메뉴 건너뛰기




Volumn 218, Issue , 2012, Pages 93-104

The global analysis of DEER data

Author keywords

DEER; Global analysis; PELDOR

Indexed keywords

BIOCHEMISTRY; RESONANCE;

EID: 84861028919     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2012.03.006     Document Type: Article
Times cited : (75)

References (41)
  • 1
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (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
  • 2
    • 79952130813 scopus 로고    scopus 로고
    • Pulsed electron-electron double resonance: Beyond nanometre distance measurements on biomacromolecules
    • G.W. Reginsson, and O. Schiemann Pulsed electron-electron double resonance: beyond nanometre distance measurements on biomacromolecules Biochem. J. 434 2011 353 363
    • (2011) Biochem. J. , vol.434 , pp. 353-363
    • Reginsson, G.W.1    Schiemann, O.2
  • 3
    • 79551492492 scopus 로고    scopus 로고
    • Studying bimolecular complexes with pulsed electron-electron double resonance spectroscopy
    • G.W. Reginsson, and O. Schiemann Studying bimolecular complexes with pulsed electron-electron double resonance spectroscopy Biochem. Soc. Trans. 39 2011 128 139
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 128-139
    • Reginsson, G.W.1    Schiemann, O.2
  • 5
    • 0001201352 scopus 로고    scopus 로고
    • Dipolar spectroscopy and spin alignment in electron paramagnetic resonance
    • G. Jeschke, M. Pannier, A. Godt, and H.W. Spiess Dipolar spectroscopy and spin alignment in electron paramagnetic resonance Chem. Phys. Lett. 331 2000 243 252
    • (2000) Chem. Phys. Lett. , vol.331 , pp. 243-252
    • Jeschke, G.1    Pannier, M.2    Godt, A.3    Spiess, H.W.4
  • 6
    • 0037093869 scopus 로고    scopus 로고
    • Protein structure determination using long-distance constraints from double-quantum coherence ESR: Study of T4 lysozyme
    • P.P. Borbat, H.S. McHaourab, and J.H. Freed Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme J. Am. Chem. Soc. 124 2002 5304 5314
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5304-5314
    • Borbat, P.P.1    McHaourab, H.S.2    Freed, J.H.3
  • 7
    • 3042741373 scopus 로고    scopus 로고
    • Visualization of distance distribution from pulsed double electron-electron resonance data
    • M.K. Bowman, A.G. Maryasov, N. Kim, and V.J. DeRose Visualization of distance distribution from pulsed double electron-electron resonance data Appl. Magn. Reson. 26 2004 23 39
    • (2004) Appl. Magn. Reson. , vol.26 , pp. 23-39
    • Bowman, M.K.1    Maryasov, A.G.2    Kim, N.3    Derose, V.J.4
  • 8
    • 11344285129 scopus 로고    scopus 로고
    • The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    • Y.W. Chiang, P.P. Borbat, and J.H. Freed The determination of pair distance distributions by pulsed ESR using Tikhonov regularization J. Magn. Reson. 172 2005 279 295
    • (2005) J. Magn. Reson. , vol.172 , pp. 279-295
    • Chiang, Y.W.1    Borbat, P.P.2    Freed, J.H.3
  • 10
    • 0036290220 scopus 로고    scopus 로고
    • Direct conversion of EPR dipolar time evolution data to distance distributions
    • G. Jeschke, A. Koch, U. Jonas, and A. Godt Direct conversion of EPR dipolar time evolution data to distance distributions J. Magn. Reson. 155 2002 72 82
    • (2002) J. Magn. Reson. , vol.155 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 12
    • 58849149026 scopus 로고    scopus 로고
    • Backbone structure of transmembrane domain IX of the Na(+)/proline transporter PutP of Escherichia coli
    • D. Hilger, Y. Polyhach, H. Jung, and G. Jeschke Backbone structure of transmembrane domain IX of the Na(+)/proline transporter PutP of Escherichia coli Biophys. J. 96 2009 217 225
    • (2009) Biophys. J. , vol.96 , pp. 217-225
    • Hilger, D.1    Polyhach, Y.2    Jung, H.3    Jeschke, G.4
  • 14
    • 36549000870 scopus 로고    scopus 로고
    • High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed election paramagnetic resonance distance measurements
    • D. Hilger, Y. Polyhach, E. Padan, H. Jung, and G. Jeschke High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed election paramagnetic resonance distance measurements Biophys. J. 93 2007 3675 3683
    • (2007) Biophys. J. , vol.93 , pp. 3675-3683
    • Hilger, D.1    Polyhach, Y.2    Padan, E.3    Jung, H.4    Jeschke, G.5
  • 16
    • 77949387765 scopus 로고    scopus 로고
    • The structure of p85ni in class IA phosphoinositide 3-kinase exhibits interdomain disorder
    • K.I. Sen, H. Wu, J.M. Backer, and G.J. Gerfen The structure of p85ni in class IA phosphoinositide 3-kinase exhibits interdomain disorder Biochemistry 49 2010 2159 2166
    • (2010) Biochemistry , vol.49 , pp. 2159-2166
    • Sen, K.I.1    Wu, H.2    Backer, J.M.3    Gerfen, G.J.4
  • 17
    • 70349785109 scopus 로고    scopus 로고
    • Conformational cycle of the ABC transporter MsbA in liposomes: Detailed analysis using double electron-electron resonance spectroscopy
    • P. Zou, M. Bortolus, and H.S. Mchaourab Conformational cycle of the ABC transporter MsbA in liposomes: detailed analysis using double electron-electron resonance spectroscopy J. Mol. Biol. 393 2009 586 597
    • (2009) J. Mol. Biol. , vol.393 , pp. 586-597
    • Zou, P.1    Bortolus, M.2    McHaourab, H.S.3
  • 18
    • 44949236117 scopus 로고    scopus 로고
    • High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    • C. Altenbach, A.K. Kusnetzow, O.P. Ernst, K.P. Hofmann, and W.L. Hubbell High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation Proc. Natl. Acad. Sci. USA 105 2008 7439 7444
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 20
    • 70349153078 scopus 로고    scopus 로고
    • Monitoring inhibitor-induced conformational population shifts in HIV-1 protease by pulsed EPR spectroscopy
    • M.E. Blackburn, A.M. Veloro, and G.E. Fanucci Monitoring inhibitor-induced conformational population shifts in HIV-1 protease by pulsed EPR spectroscopy Biochemistry 48 2009 8765 8767
    • (2009) Biochemistry , vol.48 , pp. 8765-8767
    • Blackburn, M.E.1    Veloro, A.M.2    Fanucci, G.E.3
  • 22
    • 67650546951 scopus 로고    scopus 로고
    • Transmembrane signaling in the maltose ABC transporter MalFGK2-E: Periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer
    • M. Grote, Y. Polyhach, G. Jeschke, H.J. Steinhoff, E. Schneider, and E. Bordignon Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer J. Biol. Chem. 284 2009 17521 17526
    • (2009) J. Biol. Chem. , vol.284 , pp. 17521-17526
    • Grote, M.1    Polyhach, Y.2    Jeschke, G.3    Steinhoff, H.J.4    Schneider, E.5    Bordignon, E.6
  • 23
    • 0030950516 scopus 로고    scopus 로고
    • Molecular distances from dipolar coupled spin-labels: The global analysis of multifrequency continuous wave electron paramagnetic resonance data
    • E.J. Hustedt, A.I. Smirnov, C.F. Laub, C.E. Cobb, and A.H. Beth Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data Biophys. J. 72 1997 1861 1877
    • (1997) Biophys. J. , vol.72 , pp. 1861-1877
    • Hustedt, E.J.1    Smirnov, A.I.2    Laub, C.F.3    Cobb, C.E.4    Beth, A.H.5
  • 24
    • 33748630529 scopus 로고    scopus 로고
    • High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase
    • V.P. Denysenkov, T.F. Prisner, J. Stubbe, and M. Bennati 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 2006 13386 13390
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13386-13390
    • Denysenkov, V.P.1    Prisner, T.F.2    Stubbe, J.3    Bennati, M.4
  • 25
    • 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
    • A. Savitsky, A.A. Dubinskii, M. Flores, W. Lubitz, and K. Moebius 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 2007 6245 6262
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6245-6262
    • Savitsky, A.1    Dubinskii, A.A.2    Flores, M.3    Lubitz, W.4    Moebius, K.5
  • 26
    • 77952187929 scopus 로고    scopus 로고
    • An approach towards the measurement of nanometer range distances based on Cu(2+) ions and ESR
    • Z. Yang, D. Kise, and S. Saxena An approach towards the measurement of nanometer range distances based on Cu(2+) ions and ESR J. Phys. Chem. B 114 2010 6165 6174
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6165-6174
    • Yang, Z.1    Kise, D.2    Saxena, S.3
  • 27
    • 33646127590 scopus 로고    scopus 로고
    • Dipolar coupling between nitroxide spin labels: The development and application of a tether-in-a-cone model
    • E.J. Hustedt, R.A. Stein, L. Sethaphong, S. Brandon, Z. Zhou, and S.C. DeSensi Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model Biophys. J. 90 2006 340 356
    • (2006) Biophys. J. , vol.90 , pp. 340-356
    • Hustedt, E.J.1    Stein, R.A.2    Sethaphong, L.3    Brandon, S.4    Zhou, Z.5    Desensi, S.C.6
  • 28
    • 35148883146 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: Band 3 Tuscaloosa
    • Z. Zhou, S.C. DeSensi, R.A. Stein, S. Brandon, L. Song, C.E. Cobb, E.J. Hustedt, and A.H. Beth Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: band 3 Tuscaloosa Biochemistry 46 2007 10248 10257
    • (2007) Biochemistry , vol.46 , pp. 10248-10257
    • Zhou, Z.1    Desensi, S.C.2    Stein, R.A.3    Brandon, S.4    Song, L.5    Cobb, C.E.6    Hustedt, E.J.7    Beth, A.H.8
  • 29
    • 3042819802 scopus 로고    scopus 로고
    • Data analysis procedures for pulse ELDOR measurements of broad distance distributions
    • G. Jeschke, G. Panek, A. Godt, A. Bender, and H. Paulsen Data analysis procedures for pulse ELDOR measurements of broad distance distributions Appl. Magn. Reson. 26 2004 223 244
    • (2004) Appl. Magn. Reson. , vol.26 , pp. 223-244
    • Jeschke, G.1    Panek, G.2    Godt, A.3    Bender, A.4    Paulsen, H.5
  • 30
    • 0032357748 scopus 로고    scopus 로고
    • Pulsed electron double resonance (PELDOR) and its applications in free-radicals research
    • A.D. Milov, A.G. Maryasov, and Y.D. Tsvetkov Pulsed electron double resonance (PELDOR) and its applications in free-radicals research Appl. Magn. Reson. 15 1998 107 143
    • (1998) Appl. Magn. Reson. , vol.15 , pp. 107-143
    • Milov, A.D.1    Maryasov, A.G.2    Tsvetkov, Y.D.3
  • 31
    • 0026719686 scopus 로고
    • Global analysis of biochemical and biophysical data
    • J.M. Beechem Global analysis of biochemical and biophysical data Methods Enzymol. 210 1992 37 54
    • (1992) Methods Enzymol. , vol.210 , pp. 37-54
    • Beechem, J.M.1
  • 32
    • 0020840992 scopus 로고
    • Evaluation and propagation of confidence intervals in nonlinear, asymmetrical variance spaces. Analysis of ligand-binding data
    • M.L. Johnson Evaluation and propagation of confidence intervals in nonlinear, asymmetrical variance spaces. Analysis of ligand-binding data Biophys. J. 44 1983 101 106
    • (1983) Biophys. J. , vol.44 , pp. 101-106
    • Johnson, M.L.1
  • 33
    • 0034329189 scopus 로고    scopus 로고
    • Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • D.C. Zhang, A. Kiyatkin, J.T. Bolin, and P.S. Low Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3 Blood 96 2000 2925 2933
    • (2000) Blood , vol.96 , pp. 2925-2933
    • Zhang, D.C.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4
  • 34
    • 0019877653 scopus 로고
    • Partial structural characterization of the cytoplasmic domain of the erythrocyte-membrane protein, band-3
    • K.C. Appell, and P.S. Low Partial structural characterization of the cytoplasmic domain of the erythrocyte-membrane protein, band-3 J. Biol. Chem. 256 1981 1104 1111
    • (1981) J. Biol. Chem. , vol.256 , pp. 1104-1111
    • Appell, K.C.1    Low, P.S.2
  • 35
    • 0026696751 scopus 로고
    • Band 3 Tuscaloosa: Pro327 - Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2
    • P. Jarolim, J. Palek, H.L. Rubin, J.T. Prchal, C. Korsgren, and C.M. Cohen Band 3 Tuscaloosa: Pro327 - Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2 Blood 80 1992 523 529
    • (1992) Blood , vol.80 , pp. 523-529
    • Jarolim, P.1    Palek, J.2    Rubin, H.L.3    Prchal, J.T.4    Korsgren, C.5    Cohen, C.M.6
  • 36
    • 70350313495 scopus 로고    scopus 로고
    • Pulsed electron-electron double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA
    • B. Endeward, J.A. Butterwick, R. MacKinnon, and T.F. Prisner Pulsed electron-electron double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA J. Am. Chem. Soc. 131 2009 15246 15250
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15246-15250
    • Endeward, B.1    Butterwick, J.A.2    MacKinnon, R.3    Prisner, T.F.4
  • 37
    • 0001579637 scopus 로고
    • Double electron-electron resonance spin-echo modulation: Spectroscopic measurement of electron spin pair separations in orientationally disordered solids
    • R.G. Larsen, and D.J. Singel Double electron-electron resonance spin-echo modulation: spectroscopic measurement of electron spin pair separations in orientationally disordered solids J. Chem. Phys. 98 1993 5134 5146
    • (1993) J. Chem. Phys. , vol.98 , pp. 5134-5146
    • Larsen, R.G.1    Singel, D.J.2
  • 38
    • 41149131813 scopus 로고    scopus 로고
    • Conformational flexibility of nitroxide biradicals determined by X-band PELDOR experiments
    • D. Margraf, B.E. Bode, A. Marko, O. Schiemann, and T.F. Prisner Conformational flexibility of nitroxide biradicals determined by X-band PELDOR experiments Mol. Phys. 105 2007 2153 2160
    • (2007) Mol. Phys. , vol.105 , pp. 2153-2160
    • Margraf, D.1    Bode, B.E.2    Marko, A.3    Schiemann, O.4    Prisner, T.F.5
  • 40
    • 60349094124 scopus 로고    scopus 로고
    • Molecular orientation studies by pulsed electron-electron double resonance experiments
    • A. Marko, D. Margraf, H. Yu, Y. Mu, G. Stock, and T. Prisner Molecular orientation studies by pulsed electron-electron double resonance experiments J. Chem. Phys. 130 2009
    • (2009) J. Chem. Phys. , vol.130
    • Marko, A.1    Margraf, D.2    Yu, H.3    Mu, Y.4    Stock, G.5    Prisner, T.6
  • 41
    • 33947620119 scopus 로고    scopus 로고
    • Spin pair geometry revealed by high-field DEER in the presence of conformational distributions
    • Y. Polyhach, A. Godt, C. Bauer, and G. Jeschke Spin pair geometry revealed by high-field DEER in the presence of conformational distributions J. Magn. Reson. 185 2007 118 129
    • (2007) J. Magn. Reson. , vol.185 , pp. 118-129
    • Polyhach, Y.1    Godt, A.2    Bauer, C.3    Jeschke, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.