genetics , vol.6 , Issue.3 , pp. 294-305
    • Todd, A.P.1    Cong, J.2    Levinthal, F.3    Levinthal, C.4    Hubbell, W.L.5
  • 11
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell WL, Cafiso DS, Altenbach C. 2000. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7:735-39
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 12
    • 0001590048 scopus 로고    scopus 로고
    • Multiple-quantum ESR and distance measurements
    • PII S0009261499009720
    • Borbat PP, Freed JH. 1999. Multiple-quantum ESR and distance measurements. Chem. Phys. Lett. 313:145-54 (Pubitemid 129556635)
    • (1999) Chemical Physics Letters , vol.313 , Issue.1-2 , pp. 145-154
    • Borbat, P.P.1    Freed, J.H.2
  • 13
    • 0036290220 scopus 로고    scopus 로고
    • Direct conversion of EPR dipolar time evolution data to distance distributions
    • Jeschke G, Koch A, Jonas U, Godt A. 2002. Direct conversion of EPR dipolar time evolution data to distance distributions. J. Magn. Reson. 155:72-82
    • (2002) J. Magn. Reson. , vol.155 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 16
    • 0037093869 scopus 로고    scopus 로고
    • Protein structure determination using long-distance constraints from double-quantum coherence ESR: Study of T4 lysozyme
    • DOI 10.1021/ja020040y
    • Borbat PP, Mchaourab HS, Freed JH. 2002. Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme. J. Am. Chem. Soc. 124:5304-14 (Pubitemid 34506927)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.19 , pp. 5304-5314
    • Borbat, P.P.1    Mchaourab, H.S.2    Freed, J.H.3
  • 17
    • 0344236128 scopus 로고    scopus 로고
    • Pulsed ELDOR Spectroscopy Measures the Distance between the Two Tyrosyl Radicals in the R2 Subunit of the E. coli Ribonucleotide Reductase
    • DOI 10.1021/ja0362095
    • Bennati M, Weber A, Antonic J, Perlstein DL, Robblee J, Stubbe J. 2003. Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl radicals in the R2 subunit of the E. coli ribonucleotide reductase. J. Am. Chem. Soc. 125:14988-89 (Pubitemid 37509653)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.49 , pp. 14988-14989
    • Bennati, M.1    Weber, A.2    Antonic, J.3    Perlstein, D.L.4    Robblee, J.5    Stubbe, J.6
  • 18
    • 1942487282 scopus 로고    scopus 로고
    • +/Proline Transporter PutP of Escherichia coli
    • Jeschke G,Wegener C, Nietschke M, Jung H, Steinhoff H. 2004. Interresidual distance determination by four-pulse double electron-electron resonance in an integral membrane protein: the Na+/praline transporter PutP of Escherichia coli. Biophys. J. 86:2551-57 (Pubitemid 38524441)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2551-2557
    • Jeschke, G.1    Wegener, C.2    Nietschke, M.3    Jung, H.4    Steinhoff, H.-J.5
  • 19
    • 21444441143 scopus 로고    scopus 로고
    • Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein by EPR measurements
    • DOI 10.1074/jbc.M501171200
    • Jeschke G, Bender A, Schweikardt T, Panek G, Decker H, Paulsen H. 2005. Localization of the Nterminal domain in light-harvesting chlorophyll a/b protein by EPR measurements. J. Biol. Chem. 280:18623-30 (Pubitemid 41379561)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18623-18630
    • Jeschke, G.1    Bender, A.2    Schweikardt, T.3    Panek, G.4    Decker, H.5    Paulsen, H.6
  • 20
    • 0032357748 scopus 로고    scopus 로고
    • Pulsed electron double resonance (PELDOR) and its applications in free-radicals research
    • Milov AD, Maryasov AG, Tsvetkov YD. 1998. Pulsed electron double resonance (PELDOR) and its applications in free-radicals research. Appl. Magn. Reson. 15:107-43
    • (1998) Appl. Magn. Reson. , vol.15 , pp. 107-143
    • Milov, A.D.1    Maryasov, A.G.2    Tsvetkov, Y.D.3
  • 21
    • 33749178896 scopus 로고    scopus 로고
    • Distance measurements in solid-state NMR and EPR spectroscopy
    • DOI 10.1007/3-540-32627-8-2, Novel NMR and EPR Techniques
    • Jeschke G, Spiess HW. 2006. Distance measurements in solid-state NMR and EPR spectroscopy. Lect. Notes Phys. 684:21-63 (Pubitemid 44472770)
    • (2006) Lecture Notes in Physics , vol.684 , pp. 21-63
    • Jeschke, G.1    Spiess, H.W.2
  • 22
    • 0034398249 scopus 로고    scopus 로고
    • Formation of the pulsed electron-electron double resonance signal in the case of a finite amplitude of microwave fields
    • Maryasov AG, Tsvetkov YD. 2000. Formation of the pulsed electron-electron double resonance signal in the case of a finite amplitude of microwave fields. Appl. Magn. Reson. 18:583-605
    • (2000) Appl. Magn. Reson. , vol.18 , pp. 583-605
    • Maryasov, A.G.1    Tsvetkov, Y.D.2
  • 23
    • 34247478142 scopus 로고    scopus 로고
    • Dynamic phase shifts in nanoscale distance measurements by double electron electron resonance (DEER)
    • DOI 10.1016/j.jmr.2006.12.011, PII S1090780706004071
    • Bowman MK,Maryasov AG. 2007. Dynamic phase shifts in nanoscale distance measurements by double electron electron resonance (DEER). J. Magn. Reson. 185:270-82 (Pubitemid 46656356)
    • (2007) Journal of Magnetic Resonance , vol.185 , Issue.2 , pp. 270-282
    • Bowman, M.K.1    Maryasov, A.G.2
  • 24
    • 0031485790 scopus 로고    scopus 로고
    • Double electron-electron resonance in electron spin echo: Conformations of spin-labeled poly-4-vinilpyridine in glassy solutions
    • Milov AD, Tsvetkov YD. 1997. Double electron-electron resonance in electron spin echo: conformations of spin-labeled poly-4-vinilpyridine in glassy solutions. Appl. Magn. Reson. 12:495-504
    • (1997) Appl. Magn. Reson. , vol.12 , pp. 495-504
    • Milov, A.D.1    Tsvetkov, Y.D.2
  • 25
    • 68349085642 scopus 로고    scopus 로고
    • Three-spin correlations in double electron-electron resonance
    • Jeschke G, Sajid M, Schulte M, Godt A. 2009. Three-spin correlations in double electron-electron resonance. Phys. Chem. Chem. Phys. 11:6580-91
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6580-6591
    • Jeschke, G.1    Sajid, M.2    Schulte, M.3    Godt, A.4
  • 26
    • 0001201352 scopus 로고    scopus 로고
    • Dipolar spectroscopy and spin alignment in electron paramagnetic resonance
    • Jeschke G, Pannier M, Godt A, Spiess HW. 2000. Dipolar spectroscopy and spin alignment in electron paramagnetic resonance. Chem. Phys. Lett. 331:243-52
    • (2000) Chem. Phys. Lett. , vol.331 , pp. 243-252
    • Jeschke, G.1    Pannier, M.2    Godt, A.3    Spiess, H.W.4
  • 27
    • 33845992936 scopus 로고    scopus 로고
    • Distance determination in human ubiquitin by pulsed double electron-electron resonance and double quantum coherence ESR methods
    • DOI 10.1016/j.jmr.2006.09.017, PII S1090780706003089
    • Hara H, Tenno T, Shirakawa M. 2007. Distance determination in human ubiquitin by pulsed double electron-electron resonance and double quantum coherence ESR methods. J. Magn. Reson. 184:78-84 (Pubitemid 46049047)
    • (2007) Journal of Magnetic Resonance , vol.184 , Issue.1 , pp. 78-84
    • Hara, H.1    Tenno, T.2    Shirakawa, M.3
  • 30
    • 70350313495 scopus 로고    scopus 로고
    • Pulsed electron-electron doubleresonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA
    • Endeward B, Butterwick JA, MacKinnon R, Prisner TF. 2009. Pulsed electron-electron doubleresonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA. J. Am. Chem. Soc. 131:15246-50
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15246-15250
    • Endeward, B.1    Butterwick, J.A.2    MacKinnon, R.3    Prisner, T.F.4
  • 31
    • 77958469125 scopus 로고    scopus 로고
    • Optimization of transversal relaxation of nitroxides for pulsed electron-electron double resonance spectroscopy in phospholipids membranes
    • Dastvan R, Bode BE, Karuppiah MPR, Marko A, Lyubenova S, et al. 2010. Optimization of transversal relaxation of nitroxides for pulsed electron-electron double resonance spectroscopy in phospholipids membranes. J. Phys. Chem. B 114:13507-16
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13507-13516
    • Dastvan, R.1    Bode, B.E.2    Karuppiah, M.P.R.3    Marko, A.4    Lyubenova, S.5
  • 32
    • 77954643681 scopus 로고    scopus 로고
    • Functional reconstitution of anABCtransporter in nanodiscs for use in electron paramagnetic resonance spectroscopy
    • Alvarez FJD, Orelle C, Davidson AL. 2010. Functional reconstitution of anABCtransporter in nanodiscs for use in electron paramagnetic resonance spectroscopy. J. Am. Chem. Soc. 132:9513-15
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9513-9515
    • Alvarez, F.J.D.1    Orelle, C.2    Davidson, A.L.3
  • 33
    • 77949608570 scopus 로고    scopus 로고
    • Increased sensitivity and extended range of distance measurements in spin-labeled membrane proteins: Q-band double electron-electron resonance and nanoscale bilayers
    • Zou P, Mchaourab HS. 2010. Increased sensitivity and extended range of distance measurements in spin-labeled membrane proteins: Q-band double electron-electron resonance and nanoscale bilayers. Biophys. J. 98:L18-20
    • (2010) Biophys. J. , vol.98
    • Zou, P.1    McHaourab, H.S.2
  • 35
    • 67649607260 scopus 로고    scopus 로고
    • Significantly improved sensitivity of Q-band PELDOR/DEER experiments relative to X-band is observed in measuring the intercoil distance of a leucine zipper motif peptide (GCN4-LZ)
    • Ghimire H,McCarrick RM, Budil DE, Lorigan GA. 2009. Significantly improved sensitivity of Q-band PELDOR/DEER experiments relative to X-band is observed in measuring the intercoil distance of a leucine zipper motif peptide (GCN4-LZ). Biochemistry 48:5782-84
    • (2009) Biochemistry , vol.48 , pp. 5782-5784
    • Ghimire, H.1    McCarrick, R.M.2    Budil, D.E.3    Lorigan, G.A.4
  • 36
    • 79952170325 scopus 로고    scopus 로고
    • Electron transfer flavoprotein domain II orientation monitored using double electron-electron resonance between an enzymatically reduced, native FAD cofactor, and spin labels
    • Swanson MA, Kathirvelu V, Majtan T, Frerman FE, Eaton GR, Eaton SS. 2011. Electron transfer flavoprotein domain II orientation monitored using double electron-electron resonance between an enzymatically reduced, native FAD cofactor, and spin labels. Protein. Sci. 20:610-20
    • (2011) Protein. Sci. , vol.20 , pp. 610-620
    • Swanson, M.A.1    Kathirvelu, V.2    Majtan, T.3    Frerman, F.E.4    Eaton, G.R.5    Eaton, S.S.6
  • 37
    • 68049112349 scopus 로고    scopus 로고
    • Cryogenic 35 GHz pulse ENDOR probehead accommodating large sample sizes: Performance and applications
    • Tschaggelar R, Kasumaj B, Santangelo MG, Forrer J, Leger P, et al. 2009. Cryogenic 35 GHz pulse ENDOR probehead accommodating large sample sizes: performance and applications. J. Magn. Reson. 200:81-87
    • (2009) J. Magn. Reson. , vol.200 , pp. 81-87
    • Tschaggelar, R.1    Kasumaj, B.2    Santangelo, M.G.3    Forrer, J.4    Leger, P.5
  • 38
    • 33645453799 scopus 로고    scopus 로고
    • PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase
    • Biglino D, Schmidt PP, Reijerse EJ, Lubitz W. 2006. PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase. Phys. Chem. Chem. Phys. 8:58-62
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 58-62
    • Biglino, D.1    Schmidt, P.P.2    Reijerse, E.J.3    Lubitz, W.4
  • 39
    • 77952099112 scopus 로고    scopus 로고
    • Distance and dynamics determination by W-band DEER andW-band ST-EPR
    • Song L, Larion M, Chamoun J, Bonora M, Fajer PG. 2009. Distance and dynamics determination by W-band DEER andW-band ST-EPR. Eur. Biophys. J. 39:711-19
    • (2009) Eur. Biophys. J. , vol.39 , pp. 711-719
    • Song, L.1    Larion, M.2    Chamoun, J.3    Bonora, M.4    Fajer, P.G.5
  • 40
    • 70350786674 scopus 로고    scopus 로고
    • A kilowatt pulsed 94 GHz electron paramagnetic resonance spectrometer with high concentration sensitivity, high instantaneous bandwidth, and low dead time
    • Cruickshank PA, Bolton DR, Robertson DA, Hunter RI, Wylde RJ, Smith GM. 2009. A kilowatt pulsed 94 GHz electron paramagnetic resonance spectrometer with high concentration sensitivity, high instantaneous bandwidth, and low dead time. Rev. Sci. Instrum. 80:103102
    • (2009) Rev. Sci. Instrum. , vol.80 , pp. 103102
    • Cruickshank, P.A.1    Bolton, D.R.2    Robertson, D.A.3    Hunter, R.I.4    Wylde, R.J.5    Smith, G.M.6
  • 42
    • 0001579637 scopus 로고
    • Double electron-electron resonance spin-echo modulation: Spectroscopic measurement of electron spin pair separations in orientationally disordered solids
    • Larsen RG, Singel DJ. 1993. Double electron-electron resonance spin-echo modulation: spectroscopic measurement of electron spin pair separations in orientationally disordered solids. J. Chem. Phys. 98:5134-46
    • (1993) J. Chem. Phys. , vol.98 , pp. 5134-5146
    • Larsen, R.G.1    Singel, D.J.2
  • 44
    • 77955806633 scopus 로고    scopus 로고
    • Flexibility of shape-persistent molecular building blocks composed of p-phenylene and ethynylene units
    • Jeschke G, Sajid M, Schulte M, Ramezanian N, Volkov A, et al. 2010. Flexibility of shape-persistent molecular building blocks composed of p-phenylene and ethynylene units. J. Am. Chem. Soc. 132:10107-17
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10107-10117
    • Jeschke, G.1    Sajid, M.2    Schulte, M.3    Ramezanian, N.4    Volkov, A.5
  • 45
    • 60349094124 scopus 로고    scopus 로고
    • Molecular orientation studies by pulsed electron-electron double resonance experiments
    • Marko A, Margraf D, Yu H, Mu Y, Stock G, Prisner T. 2009. Molecular orientation studies by pulsed electron-electron double resonance experiments. J. Chem. Phys. 130:064102
    • (2009) J. Chem. Phys. , vol.130 , pp. 064102
    • Marko, A.1    Margraf, D.2    Yu, H.3    Mu, Y.4    Stock, G.5    Prisner, T.6
  • 46
    • 45149146601 scopus 로고
    • Selection of dipolar interaction by the "2 + 1" pulse train ESE
    • Kurshev VV, Raitsimring AM, Tsvetkov YD. 1989. Selection of dipolar interaction by the "2 + 1" pulse train ESE. J. Magn. Reson. 81:441-54
    • (1989) J. Magn. Reson. , vol.81 , pp. 441-454
    • Kurshev, V.V.1    Raitsimring, A.M.2    Tsvetkov, Y.D.3
  • 48
    • 0036004918 scopus 로고    scopus 로고
    • Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy
    • Jeschke G. 2002. Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy. Macromol. Rapid. Commun. 23:227-46
    • (2002) Macromol. Rapid. Commun. , vol.23 , pp. 227-246
    • Jeschke, G.1
  • 49
    • 0036384679 scopus 로고    scopus 로고
    • PELDOR at S-and X-band frequencies and the separation of exchange coupling from dipolar coupling
    • Weber A, Schiemann O, Bode B, Prisner TF. 2002. PELDOR at S-and X-band frequencies and the separation of exchange coupling from dipolar coupling. J. Magn. Reson. 157:277-85
    • (2002) J. Magn. Reson. , vol.157 , pp. 277-285
    • Weber, A.1    Schiemann, O.2    Bode, B.3    Prisner, T.F.4
  • 50
    • 67651208236 scopus 로고    scopus 로고
    • Interaction of radical pairs through-bond and through-space: Scope and limitations of the point-dipole approximation in electron paramagnetic resonance spectroscopy
    • Riplinger C, Kao JPY, Rosen GM, Kathirvelu V, Eaton GR, et al. 2009. Interaction of radical pairs through-bond and through-space: scope and limitations of the point-dipole approximation in electron paramagnetic resonance spectroscopy. J. Am. Chem. Soc. 131:10092-106
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10092-10106
    • Riplinger, C.1    Kao, J.P.Y.2    Rosen, G.M.3    Kathirvelu, V.4    Eaton, G.R.5
  • 51
    • 0020482581 scopus 로고
    • A novel reversible thiol-specific spin label: Papain active site labeling and inhibition
    • Berliner LJ, Grunwald J, Hankovszky HO, Hideg K. 1982. A novel reversible thiol-specific spin label: papain active site labeling and inhibition. Anal. Biochem. 119:450-55
    • (1982) Anal. Biochem. , vol.119 , pp. 450-455
    • Berliner, L.J.1    Grunwald, J.2    Hankovszky, H.O.3    Hideg, K.4
  • 52
    • 77953642222 scopus 로고    scopus 로고
    • Distance determination in proteins inside Xenopus laevis oocytes by double electron-electron resonance experiments
    • Igarashi R, Sakai T, Hara H, Tenno T, Tanaka T, et al. 2010. Distance determination in proteins inside Xenopus laevis oocytes by double electron-electron resonance experiments. J. Am. Chem. Soc. 132:8228-29
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 8228-8229
    • Igarashi, R.1    Sakai, T.2    Hara, H.3    Tenno, T.4    Tanaka, T.5
  • 53
    • 73249142528 scopus 로고    scopus 로고
    • Refolding of the integral membrane protein light-harvesting complex II monitored by pulse EPR
    • DockterC,VolkovA,Bauer C, Polyhach Y, Joly-LopezZ, et al. 2009. Refolding of the integral membrane protein light-harvesting complex II monitored by pulse EPR. Proc. Natl. Acad. Sci. USA 106:18485-90
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18485-18490
    • Dockter, C.1    Volkov, A.2    Bauer, C.3    Joly-Lopezz, P.Y.4
  • 54
    • 0021826632 scopus 로고
    • Factors affecting nitroxide reduction in ascorbate solution and tissue homogenates
    • DOI 10.1016/0730-725X(85)90012-8
    • CouetWR, Brasch RC, Sosnovsky G, TozerTN. 1985. Factors affecting nitroxide reduction in ascorbate solution and tissue homogenates. Magn. Reson. Imaging 3:83-88 (Pubitemid 15075066)
    • (1985) Magnetic Resonance Imaging , vol.3 , Issue.1 , pp. 83-88
    • Couet, W.R.1    Brasch, R.C.2    Sosnovsky, G.3    Tozer, T.N.4
  • 56
    • 0020682255 scopus 로고
    • Synthesis and properties of spin-labeled angiotensin derivatives
    • Nakaie CR, Schreier S, Paiva ACM. 1983. Synthesis and properties of spin-labeled angiotensin derivatives. Biochim. Biophys. Acta 742:63-71 (Pubitemid 13184793)
    • (1983) Biochimica et Biophysica Acta , vol.742 , Issue.1 , pp. 63-71
    • Nakaie, C.R.1    Schreier, S.2    Paiva, A.C.M.3
  • 57
    • 12044255745 scopus 로고
    • A novel spin-labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxycarbonyl)-2,2,6,6-tetramethylpiperidine-N-oxyl-4-amino-4- carboxylic acid
    • Marchetto R, Schreier S, Nakaie CR. 1993. A novel spin-labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxycarbonyl)-2,2,6, 6-tetramethylpiperidine-N-oxyl-4-amino-4-carboxylic acid. J. Am. Chem. Soc. 115:11042-43
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11042-11043
    • Marchetto, R.1    Schreier, S.2    Nakaie, C.R.3
  • 58
    • 0029171261 scopus 로고
    • Synthesis and conformational studies of peptides containing TOAC, a spin-labelled C alpha, alpha-disubstituted glycine
    • Toniolo C, Valente E, Formaggio F, Crisma M, Pilloni G, et al. 1995. Synthesis and conformational studies of peptides containing TOAC, a spin-labelled C alpha, alpha-disubstituted glycine. J. Pept. Sci. 1:45-57
    • (1995) J. Pept. Sci. , vol.1 , pp. 45-57
    • Toniolo, C.1    Valente, E.2    Formaggio, F.3    Crisma, M.4    Pilloni, G.5
  • 59
    • 77952159454 scopus 로고    scopus 로고
    • A spirocyclohexyl nitroxide amino acid spin label for pulsed EPR spectroscopy distance measurements
    • Rajca A, Kathirvelu V, Roy SK, PinkM, Rajca S, et al. 2010. A spirocyclohexyl nitroxide amino acid spin label for pulsed EPR spectroscopy distance measurements. Chem. Eur. J. 16:5778-82
    • (2010) Chem. Eur. J. , vol.16 , pp. 5778-5782
    • Rajca, A.1    Kathirvelu, V.2    Roy, S.K.3    Pink, M.4    Rajca, S.5
  • 60
    • 33645947031 scopus 로고    scopus 로고
    • Isotope selection in distance measurements between nitroxides
    • Jeschke G, Zimmermann H, Godt A. 2006. Isotope selection in distance measurements between nitroxides. J. Magn. Reson. 180:137-46
    • (2006) J. Magn. Reson. , vol.180 , pp. 137-146
    • Jeschke, G.1    Zimmermann, H.2    Godt, A.3
  • 62
    • 34247540806 scopus 로고    scopus 로고
    • Pulsed ELDOR determination of the intramolecular distance between the metal binding sites in dicupric human serum transferrin and lactoferrin
    • DOI 10.1021/ja068966j
    • KayCW, El Mkami H, Cammack R, Evans RW. 2007. PulsedELDORdetermination of the intramolecular distance between themetal binding sites in dicupric human serum transferrin and lactoferrin. J. Am. Chem. Soc. 129:4868-69 (Pubitemid 46651347)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.16 , pp. 4868-4869
    • Kay, C.W.M.1    El Mkami, H.2    Cammack, R.3    Evans, R.W.4
  • 63
    • 77952187929 scopus 로고    scopus 로고
    • 2+ ions and ESR
    • Yang Z, Kise D, Saxena S. 2010. An approach towards the measurement of nanometer range distances based on Cu2+ ions and ESR. J. Phys. Chem. B 114:6165-74
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6165-6174
    • Yang, Z.1    Kise, D.2    Saxena, S.3
  • 64
    • 46349097539 scopus 로고    scopus 로고
    • PELDORmeasurements on a nitroxide-labeled Cu(II) porphyrin: Orientation selection, spin-density distribution, and conformational flexibility
    • Bode BE, Plackmeyer J, Prisner TF, Schiemann O. 2008.PELDORmeasurements on a nitroxide-labeled Cu(II) porphyrin: orientation selection, spin-density distribution, and conformational flexibility. J. Phys. Chem. A 112:5064-73
    • (2008) J. Phys. Chem. A , vol.112 , pp. 5064-5073
    • Bode, B.E.1    Plackmeyer, J.2    Prisner, T.F.3    Schiemann, O.4
  • 68
    • 0037131445 scopus 로고    scopus 로고
    • Selective measurements of a nitroxide-nitroxide separation of 5 nm and a nitroxide-copper separation of 2.5 nm in a terpyridine-based copper(II) complex by pulse EPR spectroscopy
    • DOI 10.1002/1521-3773(20021018)41:20<3907::AID-ANIE3907>3.0.CO;2-T
    • Narr E, Godt A, Jeschke G. 2002. Selective measurements of a nitroxide-nitroxide separation of 5 nm and a nitroxide-copper separation of 2.5 nm in a terpyridine-based copper(II) complex by pulse EPR spectroscopy. Angew. Chem. Int. Ed. Engl. 41:3907-10 (Pubitemid 35278037)
    • (2002) Angewandte Chemie - International Edition , vol.41 , Issue.20 , pp. 3907-3910
    • Narr, E.1    Godt, A.2    Jeschke, G.3
  • 69
    • 79952787086 scopus 로고    scopus 로고
    • 3+ions and nitroxide radicals
    • Lueders P, Jeschke G, Yulikov M. 2011. Double electron-electron resonance measured between Gd3+ions and nitroxide radicals. J. Phys. Chem. Lett. 2:604-9
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 604-609
    • Lueders, P.1    Jeschke, G.2    Yulikov, M.3
  • 70
    • 33846383027 scopus 로고    scopus 로고
    • Dipole-dipole interactions of high-spin paramagnetic centers in disordered systems
    • Maryasov AG, Bowman MK, Tsvetkov YD. 2006. Dipole-dipole interactions of high-spin paramagnetic centers in disordered systems. Appl. Magn. Reson. 30:683-702
    • (2006) Appl. Magn. Reson. , vol.30 , pp. 683-702
    • Maryasov, A.G.1    Bowman, M.K.2    Tsvetkov, Y.D.3
  • 71
    • 0037164101 scopus 로고    scopus 로고
    • Pulsed electron-electron double resonance on multinuclear metal clusters: Assignment of spin projection factors based on the dipolar interaction
    • DOI 10.1021/ja027348+
    • Elsaesser C, Brecht M, Bittl R. 2002. Pulsed electron-electron double resonance on multinuclear metal clusters: assignment of spin projection factors based on the dipolar interaction. J. Am. Chem. Soc. 124:12606-11 (Pubitemid 35204587)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.42 , pp. 12606-12611
    • Elsasser, C.1    Brecht, M.2    Bittl, R.3
  • 72
    • 14644437752 scopus 로고    scopus 로고
    • Treatment of spin-coupled metal-centres in pulsed electron-electron double-resonance experiments
    • DOI 10.1042/BST0330015
    • ElsaesserC,BrechtM,Bittl R. 2005. Treatment of spin-coupled metal centres in pulsed electron-electron double-resonance experiments. Biochem. Soc. Trans. 33:15-19 (Pubitemid 40313750)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.1 , pp. 15-19
    • Elsaesser, C.1    Brecht, M.2    Bittl, R.3
  • 73
    • 6444234265 scopus 로고    scopus 로고
    • The effect of microwave pulse duration on the distance distribution function between spin labels obtained by PELDOR data analysis
    • Milov AD, Naumov BD, Tsvetkov YD. 2004. The effect of microwave pulse duration on the distance distribution function between spin labels obtained by PELDOR data analysis. Appl.Magn. Reson. 26:587-99 (Pubitemid 39406896)
    • (2004) Applied Magnetic Resonance , vol.26 , Issue.4 , pp. 587-599
    • Milov, A.D.1    Naumov, B.D.2    Tsvetkov, Yu.D.3
  • 74
    • 40949163372 scopus 로고    scopus 로고
    • Distance measurements in the borderline region of applicability of CW EPR and DEER: A model study on a homologous series of spin-labelled peptides
    • Banham JE, BakerCM, Ceola S,Day IJ, GrantGH, et al. 2008. Distance measurements in the borderline region of applicability of CW EPR and DEER: a model study on a homologous series of spin-labelled peptides. J. Magn. Reson. 191:202-18
    • (2008) J. Magn. Reson. , vol.191 , pp. 202-218
    • Banham, J.E.1    Baker, C.M.2    Ceola, S.3    Day, I.J.4    Grant, G.H.5
  • 76
    • 67650546951 scopus 로고    scopus 로고
    • Transmembrane signaling in the maltose ABC transporterMalFGK2-E: PeriplasmicMalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer
    • Grote M, Polyhach Y, Jeschke G, Steinhoff H, Schneider E, Bordignon E. 2009. Transmembrane signaling in the maltose ABC transporterMalFGK2-E: periplasmicMalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer. J. Biol. Chem. 284:17521-26
    • (2009) J. Biol. Chem. , vol.284 , pp. 17521-17526
    • Grote, M.1    Polyhach, Y.2    Jeschke, G.3    Steinhoff, H.4    Schneider, E.5    Bordignon, E.6
  • 77
    • 41149131813 scopus 로고    scopus 로고
    • Conformational flexibility of nitroxide biradicals determined by X-band PELDOR experiments
    • DOI 10.1080/00268970701724982, PII 788605202, A Special Issue Dedicated to Professor Arthur Schweiger
    • Margraf D, Bode BE,Marko A, Schiemann O, Prisner TF. 2007. Conformational flexibility of nitroxide biradicals determined by X-band PELDOR experiments. Mol. Phys. 105:2153-60 (Pubitemid 351426631)
    • (2007) Molecular Physics , vol.105 , Issue.15-16 , pp. 2153-2160
    • Margraf, D.1    Bode, B.E.2    Marko, A.3    Schiemann, O.4    Prisner, T.F.5
  • 78
    • 39649086921 scopus 로고    scopus 로고
    • Analysis of the dynamical flexibility of bis-peptide nanostructures
    • DOI 10.1021/jp077523e
    • Pornsuwan S, Schafmeister CE, Saxena S. 2008. Analysis of the dynamical flexibility of bis-peptide nanostructures. J. Phys. Chem. C 112:1377-84 (Pubitemid 351288242)
    • (2008) Journal of Physical Chemistry C , vol.112 , Issue.5 , pp. 1377-1384
    • Pornsuwan, S.1    Schafmeister, C.E.2    Saxena, S.3
  • 83
    • 33947620119 scopus 로고    scopus 로고
    • Spin pair geometry revealed by high-field DEER in the presence of conformational distributions
    • DOI 10.1016/j.jmr.2006.11.012, PII S1090780706003934
    • Polyhach Y, Godt A, Bauer C, Jeschke G. 2007. Spin pair geometry revealed by high-field DEER in the presence of conformational distributions. J. Magn. Reson. 185:118-29 (Pubitemid 46501770)
    • (2007) Journal of Magnetic Resonance , vol.185 , Issue.1 , pp. 118-129
    • Polyhach, Ye.1    Godt, A.2    Bauer, C.3    Jeschke, G.4
  • 85
    • 43949130403 scopus 로고    scopus 로고
    • Observer-selective double electron-electron-spin resonance, a pulse sequence to improve orientation selection
    • Milikisyants S, Groenen EJJ, Huber M. 2008. Observer-selective double electron-electron-spin resonance, a pulse sequence to improve orientation selection. J. Magn. Reson. 192:275-79
    • (2008) J. Magn. Reson. , vol.192 , pp. 275-279
    • Milikisyants, S.1    Ejj, G.2    Huber, M.3
  • 86
    • 3042819802 scopus 로고    scopus 로고
    • Data analysis procedures for pulse ELDOR measurements of broad distance distributions
    • Jeschke G, Panek G, Godt A, Bender A, Paulsen H. 2004. Data analysis procedures for pulse ELDOR measurements of broad distance distributions. Appl. Magn. Reson. 26:223-44 (Pubitemid 38860166)
    • (2004) Applied Magnetic Resonance , vol.26 , Issue.1-2 , pp. 223-244
    • Jeschke, G.1    Panek, G.2    Godt, A.3    Bender, A.4    Paulsen, H.5
  • 87
    • 3042741373 scopus 로고    scopus 로고
    • Visualization of distance distribution from pulsed double electron-electron resonance data
    • Bowman MK,Maryasov AG, KimN, deRoseVJ. 2004. Visualization of distance distribution from pulsed double electron-electron resonance data. Appl. Magn. Reson. 26:23-39 (Pubitemid 38860152)
    • (2004) Applied Magnetic Resonance , vol.26 , Issue.1-2 , pp. 23-39
    • Bowman, M.K.1    Maryasov, A.G.2    Kim, N.3    DeRose, V.J.4
  • 88
    • 11344285129 scopus 로고    scopus 로고
    • The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    • DOI 10.1016/j.jmr.2004.10.012, PII S1090780704003532
    • Chiang Y, Borbat PP, Freed JH. 2005. The determination of pair distance distributions by pulsed ESR using Tikhonov regularization. J. Magn. Reson. 172:279-95 (Pubitemid 40072533)
    • (2005) Journal of Magnetic Resonance , vol.172 , Issue.2 , pp. 279-295
    • Chiang, Y.-W.1    Borbat, P.P.2    Freed, J.H.3
  • 89
    • 28044472953 scopus 로고    scopus 로고
    • Maximum entropy: A complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR
    • DOI 10.1016/j.jmr.2005.07.021, PII S1090780705002466
    • Chiang Y, Borbat PP, Freed JH. 2005. Maximum entropy: a complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR. J. Magn. Reson. 177:184-96 (Pubitemid 41690881)
    • (2005) Journal of Magnetic Resonance , vol.177 , Issue.2 , pp. 184-196
    • Chiang, Y.-W.1    Borbat, P.P.2    Freed, J.H.3
  • 90
    • 33846344623 scopus 로고    scopus 로고
    • DeerAnalysis2006 - A comprehensive software package for analyzing pulsed ELDOR data
    • Jeschke G, Chechik V, Ionita P, Godt A, Zimmermann H, et al. 2006. DeerAnalysis2006-a comprehensive software package for analyzing pulsed ELDOR data. Appl. Magn. Reson. 30:473-98
    • (2006) Appl. Magn. Reson. , vol.30 , pp. 473-498
    • Jeschke, G.1    Chechik, V.2    Ionita, P.3    Godt, A.4    Zimmermann, H.5
  • 91
    • 84859884460 scopus 로고    scopus 로고
    • ETH Zürich.
    • Jeschke G. 2011. DeerAnalysis. ETH Zürich. http://www.epr.ethz.ch/ software/index
    • (2011) DeerAnalysis
    • Jeschke, G.1
  • 93
    • 34250693182 scopus 로고    scopus 로고
    • Orientation-resolving pulsed electron dipolar high-field EPR spectroscopy on disordered solids: I. Structure of spin-correlated radical pairs in bacterial photosynthetic reaction centers
    • DOI 10.1021/jp070016c
    • Savitsky A, Dubinskii AA, Flores M, Lubitz W, Mobius K. 2007. Orientation-resolving pulsed electron dipolar high-field EPR spectroscopy on disordered solids. I. Structure of spin-correlated radical pairs in bacterial photosynthetic reaction centers. J. Phys. Chem. B 111:6245-62 (Pubitemid 46966232)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.22 , pp. 6245-6262
    • Savitsky, A.1    Dubinskii, A.A.2    Flores, M.3    Lubitz, W.4    Mobius, K.5
  • 96
    • 21644446664 scopus 로고    scopus 로고
    • Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER
    • DOI 10.1021/ja051652w
    • Sale K, Song L, Liu Y, Perozo E, Fajer P. 2005. Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER. J. Am. Chem. Soc. 127:9334-35 (Pubitemid 40934724)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.26 , pp. 9334-9335
    • Sale, K.1    Song, L.2    Liu, Y.-S.3    Perozo, E.4    Fajer, P.5
  • 97
    • 36549000870 scopus 로고    scopus 로고
    • + antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurements
    • DOI 10.1529/biophysj.107.109769
    • Hilger D, Polyhach Y, Padan E, Jung H, Jeschke G. 2007. High-resolution structure of aNa+/H+antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurements. Biophys. J. 93:3675-83 (Pubitemid 350190829)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3675-3683
    • Hilger, D.1    Polyhach, Y.2    Padan, E.3    Jung, H.4    Jeschke, G.5
  • 98
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Polyhach Y, Bordignon E, Jeschke G. 2011. Rotamer libraries of spin labelled cysteines for protein studies. Phys. Chem. Chem. Phys. 13:2356-66
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 99
    • 57149113172 scopus 로고    scopus 로고
    • Accurate long-range distance measurements in a doubly spin-labeled protein by a four-pulse, double electron-electron resonance method
    • Finiguerra MG, Prudencio M, Ubbink M, HuberM. 2008. Accurate long-range distance measurements in a doubly spin-labeled protein by a four-pulse, double electron-electron resonance method. Magn. Reson. Chem. 46:1096-101
    • (2008) Magn. Reson. Chem. , vol.46 , pp. 1096-1101
    • Finiguerra, M.G.1    Prudencio, M.2    Ubbink, M.3    Huber, M.4
  • 100
    • 41149178551 scopus 로고    scopus 로고
    • Evidence from EPR that nitroxide spin labels attached to human hemoglobin alter their conformation upon freezing
    • DOI 10.1080/00268970701579501, PII 782361690, A Special Issue Dedicated to Professor Arthur Schweiger
    • Banham JE, Jeschke G, Timmel CR. 2007. Evidence from EPR that nitroxide spin labels attached to human hemoglobin alter their conformation upon freezing. Mol. Phys. 105:2041-47 (Pubitemid 351436233)
    • (2007) Molecular Physics , vol.105 , Issue.15-16 , pp. 2041-2047
    • Banham, J.E.1    Jeschke, G.2    Timmel, C.R.3
  • 101
    • 78650882203 scopus 로고    scopus 로고
    • Shigella flexneri Spa15 crystal structure verified in solution by double electron electron resonance
    • Lillington JE, Lovett JE, Johnson S, Roversi P, TimmelCR, Lea SM. 2010. Shigella flexneri Spa15 crystal structure verified in solution by double electron electron resonance. J. Mol. Biol. 405:427-35
    • (2010) J. Mol. Biol. , vol.405 , pp. 427-435
    • Lillington, J.E.1    Lovett, J.E.2    Johnson, S.3    Roversi, P.4    Timmel, C.R.5    Lea, S.M.6
  • 102
    • 59149083869 scopus 로고    scopus 로고
    • Conformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states
    • Appel M, Hizlan D, Vinothkumar KR, Ziegler C, Kuhlbrandt W. 2009. Conformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states. J. Mol. Biol. 386:351-65
    • (2009) J. Mol. Biol. , vol.386 , pp. 351-365
    • Appel, M.1    Hizlan, D.2    Vinothkumar, K.R.3    Ziegler, C.4    Kuhlbrandt, W.5
  • 103
    • 61949215199 scopus 로고    scopus 로고
    • Solute effects on spin labels at an aqueous-exposed site in the flap region of HIV-1 protease
    • Galiano L, BlackburnME, Veloro AM, BonoraM, Fanucci GE. 2009. Solute effects on spin labels at an aqueous-exposed site in the flap region of HIV-1 protease. J. Phys. Chem. B 113:1673-80
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1673-1680
    • Galiano, L.1    Blackburn, M.E.2    Veloro, A.M.3    Bonora, M.4    Fanucci, G.E.5
  • 104
    • 65649117362 scopus 로고    scopus 로고
    • Structural origin of weakly ordered nitroxide motion in spin-labeled proteins
    • Fleissner MR, Cascio D, Hubbell WL. 2009. Structural origin of weakly ordered nitroxide motion in spin-labeled proteins. Protein Sci. 18:893-908
    • (2009) Protein Sci. , vol.18 , pp. 893-908
    • Fleissner, M.R.1    Cascio, D.2    Hubbell, W.L.3
  • 105
    • 79954450578 scopus 로고    scopus 로고
    • Integrated analysis of the conformation of a protein-linked spin label by crystallography,EPRandNMRspectroscopy
    • Gruene T, ChoMK, Karyagina I,Kim HY,Grosse C, et al. 2011. Integrated analysis of the conformation of a protein-linked spin label by crystallography,EPRandNMRspectroscopy. J. Biomol.NMR49:111-19
    • (2011) J. Biomol.NMR49 , pp. 111-119
    • Gruene, T.1    Cho, M.K.2    Karyagina, I.3    Kim, H.Y.4    Grosse, C.5
  • 106
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 107
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography&NMRsystem: A new software suite for macromolecular structure determination
    • Brunger AT, Adams PD, CloreGM, DeLano WL,Gros P, et al. 1998. Crystallography&NMRsystem: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54:905-21
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    Delano, W.L.4    Gros, P.5
  • 108
    • 34250874047 scopus 로고    scopus 로고
    • Rigid Body Refinement of Protein Complexes with Long-Range Distance Restraints from Pulsed Dipolar ESR
    • DOI 10.1016/S0076-6879(07)23004-6, PII S0076687907230046, Two Component Signaling Systems, Part B
    • Bhatnagar J, Freed JH, Crane BR. 2007. Rigid body refinement of protein complexes with long-range distance restraints from pulsed dipolar ESR. Methods Enzymol. 423:117-33 (Pubitemid 46991092)
    • (2007) Methods in Enzymology , vol.423 , pp. 117-133
    • Bhatnagar, J.1    Freed, J.H.2    Crane, B.R.3
  • 109
    • 34250841296 scopus 로고    scopus 로고
    • Measuring Distances by Pulsed Dipolar ESR Spectroscopy: Spin-Labeled Histidine Kinases
    • DOI 10.1016/S0076-6879(07)23003-4, PII S0076687907230034, Two Component Signaling Systems, Part B
    • Borbat PP, Freed JH. 2007. Measuring distances by pulsed dipolar ESR spectroscopy: spin-labeled histidine kinases. Methods Enzymol. 423:52-116 (Pubitemid 46991091)
    • (2007) Methods in Enzymology , vol.423 , pp. 52-116
    • Borbat, P.P.1    Freed, J.H.2
  • 110
    • 70349298715 scopus 로고    scopus 로고
    • A combined pulse EPR and Monte Carlo simulation study provides molecular insight on peptide-membrane interactions
    • Gordon-Grossman M, Gofman Y, Zimmermann H, Frydman V, Shai Y, et al. 2009. A combined pulse EPR and Monte Carlo simulation study provides molecular insight on peptide-membrane interactions. J. Phys. Chem. B 113:12687-95
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12687-12695
    • Gordon-Grossman, M.1    Gofman, Y.2    Zimmermann, H.3    Frydman, V.4    Shai, Y.5
  • 111
    • 58849149026 scopus 로고    scopus 로고
    • Backbone structure of transmembrane domain IX of the Na+/proline transporter PutP of Escherichia coli
    • Hilger D, Polyhach Y, Jung H, Jeschke G. 2009. Backbone structure of transmembrane domain IX of the Na+/proline transporter PutP of Escherichia coli. Biophys. J. 96:217-25
    • (2009) Biophys. J. , vol.96 , pp. 217-225
    • Hilger, D.1    Polyhach, Y.2    Jung, H.3    Jeschke, G.4
  • 112
    • 58149380718 scopus 로고    scopus 로고
    • Structure ofmembrane-bound alpha-synuclein from site-directed spin labeling and computational refinement
    • Jao CC, Hegde BG,Chen J,Haworth IS,LangenR. 2008. Structure ofmembrane-bound alpha-synuclein from site-directed spin labeling and computational refinement. Proc. Natl. Acad. Sci. USA 105:19666-71
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19666-19671
    • Jao, C.C.1    Hegde, B.G.2    Chen, J.3    Haworth, I.S.4    Langen, R.5
  • 113
    • 77953906592 scopus 로고    scopus 로고
    • A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins
    • Rao JN, Jao CC, Hegde BG, Langen R, Ulmer TS. 2010. A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins. J. Am. Chem. Soc. 132:8657-68
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 8657-8668
    • Rao, J.N.1    Jao, C.C.2    Hegde, B.G.3    Langen, R.4    Ulmer, T.S.5
  • 114
    • 69849099037 scopus 로고    scopus 로고
    • The orientation of a tandem POTRA domain pair, of the beta-barrel assembly protein BamA, determined by PELDORspectroscopy
    • Ward R, Zoltner M, Beer L, El Mkami H, Henderson IR, et al. 2009. The orientation of a tandem POTRA domain pair, of the beta-barrel assembly protein BamA, determined by PELDORspectroscopy. Structure 17:1187-94
    • (2009) Structure , vol.17 , pp. 1187-1194
    • Ward, R.1    Zoltner, M.2    Beer, L.3    El Mkami, H.4    Henderson, I.R.5
  • 115
    • 77956088408 scopus 로고    scopus 로고
    • Combining NMR and EPR methods for homodimer protein structure determination
    • Yang Y, Ramelot TA, McCarrick RM, Ni S, Feldmann EA, et al. 2010. Combining NMR and EPR methods for homodimer protein structure determination. J. Am. Chem. Soc. 132:11910-13
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11910-11913
    • Yang, Y.1    Ramelot, T.A.2    McCarrick, R.M.3    Ni, S.4    Feldmann, E.A.5
  • 116
    • 51349158003 scopus 로고    scopus 로고
    • Generating properly weighted ensemble of conformations of proteins from sparse or indirect distance constraints
    • Lin M, Lu H, Chen R, Liang J. 2008. Generating properly weighted ensemble of conformations of proteins from sparse or indirect distance constraints. J. Chem. Phys. 129:094101
    • (2008) J. Chem. Phys. , vol.129 , pp. 094101
    • Lin, M.1    Lu, H.2    Chen, R.3    Liang, J.4
  • 117
    • 79851512251 scopus 로고    scopus 로고
    • RosettaEPR: An integrated tool for protein structure determination from sparse EPR data
    • Hirst SJ, Alexander N, McHaourab HS, Meiler J. 2011. RosettaEPR: an integrated tool for protein structure determination from sparse EPR data. J. Struct. Biol. 173:506-14
    • (2011) J. Struct. Biol. , vol.173 , pp. 506-514
    • Hirst, S.J.1    Alexander, N.2    McHaourab, H.S.3    Meiler, J.4
  • 118
    • 78650905964 scopus 로고    scopus 로고
    • ROSETTA3: An object-oriented software suite for the simulation and design of macromolecules
    • Leaver-Fay A, TykaM, Lewis SM, Lange OF,Thompson J, et al. 2010. ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules. Methods Enzymol. 487:545-74
    • (2010) Methods Enzymol. , vol.487 , pp. 545-574
    • Leaver-Fay, A.1    Tyka, M.2    Lewis, S.M.3    Lange, O.F.4    Thompson, J.5
  • 119
    • 38949171385 scopus 로고    scopus 로고
    • De Novo High-Resolution Protein Structure Determination from Sparse Spin-Labeling EPR Data
    • DOI 10.1016/j.str.2007.11.015, PII S0969212608000129
    • Alexander N, Bortolus M, Al-Mestarihi A, McHaourab H, Meiler J. 2008. De novo high-resolution protein structure determination from sparse spin-labeling EPR data. Structure 16:181-95 (Pubitemid 351215214)
    • (2008) Structure , vol.16 , Issue.2 , pp. 181-195
    • Alexander, N.1    Al-Mestarihi, A.2    Bortolus, M.3    Mchaourab, H.4    Meiler, J.5
  • 120
    • 33744811942 scopus 로고    scopus 로고
    • Modeling protein conformational changes by iterative fitting of distance constraints using reoriented normal modes
    • DOI 10.1529/biophysj.105.076836
    • Zheng W, Brooks BR. 2006. Modeling protein conformational changes by iterative fitting of distance constraints using reoriented normal modes. Biophys. J. 90:4327-36 (Pubitemid 43830881)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4327-4336
    • Zheng, W.1    Brooks, B.R.2
  • 121
    • 78650448443 scopus 로고    scopus 로고
    • Prediction of favourable sites for spin labelling of proteins
    • Polyhach Y, Jeschke G. 2010. Prediction of favourable sites for spin labelling of proteins. Spectroscopy 24:651-59
    • (2010) Spectroscopy , vol.24 , pp. 651-659
    • Polyhach, Y.1    Jeschke, G.2
  • 122
    • 79851516036 scopus 로고    scopus 로고
    • Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination
    • Kazmier K, Alexander NS, Meiler J, McHaourab HS. 2011. Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination. J. Struct. Biol. 173:549-57
    • (2011) J. Struct. Biol. , vol.173 , pp. 549-557
    • Kazmier, K.1    Alexander, N.S.2    Meiler, J.3    McHaourab, H.S.4
  • 123
    • 77950282521 scopus 로고    scopus 로고
    • The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria
    • Domingo Köhler S, Weber A, Howard SP, Welte W, Drescher M. 2010. The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria. Protein Sci. 19:625-30
    • (2010) Protein Sci. , vol.19 , pp. 625-630
    • Domingo Köhler, S.1    Weber, A.2    Howard, S.P.3    Welte, W.4    Drescher, M.5
  • 124
    • 78149437446 scopus 로고    scopus 로고
    • The distribution of fatty acids reveals the functional structure of human serum albumin
    • Junk MJN, Spiess HW, Hinderberger D. 2010. The distribution of fatty acids reveals the functional structure of human serum albumin. Angew. Chem. Int. Ed. Engl. 49:8755-59
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 8755-8759
    • Junk, M.J.N.1    Spiess, H.W.2    Hinderberger, D.3
  • 125
    • 79953863928 scopus 로고    scopus 로고
    • Effect of ionic liquids on the solution structure of human serum albumin
    • Akdogan Y, JunkMJN,Hinderberger D. 2011. Effect of ionic liquids on the solution structure of human serum albumin. Biomacromolecules 12:1072-79
    • (2011) Biomacromolecules , vol.12 , pp. 1072-1079
    • Akdogan, Y.1    Junk, M.J.N.2    Hinderberger, D.3
  • 127
    • 79952167215 scopus 로고    scopus 로고
    • Conformation of peptides bound to the transporter associated with antigen processing (TAP)
    • Herget M, Baldauf C, Scholz C, Parcej D,Wiesmuller K, et al. 2011. Conformation of peptides bound to the transporter associated with antigen processing (TAP). Proc. Natl. Acad. Sci. USA 108:1349-54
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1349-1354
    • Herget, M.1    Baldauf, C.2    Scholz, C.3    Parcej, D.4    Wiesmuller, K.5
  • 129
    • 79957699950 scopus 로고    scopus 로고
    • Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation
    • Vileno B, Chamoun J, Liang H, Brewer P, Haldeman BD, et al. 2011. Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation. Proc. Natl. Acad. Sci. USA 108:8218-23
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 8218-8223
    • Vileno, B.1    Chamoun, J.2    Liang, H.3    Brewer, P.4    Haldeman, B.D.5
  • 131
    • 38849101674 scopus 로고    scopus 로고
    • Solutes alter the conformation of the ligand binding loops in outer membrane transporters
    • DOI 10.1021/bi7016415
    • Kim M, Xu Q, Murray D, Cafiso DS. 2007. Solutes alter the conformation of the ligand binding loops in outer membrane transporters. Biochemistry 47:670-79 (Pubitemid 351195438)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 670-679
    • Kim, M.1    Xu, Q.2    Murray, D.3    Cafiso, D.S.4
  • 132
    • 70350520515 scopus 로고    scopus 로고
    • Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy
    • Meyer S, Bohme S, Kruger A, Steinhoff HJ, Klare JP, Wittinghofer A. 2009. Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy. PLoS Biol. 7:e1000212
    • (2009) PLoS Biol. , vol.7
    • Meyer, S.1    Bohme, S.2    Kruger, A.3    Steinhoff, H.J.4    Klare, J.P.5    Wittinghofer, A.6
  • 133
    • 77952787295 scopus 로고    scopus 로고
    • Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy
    • Bohme S, Meyer S, Kruger A, Steinhoff HJ,Wittinghofer A, Klare JP. 2010. Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy. J. Biol. Chem. 285:16991-7000
    • (2010) J. Biol. Chem. , vol.285 , pp. 16991-17000
    • Bohme, S.1    Meyer, S.2    Kruger, A.3    Steinhoff, H.J.4    Wittinghofer, A.5    Klare, J.P.6
  • 135
    • 38949096792 scopus 로고    scopus 로고
    • Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl β-D-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy
    • DOI 10.1021/bi7021377
    • Upadhyay AK, Borbat PP, Wang J, Freed JH, Edmondson DE. 2008. Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl beta-D-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy. Biochemistry 47:1554-66 (Pubitemid 351231206)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1554-1566
    • Upadhyay, A.K.1    Borbat, P.P.2    Wang, J.3    Freed, J.H.4    Edmondson, D.E.5
  • 136
    • 37549042071 scopus 로고    scopus 로고
    • PELDOR spectroscopy with DOPA-beta2 and NH2Y-alpha2s: Distancemeasurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase
    • Seyedsayamdost MR, Chan CT, Mugnaini V, Stubbe J, Bennati M. 2007. PELDOR spectroscopy with DOPA-beta2 and NH2Y-alpha2s: distancemeasurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase. J. Am. Chem. Soc. 129:15748-49
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15748-15749
    • Seyedsayamdost, M.R.1    Chan, C.T.2    Mugnaini, V.3    Stubbe, J.4    Bennati, M.5
  • 137
    • 67749118154 scopus 로고    scopus 로고
    • Molecular-scale force measurement in a coiled-coil peptide dimer by electron spin resonance
    • Gulla SV, Sharma G, Borbat P, Freed JH, Ghimire H, et al. 2009. Molecular-scale force measurement in a coiled-coil peptide dimer by electron spin resonance. J. Am. Chem. Soc. 131:5374-75
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5374-5375
    • Gulla, S.V.1    Sharma, G.2    Borbat, P.3    Freed, J.H.4    Ghimire, H.5


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