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Volumn 19, Issue 11, 2011, Pages 1549-1561

Toward the fourth dimension of membrane protein structure: Insight into dynamics from spin-labeling EPR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; LACTOSE PERMEASE; LEUCINE; MEMBRANE PROTEIN; RHODOPSIN; SODIUM;

EID: 80855144806     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.10.009     Document Type: Review
Times cited : (207)

References (78)
  • 1
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • DOI 10.1126/science.1088196
    • J. Abramson, I. Smirnova, V. Kasho, G. Verner, H.R. Kaback, and S. Iwata Structure and mechanism of the lactose permease of Escherichia coli Science 301 2003 610 615 (Pubitemid 36927939)
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 2
    • 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
    • N. Alexander, M. Bortolus, A. Al-Mestarihi, H. Mchaourab, and J. Meiler De novo high-resolution protein structure determination from sparse spin-labeling EPR data Structure 16 2008 181 195 (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
  • 3
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • C. Altenbach, T. Marti, H.G. Khorana, and W.L. Hubbell Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants Science 248 1990 1088 1092
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 5
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • T.H. Bayburt, and S.G. Sligar Membrane protein assembly into Nanodiscs FEBS Lett. 584 2010 1721 1727
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 6
    • 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
    • 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 (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
  • 8
    • 33646379349 scopus 로고    scopus 로고
    • Distance between a native cofactor and a spin label in the reaction centre of Rhodobacter sphaeroides by a two-frequency pulsed electron paramagnetic resonance method and molecular dynamics simulations
    • DOI 10.1016/j.jmr.2006.02.008, PII S1090780706000292
    • I.V. Borovykh, S. Ceola, P. Gajula, P. Gast, H.J. Steinhoff, and M. Huber Distance between a native cofactor and a spin label in the reaction centre of Rhodobacter sphaeroides by a two-frequency pulsed electron paramagnetic resonance method and molecular dynamics simulations J. Magn. Reson. 180 2006 178 185 (Pubitemid 43674434)
    • (2006) Journal of Magnetic Resonance , vol.180 , Issue.2 , pp. 178-185
    • Borovykh, I.V.1    Ceola, S.2    Gajula, P.3    Gast, P.4    Steinhoff, H.-J.5    Huber, M.6
  • 9
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • DOI 10.1016/S0959-440X(00)00223-2
    • J.U. Bowie Stabilizing membrane proteins Curr. Opin. Struct. Biol. 11 2001 397 402 (Pubitemid 32728488)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.4 , pp. 397-402
    • Bowie, J.U.1
  • 10
    • 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
    • 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 (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
  • 13
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure
    • DOI 10.1021/bi002645h
    • L. Columbus, T. Kálai, J. Jekö, K. Hideg, and W.L. Hubbell Molecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure Biochemistry 40 2001 3828 3846 (Pubitemid 32280420)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 3828-3846
    • Columbus, L.1    Kalai, T.2    Jeko, J.3    Hideg, K.4    Hubbell, W.L.5
  • 15
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA role of cytoplasmic domains in ion permeation and activation gating
    • DOI 10.1085/jgp.117.2.165
    • D.M. Cortes, L.G. Cuello, and E. Perozo Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating J. Gen. Physiol. 117 2001 165 180 (Pubitemid 32423754)
    • (2001) Journal of General Physiology , vol.117 , Issue.2 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 16
    • 79551597049 scopus 로고    scopus 로고
    • Influence of solubilizing environments on membrane protein structures
    • T.A. Cross, M. Sharma, M. Yi, and H.X. Zhou Influence of solubilizing environments on membrane protein structures Trends Biochem. Sci. 36 2011 117 125
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 117-125
    • Cross, T.A.1    Sharma, M.2    Yi, M.3    Zhou, H.X.4
  • 18
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with Rosetta
    • R. Das, and D. Baker Macromolecular modeling with Rosetta Annu. Rev. Biochem. 77 2008 363 382
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 19
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis of energy transduction in the transport cycle of MsbA
    • DOI 10.1126/science.1106592
    • J. Dong, G. Yang, and H.S. McHaourab Structural basis of energy transduction in the transport cycle of MsbA Science 308 2005 1023 1028 (Pubitemid 40664413)
    • (2005) Science , vol.308 , Issue.5724 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    Mchaourab, H.S.3
  • 21
    • 36148983388 scopus 로고    scopus 로고
    • Mapping electron paramagnetic resonance spin label conformations by the simulated scaling method
    • DOI 10.1021/ja071404v
    • M.I. Fajer, H. Li, W. Yang, and P.G. Fajer Mapping electron paramagnetic resonance spin label conformations by the simulated scaling method J. Am. Chem. Soc. 129 2007 13840 13846 (Pubitemid 350106073)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.45 , pp. 13840-13846
    • Fajer, M.I.1    Li, H.2    Yang, W.3    Fajer, P.G.4
  • 22
    • 0037452539 scopus 로고    scopus 로고
    • Substrate-induced conformational changes of the perplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling
    • DOI 10.1021/bi027120z
    • G.E. Fanucci, K.A. Coggshall, N. Cadieux, M. Kim, R.J. Kadner, and D.S. Cafiso Substrate-induced conformational changes of the periplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling Biochemistry 42 2003 1391 1400 (Pubitemid 36205945)
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1391-1400
    • Fanucci, G.E.1    Coggshall, K.A.2    Cadieux, N.3    Kim, M.4    Kadner, R.J.5    Cafiso, D.S.6
  • 23
    • 76749110236 scopus 로고    scopus 로고
    • Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins
    • R.H. Flores Jiménez, M.A. Do Cao, M. Kim, and D.S. Cafiso Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins Protein Sci. 19 2010 269 278
    • (2010) Protein Sci. , vol.19 , pp. 269-278
    • Flores Jiménez, R.H.1    Do Cao, M.A.2    Kim, M.3    Cafiso, D.S.4
  • 24
    • 77956590446 scopus 로고    scopus 로고
    • Conformational exchange in a membrane transport protein is altered in protein crystals
    • D.M. Freed, P.S. Horanyi, M.C. Wiener, and D.S. Cafiso Conformational exchange in a membrane transport protein is altered in protein crystals Biophys. J. 99 2010 1604 1610
    • (2010) Biophys. J. , vol.99 , pp. 1604-1610
    • Freed, D.M.1    Horanyi, P.S.2    Wiener, M.C.3    Cafiso, D.S.4
  • 25
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • E.R. Georgieva, T.F. Ramlall, P.P. Borbat, J.H. Freed, and D. Eliezer Membrane-bound alpha-synuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles J. Am. Chem. Soc. 130 2008 12856 12857
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 26
    • 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)
    • H. Ghimire, R.M. McCarrick, D.E. Budil, and G.A. Lorigan 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 2009 5782 5784
    • (2009) Biochemistry , vol.48 , pp. 5782-5784
    • Ghimire, H.1    McCarrick, R.M.2    Budil, D.E.3    Lorigan, G.A.4
  • 27
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • DOI 10.1126/science.1113666
    • E. Gouaux, and R. Mackinnon Principles of selective ion transport in channels and pumps Science 310 2005 1461 1465 (Pubitemid 41746336)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2
  • 29
    • 34548832250 scopus 로고    scopus 로고
    • Structural principles of intramembrane proteases
    • DOI 10.1016/j.sbi.2007.06.010, PII S0959440X07000991
    • Y. Ha Structural principles of intramembrane proteases Curr. Opin. Struct. Biol. 17 2007 405 411 (Pubitemid 47451765)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.4 , pp. 405-411
    • Ha, Y.1
  • 30
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism - An overview
    • DOI 10.1016/S0923-2508(01)01193-7
    • C.F. Higgins ABC transporters: physiology, structure and mechanism - an overview Res. Microbiol. 152 2001 205 210 (Pubitemid 32436480)
    • (2001) Research in Microbiology , vol.152 , Issue.3-4 , pp. 205-210
    • Higgins, C.F.1
  • 31
    • 36549000870 scopus 로고    scopus 로고
    • + antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurements
    • DOI 10.1529/biophysj.107.109769
    • D. Hilger, Y. Polyhach, E. Padan, H. Jung, and G. Jeschke High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurements Biophys. J. 93 2007 3675 3683 (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
  • 32
    • 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
  • 33
    • 79851512251 scopus 로고    scopus 로고
    • RosettaEPR: An integrated tool for protein structure determination from sparse EPR data
    • S.J. Hirst, N. Alexander, H.S. McHaourab, and J. Meiler RosettaEPR: an integrated tool for protein structure determination from sparse EPR data J. Struct. Biol. 173 2011 506 514
    • (2011) J. Struct. Biol. , vol.173 , pp. 506-514
    • Hirst, S.J.1    Alexander, N.2    McHaourab, H.S.3    Meiler, J.4
  • 34
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • W.L. Hubbell, D.S. Cafiso, and C. Altenbach Identifying conformational changes with site-directed spin labeling Nat. Struct. Biol. 7 2000 735 739
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 35
    • 0030586056 scopus 로고    scopus 로고
    • Watching proteins move using site-directed spin labeling
    • DOI 10.1016/S0969-2126(96)00085-8
    • W.L. Hubbell, H.S. Mchaourab, C. Altenbach, and M.A. Lietzow Watching proteins move using site-directed spin labeling Structure 4 1996 779 783 (Pubitemid 26312362)
    • (1996) Structure , vol.4 , Issue.7 , pp. 779-783
    • Hubbell, W.L.1    Mchaourab, H.S.2    Altenbach, C.3    Lietzow, M.A.4
  • 36
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • DOI 10.1016/S0065-3233(03)63010-X
    • W.L. Hubbell, C. Altenbach, C.M. Hubbell, and H.G. Khorana Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking Adv. Protein Chem. 63 2003 243 290 (Pubitemid 36268430)
    • (2003) Advances in Protein Chemistry , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 37
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement
    • C.C. Jao, B.G. Hegde, J. Chen, I.S. Haworth, and R. Langen Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement Proc. Natl. Acad. Sci. USA 105 2008 19666 19671
    • (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
  • 38
    • 34147218123 scopus 로고    scopus 로고
    • Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance
    • G. Jeschke, and Y. Polyhach Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance Phys. Chem. Chem. Phys. 9 2007 1895 1910
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 1895-1910
    • Jeschke, G.1    Polyhach, Y.2
  • 39
    • 1942487282 scopus 로고    scopus 로고
    • +/Proline Transporter PutP of Escherichia coli
    • G. Jeschke, C. Wegener, M. Nietschke, H. Jung, and H.J. Steinhoff 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 2004 2551 2557 (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
  • 41
    • 79851516036 scopus 로고    scopus 로고
    • Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination
    • K. Kazmier, N.S. Alexander, J. Meiler, and H.S. McHaourab Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination J. Struct. Biol. 173 2011 549 557
    • (2011) J. Struct. Biol. , vol.173 , pp. 549-557
    • Kazmier, K.1    Alexander, N.S.2    Meiler, J.3    McHaourab, H.S.4
  • 42
    • 38849101674 scopus 로고    scopus 로고
    • Solutes alter the conformation of the ligand binding loops in outer membrane transporters
    • DOI 10.1021/bi7016415
    • M. Kim, Q. Xu, D. Murray, and D.S. Cafiso Solutes alter the conformation of the ligand binding loops in outer membrane transporters Biochemistry 47 2008 670 679 (Pubitemid 351195438)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 670-679
    • Kim, M.1    Xu, Q.2    Murray, D.3    Cafiso, D.S.4
  • 44
    • 38749131545 scopus 로고    scopus 로고
    • New G-protein-coupled receptor crystal structures: Insights and limitations
    • B. Kobilka, and G.F. Schertler New G-protein-coupled receptor crystal structures: insights and limitations Trends Pharmacol. Sci. 29 2008 79 83
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 79-83
    • Kobilka, B.1    Schertler, G.F.2
  • 45
    • 0032530971 scopus 로고    scopus 로고
    • Identification of protein folding patterns using site-directed spin labeling. Structural characterization of a β-sheet and putative substrate binding regions in the conserved domain of αA-crystallin
    • DOI 10.1021/bi9814078
    • H.A. Koteiche, A.R. Berengian, and H.S. Mchaourab Identification of protein folding patterns using site-directed spin labeling. Structural characterization of a beta-sheet and putative substrate binding regions in the conserved domain of alpha A-crystallin Biochemistry 37 1998 12681 12688 (Pubitemid 28433498)
    • (1998) Biochemistry , vol.37 , Issue.37 , pp. 12681-12688
    • Koteiche, H.A.1    Berengian, A.R.2    Mchaourab, H.S.3
  • 46
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • H. Krishnamurthy, C.L. Piscitelli, and E. Gouaux Unlocking the molecular secrets of sodium-coupled transporters Nature 459 2009 347 355
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 47
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: Implications for the interpretation of EPR spectra in terms of structure
    • DOI 10.1021/bi000604f
    • R. Langen, K.J. Oh, D. Cascio, and W.L. Hubbell Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure Biochemistry 39 2000 8396 8405 (Pubitemid 30489936)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4
  • 48
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • DOI 10.1021/bi960482k
    • H.S. Mchaourab, M.A. Lietzow, K. Hideg, and W.L. Hubbell Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics Biochemistry 35 1996 7692 7704 (Pubitemid 26202511)
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 49
    • 0002279727 scopus 로고
    • Electron electron double-resonance in electron-spin echo: Model biradical systems and the sensitized photolysis of decalin
    • A.D. Milov, A.B. Ponomarev, and Y.D. Tsvetkov Electron electron double-resonance in electron-spin echo: model biradical systems and the sensitized photolysis of decalin Chem. Phys. Lett. 110 1984 67 72
    • (1984) Chem. Phys. Lett. , vol.110 , pp. 67-72
    • Milov, A.D.1    Ponomarev, A.B.2    Tsvetkov, Y.D.3
  • 50
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • A.K. Mittermaier, and L.E. Kay Observing biological dynamics at atomic resolution using NMR Trends Biochem. Sci. 34 2009 601 611
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 51
    • 0014103899 scopus 로고
    • Spin-label study of hemoglobin conformations in solution
    • S. Ogawa, and H.M. McConnell Spin-label study of hemoglobin conformations in solution Proc. Natl. Acad. Sci. USA 58 1967 19 26
    • (1967) Proc. Natl. Acad. Sci. USA , vol.58 , pp. 19-26
    • Ogawa, S.1    McConnell, H.M.2
  • 54
    • 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
  • 55
    • 0033516494 scopus 로고    scopus 로고
    • +-channel activation gating
    • DOI 10.1126/science.285.5424.73
    • E. Perozo, D.M. Cortes, and L.G. Cuello Structural rearrangements underlying K+-channel activation gating Science 285 1999 73 78 (Pubitemid 29307565)
    • (1999) Science , vol.285 , Issue.5424 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 57
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Y. Polyhach, E. Bordignon, and G. Jeschke Rotamer libraries of spin labelled cysteines for protein studies Phys. Chem. Chem. Phys. 13 2011 2356 2366
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 58
    • 65249169367 scopus 로고    scopus 로고
    • Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation
    • M. Quick, A.M. Winther, L. Shi, P. Nissen, H. Weinstein, and J.A. Javitch Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation Proc. Natl. Acad. Sci. USA 106 2009 5563 5568
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5563-5568
    • Quick, M.1    Winther, A.M.2    Shi, L.3    Nissen, P.4    Weinstein, H.5    Javitch, J.A.6
  • 59
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • M.D. Rabenstein, and Y.K. Shin Determination of the distance between two spin labels attached to a macromolecule Proc. Natl. Acad. Sci. USA 92 1995 8239 8243
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 62
    • 43949138917 scopus 로고    scopus 로고
    • Parametrization, molecular dynamics simulation, and calculation of electron spin resonance spectra of a nitroxide spin label on a polyalanine α-helix
    • DOI 10.1021/jp711375x
    • D. Sezer, J.H. Freed, and B. Roux Parametrization, molecular dynamics simulation, and calculation of electron spin resonance spectra of a nitroxide spin label on a polyalanine alpha-helix J. Phys. Chem. B 112 2008 5755 5767 (Pubitemid 351704592)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.18 , pp. 5755-5767
    • Sezer, D.1    Freed, J.H.2    Roux, B.3
  • 64
    • 58149360795 scopus 로고    scopus 로고
    • Structural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data
    • P. Sompornpisut, B. Roux, and E. Perozo Structural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data Biophys. J. 95 2008 5349 5361
    • (2008) Biophys. J. , vol.95 , pp. 5349-5361
    • Sompornpisut, P.1    Roux, B.2    Perozo, E.3
  • 65
    • 65249144553 scopus 로고    scopus 로고
    • A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol
    • J. Tong, P.P. Borbat, J.H. Freed, and Y.K. Shin A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol Proc. Natl. Acad. Sci. USA 106 2009 5141 5146
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5141-5146
    • Tong, J.1    Borbat, P.P.2    Freed, J.H.3    Shin, Y.K.4
  • 66
    • 0028849634 scopus 로고
    • Membrane topology of helices VII and XI in the lactose permease of Escherichia coli studied by lacY-phoA fusion analysis and site-directed spectroscopy
    • M.L. Ujwal, H. Jung, E. Bibi, C. Manoil, C. Altenbach, W.L. Hubbell, and H.R. Kaback Membrane topology of helices VII and XI in the lactose permease of Escherichia coli studied by lacY-phoA fusion analysis and site-directed spectroscopy Biochemistry 34 1995 14909 14917
    • (1995) Biochemistry , vol.34 , pp. 14909-14917
    • Ujwal, M.L.1    Jung, H.2    Bibi, E.3    Manoil, C.4    Altenbach, C.5    Hubbell, W.L.6    Kaback, H.R.7
  • 68
    • 0035852964 scopus 로고    scopus 로고
    • Helix packing in the lactose permease of Escherichia coli: Distances between site-directed nitroxides and a lanthanide
    • DOI 10.1021/bi002333e
    • J. Voss, J. Wu, W.L. Hubbell, V. Jacques, C.F. Meares, and H.R. Kaback Helix packing in the lactose permease of Escherichia coli: distances between site-directed nitroxides and a lanthanide Biochemistry 40 2001 3184 3188 (Pubitemid 32205363)
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3184-3188
    • Voss, J.1    Wu, J.2    Hubbell, W.L.3    Jacques, V.4    Meares, C.F.5    Kaback, H.R.6
  • 69
    • 0014202988 scopus 로고
    • Fluorescence depolarization of rabbit gamma globulin conjugates
    • P. Wahl, and G. Weber Fluorescence depolarization of rabbit gamma globulin conjugates J. Mol. Biol. 30 1967 371 382
    • (1967) J. Mol. Biol. , vol.30 , pp. 371-382
    • Wahl, P.1    Weber, G.2
  • 70
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • A. Ward, C.L. Reyes, J. Yu, C.B. Roth, and G. Chang Flexibility in the ABC transporter MsbA: Alternating access with a twist Proc. Natl. Acad. Sci. USA 104 2007 19005 19010
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 71
    • 0029789304 scopus 로고    scopus 로고
    • Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli
    • DOI 10.1073/pnas.93.19.10123
    • J. Wu, J. Voss, W.L. Hubbell, and H.R. Kaback Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli Proc. Natl. Acad. Sci. USA 93 1996 10123 10127 (Pubitemid 26314585)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.19 , pp. 10123-10127
    • Wu, J.1    Voss, J.2    Hubbell, W.L.3    Kaback, H.R.4
  • 72
    • 33748509727 scopus 로고    scopus 로고
    • Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance
    • DOI 10.1021/bi061051x
    • Q. Xu, J.F. Ellena, M. Kim, and D.S. Cafiso Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance Biochemistry 45 2006 10847 10854 (Pubitemid 44360154)
    • (2006) Biochemistry , vol.45 , Issue.36 , pp. 10847-10854
    • Xu, Q.1    Ellena, J.F.2    Kim, M.3    Cafiso, D.S.4
  • 73
    • 24644470065 scopus 로고    scopus 로고
    • --dependent neurotransmitter transporters
    • DOI 10.1038/nature03978
    • A. Yamashita, S.K. Singh, T. Kawate, Y. Jin, and E. Gouaux Crystal structure of a bacterial homologue of Na+/Cl - dependent neurotransmitter transporters Nature 437 2005 215 223 (Pubitemid 41294479)
    • (2005) Nature , vol.437 , Issue.7056 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 75
    • 77952402284 scopus 로고    scopus 로고
    • Single-molecule dynamics of gating in a neurotransmitter transporter homologue
    • Y. Zhao, D. Terry, L. Shi, H. Weinstein, S.C. Blanchard, and J.A. Javitch Single-molecule dynamics of gating in a neurotransmitter transporter homologue Nature 465 2010 188 193
    • (2010) Nature , vol.465 , pp. 188-193
    • Zhao, Y.1    Terry, D.2    Shi, L.3    Weinstein, H.4    Blanchard, S.C.5    Javitch, J.A.6
  • 76
    • 70349785154 scopus 로고    scopus 로고
    • Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA
    • P. Zou, and H.S. McHaourab Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA J. Mol. Biol. 393 2009 574 585
    • (2009) J. Mol. Biol. , vol.393 , pp. 574-585
    • Zou, P.1    McHaourab, H.S.2
  • 77
    • 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
    • P. Zou, and H.S. McHaourab 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 2010 L18 L20
    • (2010) Biophys. J. , vol.98
    • Zou, P.1    McHaourab, H.S.2
  • 78
    • 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


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