메뉴 건너뛰기




Volumn 152, Issue , 2013, Pages 1-82

Pulse dipolar electron spin resonance: Distance measurements

Author keywords

DEER; Dipole dipole; DQC; ESR; PDS; PELDOR; Spin label

Indexed keywords


EID: 84973594607     PISSN: 00815993     EISSN: 16168550     Source Type: Book Series    
DOI: 10.1007/430_2012_82     Document Type: Article
Times cited : (73)

References (178)
  • 1
    • 0037093869 scopus 로고    scopus 로고
    • Protein structure determination using longdistance constraints from double-quantum coherence ESR: Study of T4-lysozyme
    • Borbat PP, Mchaourab HS, Freed JH (2002) Protein structure determination using longdistance constraints from double-quantum coherence ESR: study of T4-lysozyme. J Am Chem Soc 124(19): 5304-5314
    • (2002) J Am Chem Soc , vol.124 , Issue.19 , pp. 5304-5314
    • Borbat, P.P.1    McHaourab, H.S.2    Freed, J.H.3
  • 2
    • 1942487282 scopus 로고    scopus 로고
    • Interresidual distance determination by four-pulse double electron-electron resonance in an integral membrane protein: The Na+/proline transporter PutP of Escherichia coli
    • Jeschke G, Wegener C, Nietschke M, Jung H, Steinhoff H-J (2004) Interresidual distance determination by four-pulse double electron-electron resonance in an integral membrane protein: the Na+/proline transporter PutP of Escherichia coli. Biophys J 86(4): 2551-2557
    • (2004) Biophys J , vol.86 , Issue.4 , pp. 2551-2557
    • Jeschke, G.1    Wegener, C.2    Nietschke, M.3    Jung, H.4    Steinhoff, H.-J.5
  • 6
    • 23244454211 scopus 로고    scopus 로고
    • Assessing oligomerization of membrane proteins by four-pulse DEER: PH-dependent dimerization of NhaA Na+/H + antiporter of E. coli
    • Hilger D, Jung H, Padan E, Wegener C, Vogel K-P, Steinhoff H-J, Jeschke G (2005) Assessing oligomerization of membrane proteins by four-pulse DEER: pH-dependent dimerization of NhaA Na+/H + antiporter of E. coli. Biophys J 89(2): 1328-1338
    • (2005) Biophys J , vol.89 , Issue.2 , pp. 1328-1338
    • Hilger, D.1    Jung, H.2    Padan, E.3    Wegener, C.4    Vogel, K.-P.5    Steinhoff, H.-J.6    Jeschke, G.7
  • 7
    • 18144412431 scopus 로고    scopus 로고
    • Structure and spatial distribution of the spin-labelled lipopeptide trichogin GA IV in a phospholipid membrane studied by pulsed electron-electron double resonance (PELDOR)
    • Milov AD, Erilov DA, Salnikov ES, Tsvetkov YD, Formaggio F, Toniolo C, Raap J (2005) Structure and spatial distribution of the spin-labelled lipopeptide trichogin GA IV in a phospholipid membrane studied by pulsed electron-electron double resonance (PELDOR). Phys Chem Chem Phys 7(8): 1794-1799
    • (2005) Phys Chem Chem Phys , vol.7 , Issue.8 , pp. 1794-1799
    • Milov, A.D.1    Erilov, D.A.2    Salnikov, E.S.3    Tsvetkov, Y.D.4    Formaggio, F.5    Toniolo, C.6    Raap, J.7
  • 8
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with sitedirected spin labeling
    • Hubbell WL, Cafiso DS, Altenbach CA (2000) Identifying conformational changes with sitedirected spin labeling. Nat Struct Biol 7(9): 735-739
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.A.3
  • 9
    • 0030950516 scopus 로고    scopus 로고
    • Molecular distances from dipolar coupled spin-labels: The global analysis of multifrequency continuous wave electron paramagnetic resonance data
    • Hustedt EJ, Smirnov AI, Laub CF, Cobb CE, Beth AH (1997) Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data. Biophys J 72(4): 1861-1877
    • (1997) Biophys J , vol.72 , Issue.4 , pp. 1861-1877
    • Hustedt, E.J.1    Smirnov, A.I.2    Laub, C.F.3    Cobb, C.E.4    Beth, A.H.5
  • 10
    • 27544491667 scopus 로고    scopus 로고
    • EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase
    • Bennati M, Robblee JH, Mugnaini V, Stubbe J, Freed JH, Borbat PP (2005) EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase. J Am Chem Soc 127(43): 15014-15015
    • (2005) J Am Chem Soc , vol.127 , Issue.43 , pp. 15014-15015
    • Bennati, M.1    Robblee, J.H.2    Mugnaini, V.3    Stubbe, J.4    Freed, J.H.5    Borbat, P.P.6
  • 11
    • 33846197463 scopus 로고    scopus 로고
    • Characterizing the structure and dynamics of folded oligomers: Pulsed ESR studies of peptoid helices
    • Fafarman AT, Borbat PP, Freed JH, Kirshenbaum K (2007) Characterizing the structure and dynamics of folded oligomers: pulsed ESR studies of peptoid helices. Chem Commun (4): 377-379
    • (2007) Chem Commun , Issue.4 , pp. 377-379
    • Fafarman, A.T.1    Borbat, P.P.2    Freed, J.H.3    Kirshenbaum, K.4
  • 12
    • 33746894560 scopus 로고    scopus 로고
    • Inter-helix distances in lysophospholipid micelle-bound a-synuclein from pulsed ESR measurements
    • Borbat PP, Ramlall TF, Freed JH, Eliezer D (2006) Inter-helix distances in lysophospholipid micelle-bound a-synuclein from pulsed ESR measurements. J Am Chem Soc 128 (31): 10004-10005
    • (2006) J Am Chem Soc , vol.128 , Issue.31 , pp. 10004-10005
    • Borbat, P.P.1    Ramlall, T.F.2    Freed, J.H.3    Eliezer, D.4
  • 13
    • 16344364195 scopus 로고    scopus 로고
    • Spin-labeled gramicidin a: Channel formation and dissociation
    • Dzikovski BG, Borbat PP, Freed JH (2004) Spin-labeled gramicidin a: channel formation and dissociation. Biophys J 87(5): 3504-3517
    • (2004) Biophys J , vol.87 , Issue.5 , pp. 3504-3517
    • Dzikovski, B.G.1    Borbat, P.P.2    Freed, J.H.3
  • 14
    • 33746302265 scopus 로고    scopus 로고
    • The characterization of weak protein-protein interactions: Evidence from DEER for the trimerization of a von willebrand factor A domain in solution
    • Banham JE, Timmel CR, Abbott RJM, Lea SM, Jeschke G (2006) The characterization of weak protein-protein interactions: evidence from DEER for the trimerization of a von willebrand factor A domain in solution. Angew Chem Int Ed 45(7): 1058-1061
    • (2006) Angew Chem Int Ed , vol.45 , Issue.7 , pp. 1058-1061
    • Banham, J.E.1    Timmel, C.R.2    Abbott, R.J.M.3    Lea, S.M.4    Jeschke, G.5
  • 15
    • 0001590048 scopus 로고    scopus 로고
    • Multiple-quantum ESR and distance measurements
    • Borbat PP, Freed JH (1999) Multiple-quantum ESR and distance measurements. Chem Phys Lett 313(1, 2): 145-154
    • (1999) Chem Phys Lett , vol.313 , Issue.1-2 , pp. 145-154
    • Borbat, P.P.1    Freed, J.H.2
  • 17
    • 0033660661 scopus 로고    scopus 로고
    • New technologies in electron spin resonance
    • Freed JH (2000) New technologies in electron spin resonance. Annu Rev Phys Chem 51: 655-689
    • (2000) Annu Rev Phys Chem , vol.51 , pp. 655-689
    • Freed, J.H.1
  • 18
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci GE, Cafiso DS (2006) Recent advances and applications of site-directed spin labeling. Curr Opin Struct Biol 16(5): 644-653
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.5 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 19
    • 0036606899 scopus 로고    scopus 로고
    • A new spin on protein dynamics
    • Columbus L, Hubbell WL (2002) A new spin on protein dynamics. Trends Biochem Sci 27(6): 288-295
    • (2002) Trends Biochem Sci , vol.27 , Issue.6 , pp. 288-295
    • Columbus, L.1    Hubbell, W.L.2
  • 20
    • 0345169924 scopus 로고    scopus 로고
    • Self-assembling and membrane modifying properties of a lipopeptaibol studied by CW-ESR and PELDOR spectroscopies
    • Milov AD, Tsvetkov YD, Formaggio F, Crisma M, Toniolo C, Raap J (2003) Self-assembling and membrane modifying properties of a lipopeptaibol studied by CW-ESR and PELDOR spectroscopies. J Pept Sci 9(11-12): 690-700
    • (2003) J Pept Sci , vol.9 , Issue.11-12 , pp. 690-700
    • Milov, A.D.1    Tsvetkov, Y.D.2    Formaggio, F.3    Crisma, M.4    Toniolo, C.5    Raap, J.6
  • 21
    • 33748630529 scopus 로고    scopus 로고
    • High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase
    • Denysenkov VP, Prisner TF, Stubbe J, Bennati M (2006) High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase. Proc Natl Acad Sci USA 103(36): 13386-13390
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.36 , pp. 13386-13390
    • Denysenkov, V.P.1    Prisner, T.F.2    Stubbe, J.3    Bennati, M.4
  • 22
    • 28844488267 scopus 로고    scopus 로고
    • Double quantum coherence electron spin resonance on coupled Cu(II)-Cu(II) electron spins
    • Becker JS, Saxena S (2005) Double quantum coherence electron spin resonance on coupled Cu(II)-Cu(II) electron spins. Chem Phys Lett 414(1-3): 248-252
    • (2005) Chem Phys Lett , vol.414 , Issue.1-3 , pp. 248-252
    • Becker, J.S.1    Saxena, S.2
  • 24
    • 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
    • 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 41(20): 3907-3910
    • (2002) Angew Chem Int Ed , vol.41 , Issue.20 , pp. 3907-3910
    • Narr, E.1    Godt, A.2    Jeschke, G.3
  • 25
    • 0036936765 scopus 로고    scopus 로고
    • Pulsed ELDOR spectroscopy of the Mo(V)/Fe(III) state of sulfite oxidase prepared by one-electron reduction with Ti(III) citrate
    • Codd R, Astashkin AV, Pacheco A, Raitsimring AM, Enemark JH (2002) Pulsed ELDOR spectroscopy of the Mo(V)/Fe(III) state of sulfite oxidase prepared by one-electron reduction with Ti(III) citrate. J Biol Inorg Chem 7(3): 338-350
    • (2002) J Biol Inorg Chem , vol.7 , Issue.3 , pp. 338-350
    • Codd, R.1    Astashkin, A.V.2    Pacheco, A.3    Raitsimring, A.M.4    Enemark, J.H.5
  • 26
    • 0037164101 scopus 로고    scopus 로고
    • Pulsed electron-electron double resonance on multinuclear metal clusters: Assignment of spin projection factors based on the dipolar interaction
    • 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(42): 12606-12611
    • (2002) J Am Chem Soc , vol.124 , Issue.42 , pp. 12606-12611
    • Elsaesser, C.1    Brecht, M.2    Bittl, R.3
  • 27
    • 38949096792 scopus 로고    scopus 로고
    • 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
    • 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(6): 1554-1566
    • (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
  • 28
    • 0028022949 scopus 로고
    • Distance between tyrosines Z+ and D+ in plant photosystem II as determined by pulsed EPR
    • Astashkin AV, Kodera Y, Kawamori A (1994) Distance between tyrosines Z+ and D+ in plant photosystem II as determined by pulsed EPR. Biochim Biophys Acta 1187(1): 89-93
    • (1994) Biochim Biophys Acta , vol.1187 , Issue.1 , pp. 89-93
    • Astashkin, A.V.1    Kodera, Y.2    Kawamori, A.3
  • 29
    • 0000330099 scopus 로고
    • Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids
    • Milov AD, Salikhov KM, Shirov MD (1981) Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids. Soviet Phys-Solid State 23: 565-569
    • (1981) Soviet Phys-Solid State , vol.23 , pp. 565-569
    • Milov, A.D.1    Salikhov, K.M.2    Shirov, M.D.3
  • 30
    • 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(1): 107-143
    • (1998) Appl Magn Reson , vol.15 , Issue.1 , pp. 107-143
    • Milov, A.D.1    Maryasov, A.G.2    Tsvetkov, Y.D.3
  • 31
    • 84973666564 scopus 로고    scopus 로고
    • Determination of end-to-end distances in a series of TEMPO diradicals 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 with a new four-pulse double electron electron resonance experiment. Angew Chem Int Ed 100(32): 13428-13432
    • (1998) Angew Chem Int Ed , vol.100 , Issue.32 , pp. 13428-13432
    • Martin, R.E.1    Pannier, M.2    Diederich, F.3    Gramlich, V.4    Hubrich, M.5    Spiess, H.W.6
  • 32
    • 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(7): 5134-5146
    • (1993) J Chem Phys , vol.98 , Issue.7 , pp. 5134-5146
    • Larsen, R.G.1    Singel, D.J.2
  • 33
    • 0000817613 scopus 로고
    • Electron spin echo method as used to analyze the spatial distribution of paramagnetic centers
    • Raitsimring AM, Salikhov KM (1985) Electron spin echo method as used to analyze the spatial distribution of paramagnetic centers. Bull Magn Reson 7(4): 184-217
    • (1985) Bull Magn Reson , vol.7 , Issue.4 , pp. 184-217
    • Raitsimring, A.M.1    Salikhov, K.M.2
  • 34
    • 0000890494 scopus 로고
    • The theory of electron spin-echo signal decay resulting from dipole-dipole interactions between paramagnetic centers in solids
    • Salikhov KM, Dzyuba SA, Raitsimring A (1981) The theory of electron spin-echo signal decay resulting from dipole-dipole interactions between paramagnetic centers in solids. J Magn Reson 42(2): 255-276
    • (1981) J Magn Reson , vol.42 , Issue.2 , pp. 255-276
    • Salikhov, K.M.1    Dzyuba, S.A.2    Raitsimring, A.3
  • 35
    • 0001773735 scopus 로고    scopus 로고
    • Distance measurements in biological systems by EPR
    • Berliner LJ, Eaton GR, Eaton SS (eds) Academic/ Plenum, New York
    • Borbat PP, Freed JH (2000) Distance measurements in biological systems by EPR. In: Berliner LJ, Eaton GR, Eaton SS (eds) Biological magnetic resonance, vol 19. Academic/ Plenum, New York, pp 385-459
    • (2000) Biological magnetic resonance, vol 19 , pp. 385-459
    • Borbat, P.P.1    Freed, J.H.2
  • 36
    • 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(2, 3): 243-252
    • (2000) Chem Phys Lett , vol.331 , Issue.2-3 , pp. 243-252
    • Jeschke, G.1    Pannier, M.2    Godt, A.3    Spiess, H.W.4
  • 37
    • 0001197969 scopus 로고    scopus 로고
    • Electron dipole-dipole interaction in ESEEM of nitroxide biradicals
    • Kulik LV, Dzuba SA, Grigoryev IA, Tsvetkov YD (2001) Electron dipole-dipole interaction in ESEEM of nitroxide biradicals. Chem Phys Lett 343(3, 4): 315-324
    • (2001) Chem Phys Lett , vol.343 , Issue.3-4 , pp. 315-324
    • Kulik, L.V.1    Dzuba, S.A.2    Grigoryev, I.A.3    Tsvetkov, Y.D.4
  • 38
    • 45149146601 scopus 로고
    • Selection of dipolar interaction by the "2 +1" pulse train ESE (1969-1992)
    • Kurshev VV, Raitsimring AM, Tsvetkov YD (1989) Selection of dipolar interaction by the "2 +1" pulse train ESE (1969-1992). J Magn Reson 81(3): 441-454
    • (1989) J Magn Reson , vol.81 , Issue.3 , pp. 441-454
    • Kurshev, V.V.1    Raitsimring, A.M.2    Tsvetkov, Y.D.3
  • 40
    • 8344224484 scopus 로고    scopus 로고
    • Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction
    • Steinhoff H-J (2004) Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction. Biol Chem 385(10): 913-920
    • (2004) Biol Chem , vol.385 , Issue.10 , pp. 913-920
    • Steinhoff, H.-J.1
  • 41
    • 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 PG (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(18): S1459-S1469
    • (2005) J Phys Condens Matter , vol.17 , Issue.18 , pp. S1459-S1469
    • Fajer, P.G.1
  • 43
    • 0011220727 scopus 로고
    • Theory of saturation and double resonance effects in electron spin resonance spectra. 2. Exchange vs dipolar mechanisms
    • Freed JH (1967) Theory of saturation and double resonance effects in electron spin resonance spectra. 2. Exchange vs dipolar mechanisms. J Phys Chem 71(1): 38-51
    • (1967) J Phys Chem , vol.71 , Issue.1 , pp. 38-51
    • Freed, J.H.1
  • 44
    • 36849105502 scopus 로고
    • Theory of spin relaxation via quantum-molecular systems - Resonance effects
    • Freed JH (1966) Theory of spin relaxation via quantum-molecular systems - resonance effects. J Chem Phys 45(4): 1251-1257
    • (1966) J Chem Phys , vol.45 , Issue.4 , pp. 1251-1257
    • Freed, J.H.1
  • 45
    • 0011147112 scopus 로고
    • Theory of saturation and double-resonance effects in ESR spectra
    • Freed JH (1965) Theory of saturation and double-resonance effects in ESR spectra. J Chem Phys 43(7): 2312-2332
    • (1965) J Chem Phys , vol.43 , Issue.7 , pp. 2312-2332
    • Freed, J.H.1
  • 46
    • 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 PAS, 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 (10): 103102-103115
    • (2009) Rev Sci Instrum , vol.80 , Issue.10 , pp. 103102-103115
    • Cruickshank, P.A.S.1    Bolton, D.R.2    Robertson, D.A.3    Hunter, R.I.4    Wylde, R.J.5    Smith, G.M.6
  • 51
    • 38149039368 scopus 로고    scopus 로고
    • Cryogenic Q-band (35 GHz) probehead featuring large excitation microwave fields for pulse and continuous wave electron paramagnetic resonance spectroscopy: Performance and applications
    • Forrer J, Garcia-Rubio I, Schuhmam R, Tschaggelar R, Harmer J (2008) Cryogenic Q-band (35 GHz) probehead featuring large excitation microwave fields for pulse and continuous wave electron paramagnetic resonance spectroscopy: performance and applications. J Magn Reson 190(2): 280-291
    • (2008) J Magn Reson , vol.190 , Issue.2 , pp. 280-291
    • Forrer, J.1    Garcia-Rubio, I.2    Schuhmam, R.3    Tschaggelar, R.4    Harmer, J.5
  • 52
    • 33745700182 scopus 로고    scopus 로고
    • Probehead operating at 35 GHz for continuous wave and pulse electron paramagnetic resonance applications
    • Gromov I, Forrer J, Schweiger A (2006) Probehead operating at 35 GHz for continuous wave and pulse electron paramagnetic resonance applications. Rev Sci Instrum 77(6), Article Number: 064704
    • (2006) Rev Sci Instrum , vol.77 , Issue.6
    • Gromov, I.1    Forrer, J.2    Schweiger, A.3
  • 53
    • 33745714237 scopus 로고    scopus 로고
    • Design of Q-band loop-gap resonators at frequencies of 34-36 GHz for single electron spin spectroscopy in semiconductor nanostructures
    • Simovic B, Studerus P, Gustavsson S, Leturcq R, Ensslin K, Schuhmann R, Forrer J, Schweiger A (2006) Design of Q-band loop-gap resonators at frequencies of 34-36 GHz for single electron spin spectroscopy in semiconductor nanostructures. Rev Sci Instrum 77(6), Article Number: 064702
    • (2006) Rev Sci Instrum , vol.77 , Issue.6
    • Simovic, B.1    Studerus, P.2    Gustavsson, S.3    Leturcq, R.4    Ensslin, K.5    Schuhmann, R.6    Forrer, J.7    Schweiger, A.8
  • 55
    • 54749154073 scopus 로고    scopus 로고
    • Dielectric microwave resonators in TE (011) cavities for electron paramagnetic resonance spectroscopy
    • Mett RR, Sidabras JW, Golovina IS, Hyde JS (2008) Dielectric microwave resonators in TE (011) cavities for electron paramagnetic resonance spectroscopy. Rev Sci Instrum 79(9), Article Number: 094702
    • (2008) Rev Sci Instrum , vol.79 , Issue.9
    • Mett, R.R.1    Sidabras, J.W.2    Golovina, I.S.3    Hyde, J.S.4
  • 56
    • 34249036549 scopus 로고    scopus 로고
    • Uniform radio frequency fields in loop-gap resonators for EPR spectroscopy
    • Mett RR, Sidabras JW, Hyde JS (2007) Uniform radio frequency fields in loop-gap resonators for EPR spectroscopy. Appl Magn Reson 31(3-4): 573-589
    • (2007) Appl Magn Reson , vol.31 , Issue.3-4 , pp. 573-589
    • Mett, R.R.1    Sidabras, J.W.2    Hyde, J.S.3
  • 57
    • 79953219014 scopus 로고    scopus 로고
    • A dual-mode microwave resonator for double electron-electron spin resonance spectroscopy at W-band microwave frequencies
    • Tkach I, Sicoli G, Hobartner C, Bennati M (2011) A dual-mode microwave resonator for double electron-electron spin resonance spectroscopy at W-band microwave frequencies. J Magn Reson 209(2): 341-346
    • (2011) J Magn Reson , vol.209 , Issue.2 , pp. 341-346
    • Tkach, I.1    Sicoli, G.2    Hobartner, C.3    Bennati, M.4
  • 58
    • 3042690165 scopus 로고    scopus 로고
    • Measurement of large distances in biomolecules using double-quantum filtered refocused electron spin-echoes
    • Borbat PP, Davis JH, Butcher SE, Freed JH (2004) Measurement of large distances in biomolecules using double-quantum filtered refocused electron spin-echoes. J Am Chem Soc 126(25): 7746-7747
    • (2004) J Am Chem Soc , vol.126 , Issue.25 , pp. 7746-7747
    • Borbat, P.P.1    Davis, J.H.2    Butcher, S.E.3    Freed, J.H.4
  • 60
    • 43949130403 scopus 로고    scopus 로고
    • Observer-selective double electron-electronspin resonance, a pulse sequence to improve orientation selection
    • Milikisyants S, Groenen EJJ, Huber M (2008) Observer-selective double electron-electronspin resonance, a pulse sequence to improve orientation selection. J Magn Reson 192(2): 275-279
    • (2008) J Magn Reson , vol.192 , Issue.2 , pp. 275-279
    • Milikisyants, S.1    Groenen, E.J.J.2    Huber, M.3
  • 61
    • 70349734868 scopus 로고    scopus 로고
    • A pulsed EPR method to determine distances between paramagnetic centers with strong spectral anisotropy and radicals: The dead-time free RIDME sequence
    • Milikisyants S, Scarpelli F, Finiguerra MG, Ubbink M, Huber M (2009) A pulsed EPR method to determine distances between paramagnetic centers with strong spectral anisotropy and radicals: the dead-time free RIDME sequence. J Magn Reson 201(1): 48-56
    • (2009) J Magn Reson , vol.201 , Issue.1 , pp. 48-56
    • Milikisyants, S.1    Scarpelli, F.2    Finiguerra, M.G.3    Ubbink, M.4    Huber, M.5
  • 62
    • 79851512251 scopus 로고    scopus 로고
    • An integrated tool for protein structure determination from sparse EPR data
    • Hirst SJ, Alexander N, Mchaourab HS, Meiler J (2011) Rosetta EPR: an integrated tool for protein structure determination from sparse EPR data. J Struct Biol 173(3): 506-514
    • (2011) J Struct Biol , vol.173 , Issue.3 , pp. 506-514
    • Hirst, S.J.1    Alexander, N.2    McHaourab, H.S.3    Meiler, J.4
  • 64
    • 34250874047 scopus 로고    scopus 로고
    • Rigid body refinement of protein complexes with long-range distance restraints from pulsed dipolar ESR. Two-component signaling systems
    • Bhatnagar J, Freed JH, Crane BR (2007) Rigid body refinement of protein complexes with long-range distance restraints from pulsed dipolar ESR. Two-component signaling systems. Methods Enzymol B 423: 117-133
    • (2007) Methods Enzymol B , vol.423 , pp. 117-133
    • Bhatnagar, J.1    Freed, J.H.2    Crane, B.R.3
  • 65
    • 77951922143 scopus 로고    scopus 로고
    • Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the Che A histidine kinase, and the coupling protein Che W As determined by pulsed dipolar ESR spectroscopy
    • Bhatnagar J, Borbat PP, Pollard AM, Bilwes AM, Freed JH, Crane BR (2010) Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW As determined by pulsed dipolar ESR spectroscopy. Biochemistry 49(18): 3824-3841
    • (2010) Biochemistry , vol.49 , Issue.18 , pp. 3824-3841
    • Bhatnagar, J.1    Borbat, P.P.2    Pollard, A.M.3    Bilwes, A.M.4    Freed, J.H.5    Crane, B.R.6
  • 67
    • 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(1-2): 223-244
    • (2004) Appl Magn Reson , vol.26 , Issue.1-2 , pp. 223-244
    • Jeschke, G.1    Panek, G.2    Godt, A.3    Bender, A.4    Paulsen, H.5
  • 68
    • 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(6): 2356-2366
    • (2011) Phys Chem Chem Phys , vol.13 , Issue.6 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 69
    • 28044472953 scopus 로고    scopus 로고
    • Maximum entropy: A complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR
    • Chiang Y-W, 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(2): 184-196
    • (2005) J Magn Reson , vol.177 , Issue.2 , pp. 184-196
    • Chiang, Y.-W.1    Borbat, P.P.2    Freed, J.H.3
  • 70
    • 11344285129 scopus 로고    scopus 로고
    • The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    • Chiang Y-W, Borbat PP, Freed JH (2005) The determination of pair distance distributions by pulsed ESR using Tikhonov regularization. J Magn Reson 172(2): 279-295
    • (2005) J Magn Reson , vol.172 , Issue.2 , pp. 279-295
    • Chiang, Y.-W.1    Borbat, P.P.2    Freed, J.H.3
  • 73
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke G (2002) Distance measurements in the nanometer range by pulse EPR. Chemphyschem 3(11): 927-932
    • (2002) Chemphyschem , vol.3 , Issue.11 , pp. 927-932
    • Jeschke, G.1
  • 74
    • 34250902869 scopus 로고    scopus 로고
    • Pulsed EPR structural studies in the nanometer range of distances
    • Dzuba SA (2005) Pulsed EPR structural studies in the nanometer range of distances. Russian Chem Rev 74(7): 619-637
    • (2005) Russian Chem Rev , vol.74 , Issue.7 , pp. 619-637
    • Dzuba, S.A.1
  • 75
    • 0034743154 scopus 로고    scopus 로고
    • Pulsed EPR spectroscopy: Biological applications
    • Prisner T, Rohrer M, MacMillan F (2001) Pulsed EPR spectroscopy: biological applications. Annu Rev Phys Chem 52: 279-313
    • (2001) Annu Rev Phys Chem , vol.52 , pp. 279-313
    • Prisner, T.1    Rohrer, M.2    McMillan, F.3
  • 78
    • 33749178896 scopus 로고    scopus 로고
    • Distance measurements in solid-state NMR and EPR spectroscopy
    • Dolinsek J, Vilfan M, Zumer S (eds) Springer, Berlin
    • Jeschke G, Spiess HW (2006) Distance measurements in solid-state NMR and EPR spectroscopy. In: Dolinsek J, Vilfan M, Zumer S (eds) Novel NMR and EPR techniques. Springer, Berlin, pp 21-63
    • (2006) Novel NMR and EPR techniques , pp. 21-63
    • Jeschke, G.1    Spiess, H.W.2
  • 79
    • 0642327965 scopus 로고
    • Nuclear resonance absorption in hydrated crystals: Fine structure of the proton line
    • Pake GE (1948) Nuclear resonance absorption in hydrated crystals: fine structure of the proton line. J Chem Phys 16: 327-336
    • (1948) J Chem Phys , vol.16 , pp. 327-336
    • Pake, G.E.1
  • 80
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein MD, Shin Y-K (1995) Determination of the distance between two spin labels attached to a macromolecule. Proc Natl Acad Sci USA 92(18): 8239-8243
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.18 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.-K.2
  • 81
    • 42949177561 scopus 로고    scopus 로고
    • High-frequency dynamic nuclear polarization using biradicals: A multifrequency EPR lineshape analysis
    • Hu KN, Song C, Yu HH, Swager TM, Griffin RG (2008) High-frequency dynamic nuclear polarization using biradicals: a multifrequency EPR lineshape analysis. J Chem Phys 128(5), Article Number: 052302
    • (2008) J Chem Phys , vol.128 , Issue.5
    • Hu, K.N.1    Song, C.2    Yu, H.H.3    Swager, T.M.4    Griffin, R.G.5
  • 82
    • 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 JR, Hammarstrom P, Mitri R, Martensson L-G, Carlsson U, Eaton GR, Eaton SS (2001) Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II. Biophys J 80(6): 2886-2897
    • (2001) Biophys J , vol.80 , Issue.6 , 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
  • 83
    • 0033607618 scopus 로고    scopus 로고
    • Folding pattern of the a-crystallin domain in aA-crystallin determined by site-directed spin labeling
    • Koteiche HA, Mchaourab HS (1999) Folding pattern of the a-crystallin domain in aA-crystallin determined by site-directed spin labeling. J Mol Biol 294(2): 561-577
    • (1999) J Mol Biol , vol.294 , Issue.2 , pp. 561-577
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 85
    • 0035066645 scopus 로고    scopus 로고
    • The neuronal t-SNARE complex is a parallel four-helix bundle
    • Xiao W, Poirier MA, Bennett MK, Shin Y-K (2001) The neuronal t-SNARE complex is a parallel four-helix bundle. Nat Struct Biol 8(4): 308-311
    • (2001) Nat Struct Biol , vol.8 , Issue.4 , pp. 308-311
    • Xiao, W.1    Poirier, M.A.2    Bennett, M.K.3    Shin, Y.-K.4
  • 86
    • 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, Baker CM, Ceola S, Day IJ, Grant GH, Groenen EJJ, Rodgers CT, Jeschke G, Timmel CR (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(2): 202-218
    • (2008) J Magn Reson , vol.191 , Issue.2 , pp. 202-218
    • Banham, J.E.1    Baker, C.M.2    Ceola, S.3    Day, I.J.4    Grant, G.H.5    Groenen, E.J.J.6    Rodgers, C.T.7    Jeschke, G.8    Timmel, C.R.9
  • 88
    • 33749622370 scopus 로고
    • Spin echoes
    • Hahn EL (1950) Spin echoes. Phys Rev 80(4): 580-594
    • (1950) Phys Rev , vol.80 , Issue.4 , pp. 580-594
    • Hahn, E.L.1
  • 89
    • 35949043972 scopus 로고
    • Envelope modulation in spin-echo experiments
    • Mims WB (1972) Envelope modulation in spin-echo experiments. Phys Rev B-Solid State 5(7): 2409-2419
    • (1972) Phys Rev B-Solid State , vol.5 , Issue.7 , pp. 2409-2419
    • Mims, W.B.1
  • 90
    • 36749112745 scopus 로고
    • Nuclear modulation effect in electron-spin echoes for complexes of Cu2+ and imidazole with N-14 and N-15
    • Mims WB, Peisach J (1978) Nuclear modulation effect in electron-spin echoes for complexes of Cu2+ and imidazole with N-14 and N-15. J Chem Phys 69(11): 4921-4930
    • (1978) J Chem Phys , vol.69 , Issue.11 , pp. 4921-4930
    • Mims, W.B.1    Peisach, J.2
  • 93
    • 79960890461 scopus 로고    scopus 로고
    • Calculation of double-quantum-coherence twodimensional spectra: Distance measurements and orientational correlations
    • Misra SK, Borbat PP, Freed JH (2009) Calculation of double-quantum-coherence twodimensional spectra: distance measurements and orientational correlations. Appl Magn Reson 36(2-4): 237-258
    • (2009) Appl Magn Reson , vol.36 , Issue.2-4 , pp. 237-258
    • Misra, S.K.1    Borbat, P.P.2    Freed, J.H.3
  • 98
    • 34247478142 scopus 로고    scopus 로고
    • Dynamic phase shifts in nanoscale distance measurements by double electron electron resonance (DEER)
    • Bowman MK, Maryasov AG (2007) Dynamic phase shifts in nanoscale distance measurements by double electron electron resonance (DEER). J Magn Reson 185 (2): 270-282
    • (2007) J Magn Reson , vol.185 , Issue.2 , pp. 270-282
    • Bowman, M.K.1    Maryasov, A.G.2
  • 100
    • 0030584398 scopus 로고    scopus 로고
    • Double quantum two-dimensional Fourier transform electron spin resonance: Distance measurements
    • Saxena S, Freed JH (1996) Double quantum two-dimensional Fourier transform electron spin resonance: distance measurements. Chem Phys Lett 251(1): 102-110
    • (1996) Chem Phys Lett , vol.251 , Issue.1 , pp. 102-110
    • Saxena, S.1    Freed, J.H.2
  • 101
    • 51649117568 scopus 로고    scopus 로고
    • Pro's and con's of pulse dipolar ESR: DQC and DEER
    • Borbat PP, Freed JH (2007) Pro's and con's of pulse dipolar ESR: DQC and DEER. EPR Newslett 17(2-3): 21-33
    • (2007) EPR Newslett , vol.17 , Issue.2-3 , pp. 21-33
    • Borbat, P.P.1    Freed, J.H.2
  • 102
    • 0031206837 scopus 로고    scopus 로고
    • Theory of double quantum two-dimensional electron spin resonance with application to distance measurements
    • Saxena S, Freed JH (1997) Theory of double quantum two-dimensional electron spin resonance with application to distance measurements. J Chem Phys 107(5): 1317-1340
    • (1997) J Chem Phys , vol.107 , Issue.5 , pp. 1317-1340
    • Saxena, S.1    Freed, J.H.2
  • 103
    • 0001427737 scopus 로고
    • Orientation dependence of electron spin resonance spectrum of di tert butyl nitroxide
    • Libertini LJ, Griffith OH (1970) Orientation dependence of electron spin resonance spectrum of di tert butyl nitroxide. J Chem Phys 53(4): 1359-1367
    • (1970) J Chem Phys , vol.53 , Issue.4 , pp. 1359-1367
    • Libertini, L.J.1    Griffith, O.H.2
  • 104
    • 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(4): 583-605
    • (2000) Appl Magn Reson , vol.18 , Issue.4 , pp. 583-605
    • Maryasov, A.G.1    Tsvetkov, Y.D.2
  • 105
    • 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(1): 67-72
    • (1984) Chem Phys Lett , vol.110 , Issue.1 , pp. 67-72
    • Milov, A.D.1    Ponomarev, A.B.2    Tsvetkov, Y.D.3
  • 106
    • 0001773735 scopus 로고    scopus 로고
    • Distance measurements in biological systems by EPR
    • Berliner LJ, Eaton GR, Eaton SS (eds) Kluwer, New York
    • Raitsimring A (2000) Distance measurements in biological systems by EPR. In: Berliner LJ, Eaton GR, Eaton SS (eds) Biological magnetic resonance, vol 19. Kluwer, New York, pp 385-459
    • (2000) Biological magnetic resonance, vol 19 , pp. 385-459
    • Raitsimring, A.1
  • 107
    • 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(2): 331-340
    • (2000) J Magn Reson , vol.142 , Issue.2 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 108
    • 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(2): 277-285
    • (2002) J Magn Reson , vol.157 , Issue.2 , pp. 277-285
    • Weber, A.1    Schiemann, O.2    Bode, B.3    Prisner, T.F.4
  • 109
    • 0031485790 scopus 로고    scopus 로고
    • Double electron-electron resonance in electron spin echo. Conformations of spin-labeled poly-4-vinylpyridine in glassy solutions
    • Milov AD, Tsvetkov YD (1997) Double electron-electron resonance in electron spin echo. Conformations of spin-labeled poly-4-vinylpyridine in glassy solutions. Appl Magn Reson 12(4): 495-504
    • (1997) Appl Magn Reson , vol.12 , Issue.4 , pp. 495-504
    • Milov, A.D.1    Tsvetkov, Y.D.2
  • 110
    • 0001267309 scopus 로고
    • Phase relaxation of hydrogen atoms stabilized in an amorphous matrix
    • Milov AD, Salikhov KM, Tsvetkov YD (1973) Phase relaxation of hydrogen atoms stabilized in an amorphous matrix. Soviet Phys-Solid State 15: 802-806
    • (1973) Soviet Phys-Solid State , vol.15 , pp. 802-806
    • Milov, A.D.1    Salikhov, K.M.2    Tsvetkov, Y.D.3
  • 113
    • 0000484383 scopus 로고    scopus 로고
    • Dephasing of electron spin echoes for nitroxyl radicals in glassy solvents by non-methyl and methyl protons
    • Zecevic A, Eaton GR, Eaton SS, Lindgren M (1998) Dephasing of electron spin echoes for nitroxyl radicals in glassy solvents by non-methyl and methyl protons. Mol Phys 95 (6): 1255-1263
    • (1998) Mol Phys , vol.95 , Issue.6 , pp. 1255-1263
    • Zecevic, A.1    Eaton, G.R.2    Eaton, S.S.3    Lindgren, M.4
  • 114
    • 0035951161 scopus 로고    scopus 로고
    • Phase memory relaxation times of spin labels in human carbonic anhydrase II: Pulsed EPR to determine spin label location
    • Huber M, Lindgren M, Hammarstrom P, Martensson L-G, Carlsson U, Eaton GR, Eaton SS (2001) Phase memory relaxation times of spin labels in human carbonic anhydrase II: pulsed EPR to determine spin label location. Biophys Chem 94(3): 245-256
    • (2001) Biophys Chem , vol.94 , Issue.3 , pp. 245-256
    • Huber, M.1    Lindgren, M.2    Hammarstrom, P.3    Martensson, L.-G.4    Carlsson, U.5    Eaton, G.R.6    Eaton, S.S.7
  • 115
    • 33646580725 scopus 로고    scopus 로고
    • Time-resolved electron spin resonance studies of spin-labelled lipids in membranes
    • Bartucci R, Erilov DA, Guzzi R, Sportelli L, Dzuba SA, Marsh D (2006) Time-resolved electron spin resonance studies of spin-labelled lipids in membranes. Chem Phys Lipids 141 (1-2): 142-157
    • (2006) Chem Phys Lipids , vol.141 , Issue.1-2 , pp. 142-157
    • Bartucci, R.1    Erilov, D.A.2    Guzzi, R.3    Sportelli, L.4    Dzuba, S.A.5    Marsh, D.6
  • 116
    • 77956258196 scopus 로고    scopus 로고
    • The lipid-binding domain of wild type and mutant alpha-synuclein: Compactness and interconversion between the broken and extended helix forms
    • Georgieva ER, Ramlall TF, Borbat PP, Freed JH, Eliezer D (2010) The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms. J Biol Chem 285(36): 28261-28274
    • (2010) J Biol Chem , vol.285 , Issue.36 , pp. 28261-28274
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 117
    • 0035827966 scopus 로고    scopus 로고
    • A many-body analysis of the effects of the matrix protons and their diffusional motion on electron spin resonance line shapes and electron spin echoes
    • Nevzorov AA, Freed JH (2001) A many-body analysis of the effects of the matrix protons and their diffusional motion on electron spin resonance line shapes and electron spin echoes. J Chem Phys 115(6): 2416-2429
    • (2001) J Chem Phys , vol.115 , Issue.6 , pp. 2416-2429
    • Nevzorov, A.A.1    Freed, J.H.2
  • 118
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alphasynuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • Georgieva ER, Ramlall TF, Borbat PP, Freed JH, Eliezer D (2008) Membrane-bound alphasynuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles. J Am Chem Soc 130(39): 12856-12857
    • (2008) J Am Chem Soc , vol.130 , Issue.39 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 120
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr HY, Purcell EM (1954) Effects of diffusion on free precession in nuclear magnetic resonance experiments. Phys Rev 94(3): 630-638
    • (1954) Phys Rev , vol.94 , Issue.3 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 121
    • 79952787086 scopus 로고    scopus 로고
    • Double electron-electron resonance measured between Gd(3+) ions and nitroxide radicals
    • Lueders P, Jeschke G, Yulikov M (2011) Double electron-electron resonance measured between Gd(3+) ions and nitroxide radicals. J Phys Chem Lett 2(6): 604-609
    • (2011) J Phys Chem Lett , vol.2 , Issue.6 , pp. 604-609
    • Lueders, P.1    Jeschke, G.2    Yulikov, M.3
  • 122
    • 34250841296 scopus 로고    scopus 로고
    • Measuring distances by pulsed dipolar ESR spectroscopy: Spinlabeled histidine kinases
    • Simon MI, Crane BR, Crane A (eds). Elsevier, San Diego
    • Borbat PP, Freed JH (2007) Measuring distances by pulsed dipolar ESR spectroscopy: spinlabeled histidine kinases. In: Simon MI, Crane BR, Crane A (eds) Two-component signaling systems, Pt B, vol. 423. Methods in enzymology. Elsevier, San Diego, pp 52-116
    • (2007) Two-component signaling systems, Pt B, vol. 423. Methods in enzymology , pp. 52-116
    • Borbat, P.P.1    Freed, J.H.2
  • 123
    • 0030596171 scopus 로고    scopus 로고
    • Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15 N and 1H assignments of human carbonic anhydrase II
    • Venters RA, Farmer BT II, Fierke CA, Spicer LD (1996) Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15 N and 1H assignments of human carbonic anhydrase II. J Mol Biol 264(5): 1101-1116
    • (1996) J Mol Biol , vol.264 , Issue.5 , pp. 1101-1116
    • Venters, R.A.1    Farmer, B.T.2    Fierke, C.A.3    Spicer, L.D.4
  • 125
    • 22144435546 scopus 로고    scopus 로고
    • The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy
    • Hamel DJ, Dahlquist FW (2005) The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy. J Am Chem Soc 127(27): 9676-9677
    • (2005) J Am Chem Soc , vol.127 , Issue.27 , pp. 9676-9677
    • Hamel, D.J.1    Dahlquist, F.W.2
  • 126
    • 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(1): 72-82
    • (2002) J Magn Reson , vol.155 , Issue.1 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 127
    • 3042741373 scopus 로고    scopus 로고
    • Visualization of distance distribution from pulsed double electron-electron resonance data
    • Bowman MK, Maryasov AG, Kim N, De Rose VJ (2004) Visualization of distance distribution from pulsed double electron-electron resonance data. Appl Magn Reson 26(1-2): 23-39
    • (2004) Appl Magn Reson , vol.26 , Issue.1-2 , pp. 23-39
    • Bowman, M.K.1    Maryasov, A.G.2    Kim, N.3    De Rose, V.J.4
  • 128
    • 0000210354 scopus 로고
    • Theory of two-dimensional Fourier transform electron spin resonance for ordered and viscous fluids
    • Lee S, Budil DE, Freed JH (1994) Theory of two-dimensional Fourier transform electron spin resonance for ordered and viscous fluids. J Chem Phys 101(7): 5529-5558
    • (1994) J Chem Phys , vol.101 , Issue.7 , pp. 5529-5558
    • Lee, S.1    Budil, D.E.2    Freed, J.H.3
  • 129
    • 84860464639 scopus 로고    scopus 로고
    • Self-association of the histidine kinase CheA as studied by pulsed dipolar ESR spectroscopy
    • Bhatnagar J, Sircar R, Borbat PP, Freed JH, Crane BR (2012) Self-association of the histidine kinase CheA as studied by pulsed dipolar ESR spectroscopy. Biophys J 102(9): 2192-2201
    • (2012) Biophys J , vol.102 , Issue.9 , pp. 2192-2201
    • Bhatnagar, J.1    Sircar, R.2    Borbat, P.P.3    Freed, J.H.4    Crane, B.R.5
  • 131
    • 70349786387 scopus 로고    scopus 로고
    • Relative orientation of rigid nitroxides by PELDOR: Beyond distance measurements in nucleic acids
    • Schiemann O, Cekan P, Margraf D, Prisner TF, Sigurdsson ST (2009) Relative orientation of rigid nitroxides by PELDOR: beyond distance measurements in nucleic acids. Angew Chem Int Ed 48(18): 3292-3295
    • (2009) Angew Chem Int Ed , vol.48 , Issue.18 , pp. 3292-3295
    • Schiemann, O.1    Cekan, P.2    Margraf, D.3    Prisner, T.F.4    Sigurdsson, S.T.5
  • 132
    • 70350313495 scopus 로고    scopus 로고
    • Pulsed electron-electron double-resonance 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 double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA. J Am Chem Soc 131(42): 15246-15250
    • (2009) J Am Chem Soc , vol.131 , Issue.42 , pp. 15246-15250
    • Endeward, B.1    Butterwick, J.A.2    McKinnon, R.3    Prisner, T.F.4
  • 134
    • 80053650255 scopus 로고    scopus 로고
    • Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy
    • Fleissner MR, Bridges MD, Brooks EK, Cascio D, Kalai T, Hideg K, Hubbell WL (2011) Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy. Proc Natl Acad Sci USA 108(39): 16241-16246
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.39 , pp. 16241-16246
    • Fleissner, M.R.1    Bridges, M.D.2    Brooks, E.K.3    Cascio, D.4    Kalai, T.5    Hideg, K.6    Hubbell, W.L.7
  • 135
    • 29444455482 scopus 로고    scopus 로고
    • Double electron electron resonance as a method for characterization of micelles
    • Ruthstein S, Potapov A, Raitsimring AM, Goldfarb D (2005) Double electron electron resonance as a method for characterization of micelles. J Phys Chem B 109(48): 22843-22851
    • (2005) J Phys Chem B , vol.109 , Issue.48 , pp. 22843-22851
    • Ruthstein, S.1    Potapov, A.2    Raitsimring, A.M.3    Goldfarb, D.4
  • 136
    • 34249815195 scopus 로고    scopus 로고
    • Counting the monomers in nanometer-sized oligomers by pulsed electron - Electron double resonance
    • Bode BE, Margraf D, Plackmeyer J, Durner G, Prisner TF, Schiemann O (2007) Counting the monomers in nanometer-sized oligomers by pulsed electron - electron double resonance. J Am Chem Soc 129(21): 6736-6745
    • (2007) J Am Chem Soc , vol.129 , Issue.21 , pp. 6736-6745
    • Bode, B.E.1    Margraf, D.2    Plackmeyer, J.3    Durner, G.4    Prisner, T.F.5    Schiemann, O.6
  • 137
    • 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(31): 6580-6591
    • (2009) Phys Chem Chem Phys , vol.11 , Issue.31 , pp. 6580-6591
    • Jeschke, G.1    Sajid, M.2    Schulte, M.3    Godt, A.4
  • 138
    • 0035827984 scopus 로고    scopus 로고
    • Direct-product formalism for calculating magnetic resonance signals in many-body systems of interacting spins
    • Nevzorov AA, Freed JH (2001) Direct-product formalism for calculating magnetic resonance signals in many-body systems of interacting spins. J Chem Phys 115(6): 2401-2415
    • (2001) J Chem Phys , vol.115 , Issue.6 , pp. 2401-2415
    • Nevzorov, A.A.1    Freed, J.H.2
  • 139
    • 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(16): 1895-1910
    • (2007) Phys Chem Chem Phys , vol.9 , Issue.16 , pp. 1895-1910
    • Jeschke, G.1    Polyhach, Y.2
  • 140
    • 0002121327 scopus 로고
    • Stochastic problems in physics and astronomy
    • Chandrasekhar S (1943) Stochastic problems in physics and astronomy. Rev Mod Phys 15(1): 1-89
    • (1943) Rev Mod Phys , vol.15 , Issue.1 , pp. 1-89
    • Chandrasekhar, S.1
  • 141
    • 0034381602 scopus 로고    scopus 로고
    • Charge effect on relative distance distribution of Fremy's radical ions in frozen glassy solution studied by PELDOR
    • Milov AD, Tsvetkov YD (2000) Charge effect on relative distance distribution of Fremy's radical ions in frozen glassy solution studied by PELDOR. Appl Magn Reson 18(2): 217-226
    • (2000) Appl Magn Reson , vol.18 , Issue.2 , pp. 217-226
    • Milov, A.D.1    Tsvetkov, Y.D.2
  • 142
    • 84858332577 scopus 로고    scopus 로고
    • Effect of freezing conditions on distances and their distributions derived from double electron electron resonance (DEER): A study of doubly-spin-labeled T4 lysozyme
    • Georgieva ER, Roy AS, Grigoryants VM, Borbat PP, Earle KA, Scholes CP, Freed JH (2012) Effect of freezing conditions on distances and their distributions derived from double electron electron resonance (DEER): a study of doubly-spin-labeled T4 lysozyme. J Magn Reson 216: 69-77
    • (2012) J Magn Reson , vol.216 , pp. 69-77
    • Georgieva, E.R.1    Roy, A.S.2    Grigoryants, V.M.3    Borbat, P.P.4    Earle, K.A.5    Scholes, C.P.6    Freed, J.H.7
  • 143
    • 36149007455 scopus 로고
    • Spectral diffusion decay in spin resonance experiments
    • Klauder JR, Anderson PW (1962) Spectral diffusion decay in spin resonance experiments. Phys Rev 125: 912-932
    • (1962) Phys Rev , vol.125 , pp. 912-932
    • Klauder, J.R.1    Anderson, P.W.2
  • 144
    • 78651237011 scopus 로고    scopus 로고
    • Channel and nonchannel forms of spin-labeled gramicidin in membranes and their equilibria
    • Dzikovski BG, Borbat PP, Freed JH (2011) Channel and nonchannel forms of spin-labeled gramicidin in membranes and their equilibria. J Phys Chem B 115(1): 176-185
    • (2011) J Phys Chem B , vol.115 , Issue.1 , pp. 176-185
    • Dzikovski, B.G.1    Borbat, P.P.2    Freed, J.H.3
  • 146
    • 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(6): L18-L20
    • (2010) Biophys J , vol.98 , Issue.6 , pp. L18-L20
    • Zou, P.1    McHaourab, H.S.2
  • 147
    • 0031203438 scopus 로고    scopus 로고
    • Multifrequency two-dimensional Fourier transform ESR: An X/Ku-band spectrometer
    • Borbat PP, Crepeau RH, Freed JH (1997) Multifrequency two-dimensional Fourier transform ESR: an X/Ku-band spectrometer. J Magn Reson 127(2): 155-167
    • (1997) J Magn Reson , vol.127 , Issue.2 , pp. 155-167
    • Borbat, P.P.1    Crepeau, R.H.2    Freed, J.H.3
  • 148
    • 0037532022 scopus 로고
    • Two-dimensional Fourier transform ESR spectroscopy
    • Gorcester J, Freed JH (1986) Two-dimensional Fourier transform ESR spectroscopy. J Chem Phys 85(9): 5375-5377
    • (1986) J Chem Phys , vol.85 , Issue.9 , pp. 5375-5377
    • Gorcester, J.1    Freed, J.H.2
  • 149
    • 0002214132 scopus 로고
    • Elimination of unwanted echoes and reduction of dead time in 3-pulse electron spin-echo spectroscopy
    • Fauth JM, Schweiger A, Braunschweiler L, Forrer J, Ernst RR (1986) Elimination of unwanted echoes and reduction of dead time in 3-pulse electron spin-echo spectroscopy. J Magn Reson 66(1): 74-85
    • (1986) J Magn Reson , vol.66 , Issue.1 , pp. 74-85
    • Fauth, J.M.1    Schweiger, A.2    Braunschweiler, L.3    Forrer, J.4    Ernst, R.R.5
  • 150
    • 0000068844 scopus 로고
    • Critical factors in design of sensitive high-resolution nuclear magnetic-resonance spectrometers
    • Hoult DI, Richards RE (1975) Critical factors in design of sensitive high-resolution nuclear magnetic-resonance spectrometers. Proc R Soc Lond Ser A-Math Phys Eng Sci 344 (1638): 311-340
    • (1975) Proc R Soc Lond Ser A-Math Phys Eng Sci , vol.344 , Issue.1638 , pp. 311-340
    • Hoult, D.I.1    Richards, R.E.2
  • 151
    • 84862542770 scopus 로고    scopus 로고
    • Pulsed ESR dipolar spectroscopy for distance measurements in immobilized spin labeled proteins in liquid solution
    • Yang ZY, Liu YP, Borbat P, Zweier JL, Freed JH, Hubbell WL (2012) Pulsed ESR dipolar spectroscopy for distance measurements in immobilized spin labeled proteins in liquid solution. J Am Chem Soc 134(24): 9950-9952
    • (2012) J Am Chem Soc , vol.134 , Issue.24 , pp. 9950-9952
    • Yang, Z.Y.1    Liu, Y.P.2    Borbat, P.3    Zweier, J.L.4    Freed, J.H.5    Hubbell, W.L.6
  • 153
    • 0347648115 scopus 로고
    • Symmetrical composite pulse sequences for NMR population-inversion 1. Compensation of radiofrequency field inhomogeneity
    • Levitt MH (1982) Symmetrical composite pulse sequences for NMR population-inversion 1. Compensation of radiofrequency field inhomogeneity. J Magn Reson 48(2): 234-264
    • (1982) J Magn Reson , vol.48 , Issue.2 , pp. 234-264
    • Levitt, M.H.1
  • 155
    • 49249151634 scopus 로고
    • NMR population-inversion using a composite pulse
    • Levitt MH, Freeman R (1979) NMR population-inversion using a composite pulse. J Magn Reson 33(2): 473-476
    • (1979) J Magn Reson , vol.33 , Issue.2 , pp. 473-476
    • Levitt, M.H.1    Freeman, R.2
  • 156
    • 0000741505 scopus 로고
    • Symmetrical phase-alternating composite pulses
    • Shaka AJ, Pines A (1987) Symmetrical phase-alternating composite pulses. J Magn Reson 71 (3): 495-503
    • (1987) J Magn Reson , vol.71 , Issue.3 , pp. 495-503
    • Shaka, A.J.1    Pines, A.2
  • 157
    • 0041923331 scopus 로고
    • Amplitude-modulated composite pulses
    • Zax DB, Goelman G, Vega S (1988) Amplitude-modulated composite pulses. J Magn Reson 80(2): 375-382
    • (1988) J Magn Reson , vol.80 , Issue.2 , pp. 375-382
    • Zax, D.B.1    Goelman, G.2    Vega, S.3
  • 158
    • 0008445577 scopus 로고
    • Broad-band excitation pulses of arbitrary flip angle
    • Zax DB, Vega S (1989) Broad-band excitation pulses of arbitrary flip angle. Phys Rev Lett 62(16): 1840-1843
    • (1989) Phys Rev Lett , vol.62 , Issue.16 , pp. 1840-1843
    • Zax, D.B.1    Vega, S.2
  • 159
    • 0001549644 scopus 로고
    • Broad-band and adiabatic inversion of a 2-level system by phase-modulated pulses
    • Baum J, Tycko R, Pines A (1985) Broad-band and adiabatic inversion of a 2-level system by phase-modulated pulses. Phys Rev A 32(6): 3435-3447
    • (1985) Phys Rev A , vol.32 , Issue.6 , pp. 3435-3447
    • Baum, J.1    Tycko, R.2    Pines, A.3
  • 160
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H, Freeman R (1991) Band-selective radiofrequency pulses. J Magn Reson 93(1): 93-141
    • (1991) J Magn Reson , vol.93 , Issue.1 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 161
    • 0000494530 scopus 로고
    • Computer-optimized narrow-band pulses for multislice imaging
    • Murdoch JB, Lent AH, Kritzer MR (1987) Computer-optimized narrow-band pulses for multislice imaging. J Magn Reson 74(2): 226-263
    • (1987) J Magn Reson , vol.74 , Issue.2 , pp. 226-263
    • Murdoch, J.B.1    Lent, A.H.2    Kritzer, M.R.3
  • 162
    • 4243461379 scopus 로고
    • Selective spin inversion in nuclear magneticresonance and coherent optics through an exact solution of the Bloch-Riccati equation
    • Silver MS, Joseph RI, Hoult DI (1985) Selective spin inversion in nuclear magneticresonance and coherent optics through an exact solution of the Bloch-Riccati equation. Phys Rev A 31(4): 2753-2755
    • (1985) Phys Rev A , vol.31 , Issue.4 , pp. 2753-2755
    • Silver, M.S.1    Joseph, R.I.2    Hoult, D.I.3
  • 163
    • 0000789516 scopus 로고
    • Effects of arbitrary laser or NMR pulse shapes on population-inversion and coherence
    • Warren WS (1984) Effects of arbitrary laser or NMR pulse shapes on population-inversion and coherence. J Chem Phys 81(12): 5437-5448
    • (1984) J Chem Phys , vol.81 , Issue.12 , pp. 5437-5448
    • Warren, W.S.1
  • 164
    • 0030575752 scopus 로고    scopus 로고
    • A theoretical approach to the analysis of arbitrary pulses in magnetic resonance
    • Salikhov KM, Schneider DJ, Saxena S, Freed JH (1996) A theoretical approach to the analysis of arbitrary pulses in magnetic resonance. Chem Phys Lett 262(1, 2): 17-26
    • (1996) Chem Phys Lett , vol.262 , Issue.1-2 , pp. 17-26
    • Salikhov, K.M.1    Schneider, D.J.2    Saxena, S.3    Freed, J.H.4
  • 165
    • 0001755357 scopus 로고
    • Decomposition formulas of exponential operators and lie exponentials with some applications to quantum mechanics and statistical physics
    • Suzuki M (1985) Decomposition formulas of exponential operators and lie exponentials with some applications to quantum mechanics and statistical physics. J Math Phys 26: 601-612
    • (1985) J Math Phys , vol.26 , pp. 601-612
    • Suzuki, M.1
  • 166
    • 84968520470 scopus 로고
    • On the product of semi-groups of operators
    • Trotter HF (1959) On the product of semi-groups of operators. Proc Am Math Soc 10(4): 545-551
    • (1959) Proc Am Math Soc , vol.10 , Issue.4 , pp. 545-551
    • Trotter, H.F.1
  • 169
    • 0001258096 scopus 로고
    • Electron echo methods in spin resonance spectrometry
    • Mims WB (1965) Electron echo methods in spin resonance spectrometry. Rev Sci Instrum 36(10): 1472-1479
    • (1965) Rev Sci Instrum , vol.36 , Issue.10 , pp. 1472-1479
    • Mims, W.B.1
  • 170
    • 33845992936 scopus 로고    scopus 로고
    • Distance determination in human ubiquitin by pulsed double electron-electron resonance and double quantum coherence ESR methods
    • 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(1): 78-84
    • (2007) J Magn Reson , vol.184 , Issue.1 , pp. 78-84
    • Hara, H.1    Tenno, T.2    Shirakawa, M.3
  • 171
    • 84872200039 scopus 로고    scopus 로고
    • Improved sensitivity for long-distance measurements in biomolecules: Five-pulse double electron-electron resonance
    • Borbat PP, Georgieva ER, Freed JH (2012) Improved sensitivity for long-distance measurements in biomolecules: five-pulse double electron-electron resonance. J Phys Chem Lett. doi: 10. 1021/jz301788n
    • (2012) J Phys Chem Lett
    • Borbat, P.P.1    Georgieva, E.R.2    Freed, J.H.3
  • 172
    • 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(25): 5782-5784
    • (2009) Biochemistry , vol.48 , Issue.25 , pp. 5782-5784
    • Ghimire, H.1    McCarrick, R.M.2    Budil, D.E.3    Lorigan, G.A.4
  • 173
    • 78651265890 scopus 로고    scopus 로고
    • Simultaneous acquisition of pulse EPR orientation selective spectra
    • Kaminker I, Florent M, Epel B, Goldfarb D (2011) Simultaneous acquisition of pulse EPR orientation selective spectra. J Magn Reson 208(1): 95-102
    • (2011) J Magn Reson , vol.208 , Issue.1 , pp. 95-102
    • Kaminker, I.1    Florent, M.2    Epel, B.3    Goldfarb, D.4
  • 176
    • 79960059173 scopus 로고    scopus 로고
    • Gadolinium tagging for high-precision measurements of 6 nm distances in protein assemblies by EPR
    • Yagi H, Banerjee D, Graham B, Huber T, Goldfarb D, Otting G (2011) Gadolinium tagging for high-precision measurements of 6 nm distances in protein assemblies by EPR. J Am Chem Soc 133(27): 10418-10421
    • (2011) J Am Chem Soc , vol.133 , Issue.27 , pp. 10418-10421
    • Yagi, H.1    Banerjee, D.2    Graham, B.3    Huber, T.4    Goldfarb, D.5    Otting, G.6
  • 177
    • 77954273484 scopus 로고    scopus 로고
    • Distance measurements in model bis-Gd(III) complexes with flexible "bridge". Emulation of biological molecules having flexible structure with Gd(III) labels attached
    • Potapov A, Song Y, Meade TJ, Goldfarb D, Astashkin AV, Raitsimring A (2010) Distance measurements in model bis-Gd(III) complexes with flexible "bridge". Emulation of biological molecules having flexible structure with Gd(III) labels attached. J Magn Reson 205(1): 38-49
    • (2010) J Magn Reson , vol.205 , Issue.1 , pp. 38-49
    • Potapov, A.1    Song, Y.2    Meade, T.J.3    Goldfarb, D.4    Astashkin, A.V.5    Raitsimring, A.6
  • 178
    • 79955059401 scopus 로고    scopus 로고
    • Pulsed dipolar spectroscopy distance measurements in biomacromolecules labeled with Gd(III) markers
    • Song Y, Meade TJ, Astashkin AV, Klein EL, Enemark JH, Raitsimring A (2011) Pulsed dipolar spectroscopy distance measurements in biomacromolecules labeled with Gd(III) markers. J Magn Reson 210(1): 59-68
    • (2011) J Magn Reson , vol.210 , Issue.1 , pp. 59-68
    • Song, Y.1    Meade, T.J.2    Astashkin, A.V.3    Klein, E.L.4    Enemark, J.H.5    Raitsimring, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.