메뉴 건너뛰기




Volumn 118, Issue 8, 2014, Pages 2124-2133

Secondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOLOGICAL MEMBRANES; PHOSPHOLIPIDS; PHOSPHORYLATION; SOLID STATE PHYSICS;

EID: 84896878195     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp500316s     Document Type: Article
Times cited : (17)

References (72)
  • 1
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A Crucial Regulator of Cardiac Contractility
    • MacLennan, D. H.; Kranias, E. G. Phospholamban: A Crucial Regulator of Cardiac Contractility Nat. Rev. Mol. Cell Biol. 2003, 4, 566-577
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 3
    • 3042730955 scopus 로고    scopus 로고
    • Direct Detection of Phospholamban and Sarcoplasmic Reticulum Ca-ATPase Interaction in Membranes Using Fluorescence Resonance Energy Transfers
    • Mueller, B.; Karim, C. B.; Negrashov, I. V.; Kutchai, H.; Thomas, D. D. Direct Detection of Phospholamban and Sarcoplasmic Reticulum Ca-ATPase Interaction in Membranes Using Fluorescence Resonance Energy Transfers Biochemistry 2004, 43, 8754-8765
    • (2004) Biochemistry , vol.43 , pp. 8754-8765
    • Mueller, B.1    Karim, C.B.2    Negrashov, I.V.3    Kutchai, H.4    Thomas, D.D.5
  • 4
    • 77449089784 scopus 로고    scopus 로고
    • Ca(2+) Binding to Site I of the Cardiac Ca(2+) Pump Is Sufficient to Dissociate Phospholamban
    • Chen, Z.; Akin, B. L.; Jones, L. R. Ca(2+) Binding to Site I of the Cardiac Ca(2+) Pump Is Sufficient to Dissociate Phospholamban J. Biol. Chem. 2010, 285, 3253-3260
    • (2010) J. Biol. Chem. , vol.285 , pp. 3253-3260
    • Chen, Z.1    Akin, B.L.2    Jones, L.R.3
  • 6
    • 67649865606 scopus 로고    scopus 로고
    • Structure and Topology of Monomeric Phospholamban in Lipid Membranes Determined by a Hybrid Solution and Solid-State NMR Approach
    • Traaseth, N. J.; Shi, L.; Verardi, R.; Mullen, D. G.; Barany, G.; Veglia, G. Structure and Topology of Monomeric Phospholamban in Lipid Membranes Determined by a Hybrid Solution and Solid-State NMR Approach Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 10165-10170
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10165-10170
    • Traaseth, N.J.1    Shi, L.2    Verardi, R.3    Mullen, D.G.4    Barany, G.5    Veglia, G.6
  • 7
    • 23344441824 scopus 로고    scopus 로고
    • The Structure of Phospholamban Pentamer Reveals a Channel-Like Architecture in Membranes
    • Oxenoid, K.; Chou, J. J. The Structure of Phospholamban Pentamer Reveals a Channel-Like Architecture in Membranes Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 10870-10875
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 8
    • 25144453329 scopus 로고    scopus 로고
    • Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy
    • Andronesi, O. C.; Becker, S.; Seidel, K.; Heise, H.; Young, H. S.; Baldus, M. Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2005, 127, 12965-12974
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 9
    • 74249121898 scopus 로고    scopus 로고
    • Probing Excited States and Activation Energy for the Integral Membrane Protein Phospholamban by NMR Cpmg Relaxation Dispersion Experiments
    • Traaseth, N. J.; Veglia, G. Probing Excited States and Activation Energy for the Integral Membrane Protein Phospholamban by NMR Cpmg Relaxation Dispersion Experiments Biochim. Biophys. Acta 2010, 1798, 77-81
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 77-81
    • Traaseth, N.J.1    Veglia, G.2
  • 10
    • 79954557710 scopus 로고    scopus 로고
    • An Allosteric Mechanism Inferred from Molecular Dynamics Simulations on Phospholamban Pentamer in Lipid Membranes
    • Lian, P.; Wei, D.-Q.; Wang, J.-F.; Chou, K.-C. An Allosteric Mechanism Inferred from Molecular Dynamics Simulations on Phospholamban Pentamer in Lipid Membranes PLOS One 2011, 6, e18587
    • (2011) PLOS One , vol.6 , pp. 18587
    • Lian, P.1    Wei, D.-Q.2    Wang, J.-F.3    Chou, K.-C.4
  • 11
    • 42049119152 scopus 로고    scopus 로고
    • Structural Characterization of Ca2+-ATPase-Bound Phospholarnban in Lipid Bilayers by Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy
    • Seidel, K.; Andronesi, O. C.; Krebs, J.; Griesinger, C.; Young, H. S.; Becker, S.; Baldus, M. Structural Characterization of Ca2+-ATPase-Bound Phospholarnban in Lipid Bilayers by Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy Biochemistry 2008, 47, 4369-4376
    • (2008) Biochemistry , vol.47 , pp. 4369-4376
    • Seidel, K.1    Andronesi, O.C.2    Krebs, J.3    Griesinger, C.4    Young, H.S.5    Becker, S.6    Baldus, M.7
  • 12
    • 79959340086 scopus 로고    scopus 로고
    • Structural Topology of Phospholamban Pentamer in Lipid Bilayers by a Hybrid Solution and Solid-State NMR Method
    • Verardi, R.; Shi, L.; Traaseth, N. J.; Walsh, N.; Veglia, G. Structural Topology of Phospholamban Pentamer in Lipid Bilayers by a Hybrid Solution and Solid-State NMR Method Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 9101-9106
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9101-9106
    • Verardi, R.1    Shi, L.2    Traaseth, N.J.3    Walsh, N.4    Veglia, G.5
  • 13
    • 79954989974 scopus 로고    scopus 로고
    • Lipid-Mediated Folding/Unfolding of Phospholamban as a Regulatory Mechanism for the Sarcoplasmic Reticulum Ca(2+)-ATPase
    • Gustavsson, M.; Traaseth, N. J.; Karim, C. B.; Lockamy, E. L.; Thomas, D. D.; Veglia, G. Lipid-Mediated Folding/Unfolding of Phospholamban as a Regulatory Mechanism for the Sarcoplasmic Reticulum Ca(2+)-ATPase J. Mol. Biol. 2011, 408, 755-765
    • (2011) J. Mol. Biol. , vol.408 , pp. 755-765
    • Gustavsson, M.1    Traaseth, N.J.2    Karim, C.B.3    Lockamy, E.L.4    Thomas, D.D.5    Veglia, G.6
  • 14
    • 80052026932 scopus 로고    scopus 로고
    • Camp-Dependent Protein Kinase a Selects the Excited State of the Membrane Substrate Phospholamban
    • Masterson, L. R.; Yu, T.; Shi, L.; Wang, Y.; Gustavsson, M.; Mueller, M. M.; Veglia, G. Camp-Dependent Protein Kinase a Selects the Excited State of the Membrane Substrate Phospholamban J. Mol. Biol. 2011, 412, 155-164
    • (2011) J. Mol. Biol. , vol.412 , pp. 155-164
    • Masterson, L.R.1    Yu, T.2    Shi, L.3    Wang, Y.4    Gustavsson, M.5    Mueller, M.M.6    Veglia, G.7
  • 15
    • 33646112404 scopus 로고    scopus 로고
    • Phosphorylation-Dependent Conformational Switch in Spin-Labeled Phospholamban Bound to SERCA
    • Karim, C. B.; Zhang, Z. W.; Howard, E. C.; Torgersen, K. D.; Thomas, D. D. Phosphorylation-Dependent Conformational Switch in Spin-Labeled Phospholamban Bound to SERCA J. Mol. Biol. 2006, 358, 1032-1040
    • (2006) J. Mol. Biol. , vol.358 , pp. 1032-1040
    • Karim, C.B.1    Zhang, Z.W.2    Howard, E.C.3    Torgersen, K.D.4    Thomas, D.D.5
  • 16
    • 84855748562 scopus 로고    scopus 로고
    • Probing the Helical Tilt and Dynamic Properties of Membrane-Bound Phospholamban in Magnetically Aligned Bicelles Using Electron Paramagnetic Resonance Spectroscopy
    • Ghimire, H.; Abu-Baker, S.; Sahu, I. D.; Zhou, A. D.; Mayo, D. J.; Lee, R. T.; Lorigan, G. A. Probing the Helical Tilt and Dynamic Properties of Membrane-Bound Phospholamban in Magnetically Aligned Bicelles Using Electron Paramagnetic Resonance Spectroscopy Biochim. Biophys. Acta, Biomembr. 2012, 1818, 645-650
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 645-650
    • Ghimire, H.1    Abu-Baker, S.2    Sahu, I.D.3    Zhou, A.D.4    Mayo, D.J.5    Lee, R.T.6    Lorigan, G.A.7
  • 17
    • 16344378243 scopus 로고    scopus 로고
    • Mapping the Interaction Surface of a Membrane Protein: Unveiling the Conformational Switch of Phospholamban in Calcium Pump Regulation
    • Zamoon, J.; Nitu, F.; Karim, C.; Thomas, D. D.; Veglia, G. Mapping the Interaction Surface of a Membrane Protein: Unveiling the Conformational Switch of Phospholamban in Calcium Pump Regulation Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 4747-4752
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4747-4752
    • Zamoon, J.1    Nitu, F.2    Karim, C.3    Thomas, D.D.4    Veglia, G.5
  • 18
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and Phosphorylation Change the Oligomeric Structure of Phospholamban in Lipid Bilayers
    • Cornea, R. L.; Jones, L. R.; Autry, J. M.; Thomas, D. D. Mutation and Phosphorylation Change the Oligomeric Structure of Phospholamban in Lipid Bilayers Biochemistry 1997, 36, 2960-2967
    • (1997) Biochemistry , vol.36 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4
  • 19
    • 79955756677 scopus 로고    scopus 로고
    • Functional and Physical Competition between Phospholamban and Its Mutants Provides Insight into the Molecular Mechanism of Gene Therapy for Heart Failure
    • Lockamy, E. L.; Cornea, R. L.; Karim, C. B.; Thomas, D. D. Functional and Physical Competition between Phospholamban and Its Mutants Provides Insight into the Molecular Mechanism of Gene Therapy for Heart Failure Biochem. Biophys. Res. Commun. 2011, 408, 388-392
    • (2011) Biochem. Biophys. Res. Commun. , vol.408 , pp. 388-392
    • Lockamy, E.L.1    Cornea, R.L.2    Karim, C.B.3    Thomas, D.D.4
  • 21
    • 17844405054 scopus 로고    scopus 로고
    • The Alpha-Helical Propensity of the Cytoplasmic Domain of Phospholamban: A Molecular Dynamics Simulation of the Effect of Phosphorylation and Mutation
    • Paterlini, M. G.; Thomas, D. D. The Alpha-Helical Propensity of the Cytoplasmic Domain of Phospholamban: A Molecular Dynamics Simulation of the Effect of Phosphorylation and Mutation Biophys. J. 2005, 88, 3243-3251
    • (2005) Biophys. J. , vol.88 , pp. 3243-3251
    • Paterlini, M.G.1    Thomas, D.D.2
  • 22
    • 84870182359 scopus 로고    scopus 로고
    • Role of Conformational Sampling of Ser16 and Thr17-Phosphorylated Phospholamban in Interactions with SERCA
    • Sayadi, M.; Feig, M. Role of Conformational Sampling of Ser16 and Thr17-Phosphorylated Phospholamban in Interactions with SERCA Biochim. Biophys. Acta, Biomembr. 2013, 1828, 577-585
    • (2013) Biochim. Biophys. Acta, Biomembr. , vol.1828 , pp. 577-585
    • Sayadi, M.1    Feig, M.2
  • 23
    • 81855226617 scopus 로고    scopus 로고
    • Activating and Deactivating Roles of Lipid Bilayers on the Ca(2+)-ATPase/Phospholamban Complex
    • Gustavsson, M.; Traaseth, N. J.; Veglia, G. Activating and Deactivating Roles of Lipid Bilayers on the Ca(2+)-ATPase/Phospholamban Complex Biochemistry 2011, 50, 10367-10374
    • (2011) Biochemistry , vol.50 , pp. 10367-10374
    • Gustavsson, M.1    Traaseth, N.J.2    Veglia, G.3
  • 24
    • 81855192140 scopus 로고    scopus 로고
    • Probing Ground and Excited States of Phospholamban in Model and Native Lipid Membranes by Magic Angle Spinning NMR Spectroscopy
    • Gustavsson, M.; Traaseth, N. J.; Veglia, G. Probing Ground and Excited States of Phospholamban in Model and Native Lipid Membranes by Magic Angle Spinning NMR Spectroscopy Biochim. Biophys. Acta, Biomembr. 2012, 1818, 146-153
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 146-153
    • Gustavsson, M.1    Traaseth, N.J.2    Veglia, G.3
  • 25
    • 84857711710 scopus 로고    scopus 로고
    • Characterizing Phospholamban to Sarco(Endo) Plasmic Reticulum Ca2+-ATPase 2a (SERCA2a) Protein Binding Interactions in Human Cardiac Sarcoplasmic Reticulum Vesicles Using Chemical Cross-Linking
    • Akin, B. L.; Jones, L. R. Characterizing Phospholamban to Sarco(Endo) Plasmic Reticulum Ca2+-ATPase 2a (SERCA2a) Protein Binding Interactions in Human Cardiac Sarcoplasmic Reticulum Vesicles Using Chemical Cross-Linking J. Biol. Chem. 2012, 287, 7582-7593
    • (2012) J. Biol. Chem. , vol.287 , pp. 7582-7593
    • Akin, B.L.1    Jones, L.R.2
  • 26
    • 84882646469 scopus 로고    scopus 로고
    • Probing the Interaction of Arg9cys Mutated Phospholamban with Phospholipid Bilayers by Solid-State NMR Spectroscopy
    • Yu, X.; Lorigan, G. A. Probing the Interaction of Arg9cys Mutated Phospholamban with Phospholipid Bilayers by Solid-State NMR Spectroscopy Biochim. Biophys. Acta, Biomembr. 2013, 1828, 2444-2449
    • (2013) Biochim. Biophys. Acta, Biomembr. , vol.1828 , pp. 2444-2449
    • Yu, X.1    Lorigan, G.A.2
  • 29
    • 79952607945 scopus 로고    scopus 로고
    • Lethal Arg9cys Phospholamban Mutation Hinders Ca(2+)-ATPase Regulation and Phosphorylation by Protein Kinase A
    • Ha, K. N.; Masterson, L. R.; Hou, Z.; Verardi, R.; Walsh, N.; Veglia, G.; Robia, S. L. Lethal Arg9cys Phospholamban Mutation Hinders Ca(2+)-ATPase Regulation and Phosphorylation by Protein Kinase A Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 2735-2740
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2735-2740
    • Ha, K.N.1    Masterson, L.R.2    Hou, Z.3    Verardi, R.4    Walsh, N.5    Veglia, G.6    Robia, S.L.7
  • 30
    • 36849019979 scopus 로고    scopus 로고
    • NMR Studies on Fully Hydrated Membrane Proteins, with Emphasis on Bacteriorhodopsin as a Typical and Prototype Membrane Protein
    • Saito, H.; Naito, A. NMR Studies on Fully Hydrated Membrane Proteins, with Emphasis on Bacteriorhodopsin as a Typical and Prototype Membrane Protein Biochim. Biophys. Acta 2007, 1768, 3145-3161
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3145-3161
    • Saito, H.1    Naito, A.2
  • 32
    • 45749128574 scopus 로고    scopus 로고
    • Orientation of the Escherichia Coli Outer Membrane Protein Ompx in Phospholipid Bilayer Membranes Determined by Solid-State NMR
    • Mahalakshmi, R.; Marassi, F. M. Orientation of the Escherichia Coli Outer Membrane Protein Ompx in Phospholipid Bilayer Membranes Determined by Solid-State NMR Biochemistry 2008, 47, 6531-6538
    • (2008) Biochemistry , vol.47 , pp. 6531-6538
    • Mahalakshmi, R.1    Marassi, F.M.2
  • 34
    • 0030861070 scopus 로고    scopus 로고
    • NMR and Membrane Proteins
    • Opella, S. J. NMR and Membrane Proteins Nat. Struct. Biol. 1997, 4, 845-848
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 845-848
    • Opella, S.J.1
  • 35
    • 4344704702 scopus 로고    scopus 로고
    • Structure Determination of Membrane Proteins by NMR Spectroscopy
    • Opella, S. J.; Marassi, F. M. Structure Determination of Membrane Proteins by NMR Spectroscopy Chem. Rev. 2004, 104, 3587-3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 36
    • 34548812858 scopus 로고    scopus 로고
    • Structure, Topology, and Dynamics of Membrane Peptides and Proteins from Solid-State NMR Spectroscopy
    • Hong, M. Structure, Topology, and Dynamics of Membrane Peptides and Proteins from Solid-State NMR Spectroscopy J. Phys. Chem. B 2007, 111, 10340-10351
    • (2007) J. Phys. Chem. B , vol.111 , pp. 10340-10351
    • Hong, M.1
  • 37
    • 66249095478 scopus 로고    scopus 로고
    • Liposomes: Technologies and Analytical Applications
    • Jesorka, A.; Orwar, O. Liposomes: Technologies and Analytical Applications Annu. Rev. Anal. Chem. 2008, 1, 801-832
    • (2008) Annu. Rev. Anal. Chem. , vol.1 , pp. 801-832
    • Jesorka, A.1    Orwar, O.2
  • 38
    • 84882584948 scopus 로고    scopus 로고
    • Magnetic Resonance Spectroscopic Studies of the Integral Membrane Protein Phospholamban
    • Webb, G. A. Springer: Dordrecht, The Netherlands
    • Lorigan, G. A., Magnetic Resonance Spectroscopic Studies of the Integral Membrane Protein Phospholamban. In Modern Magnetic Resonance: Applications in Chemistry, Biological and Marine Sciences; Webb, G. A., Ed.; Springer: Dordrecht, The Netherlands, 2008; Vol. 1, pp 313-318.
    • (2008) Modern Magnetic Resonance: Applications in Chemistry, Biological and Marine Sciences , vol.1 , pp. 313-318
    • Lorigan, G.A.1
  • 39
    • 79960977911 scopus 로고    scopus 로고
    • Solution NMR Study of Integral Membrane Proteins
    • Kang, C.; Li, Q. Solution NMR Study of Integral Membrane Proteins Curr. Opin. Chem. Biol. 2011, 15, 560-569
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 560-569
    • Kang, C.1    Li, Q.2
  • 40
    • 4544342928 scopus 로고    scopus 로고
    • Potassium Channels and the Atomic Basis of Selective Ion Conduction (Nobel Lecture)
    • MacKinnon, R. Potassium Channels and the Atomic Basis of Selective Ion Conduction (Nobel Lecture) Angew. Chem., Int. Ed. 2004, 43, 4265-4277
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 4265-4277
    • MacKinnon, R.1
  • 41
    • 37349016530 scopus 로고    scopus 로고
    • Protein Crystallography for Non-Crystallographers, or How to Get the Best (but Not More) from Published Macromolecular Structures
    • Wlodawer, A.; Minor, W.; Dauter, Z.; Jaskolski, M. Protein Crystallography for Non-Crystallographers, or How to Get the Best (but Not More) from Published Macromolecular Structures FEBS J. 2008, 275, 1-21
    • (2008) FEBS J. , vol.275 , pp. 1-21
    • Wlodawer, A.1    Minor, W.2    Dauter, Z.3    Jaskolski, M.4
  • 42
    • 0036310711 scopus 로고    scopus 로고
    • On the Role of the Crystal Environment in Determining Protein Side-Chain Conformations
    • Jacobson, M. P.; Friesner, R. A.; Xiang, Z. X.; Honig, B. On the Role of the Crystal Environment in Determining Protein Side-Chain Conformations J. Mol. Biol. 2002, 320, 597-608
    • (2002) J. Mol. Biol. , vol.320 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Xiang, Z.X.3    Honig, B.4
  • 43
    • 0029794277 scopus 로고    scopus 로고
    • Secondary Structure and Location of a Magainin Analogue in Synthetic Phospholipid Bilayers
    • Hirsh, D. J.; Hammer, J.; Maloy, W. L.; Blazyk, J.; Schaefer, J. Secondary Structure and Location of a Magainin Analogue in Synthetic Phospholipid Bilayers Biochemistry 1996, 35, 12733-12741
    • (1996) Biochemistry , vol.35 , pp. 12733-12741
    • Hirsh, D.J.1    Hammer, J.2    Maloy, W.L.3    Blazyk, J.4    Schaefer, J.5
  • 44
    • 0037102901 scopus 로고    scopus 로고
    • Determination of Alpha-Helix and Beta-Sheet Stability in the Solid State: A Solid-State NMR Investigation of Poly (L-Alanine)
    • Wildman, K. A. H.; Lee, D. K.; Ramamoorthy, A. Determination of Alpha-Helix and Beta-Sheet Stability in the Solid State: A Solid-State NMR Investigation of Poly (L-Alanine) Biopolymers 2002, 64, 246-254
    • (2002) Biopolymers , vol.64 , pp. 246-254
    • Wildman, K.A.H.1    Lee, D.K.2    Ramamoorthy, A.3
  • 45
    • 0027331560 scopus 로고
    • A High-Resolution Solid-State C-13-NMR Study on 1-C-13 Ala and 3-C-13 Ala and 1-C-13 Leu and Val-Labeled Bacteriorhodopsin - Conformation and Dynamics of Transmembrane Helices, Loops and Termini, and Hydration-Induced Conformational Change
    • Tuzi, S.; Naito, A.; Saito, H. A High-Resolution Solid-State C-13-NMR Study on 1-C-13 Ala and 3-C-13 Ala and 1-C-13 Leu and Val-Labeled Bacteriorhodopsin-Conformation and Dynamics of Transmembrane Helices, Loops and Termini, and Hydration-Induced Conformational Change Eur. J. Biochem. 1993, 218, 837-844
    • (1993) Eur. J. Biochem. , vol.218 , pp. 837-844
    • Tuzi, S.1    Naito, A.2    Saito, H.3
  • 46
    • 0028670894 scopus 로고
    • C-13 NMR-Study on Conformation and Dynamics of the Transmembrane Alpha-Helices, Loops, and C-Terminus of 3-C-13 Ala-Labeled Bacteriorhodopsin
    • Tuzi, S.; Naito, A.; Saito, H. C-13 NMR-Study on Conformation and Dynamics of the Transmembrane Alpha-Helices, Loops, and C-Terminus of 3-C-13 Ala-Labeled Bacteriorhodopsin Biochemistry 1994, 33, 15046-15052
    • (1994) Biochemistry , vol.33 , pp. 15046-15052
    • Tuzi, S.1    Naito, A.2    Saito, H.3
  • 47
    • 4744363014 scopus 로고    scopus 로고
    • Structural Investigations of a Human Calcitonin-Derived Carrier Peptide in a Membrane Environment by Solid-State NMR
    • Wagner, K.; Beck-Sickinger, A. G.; Huster, D. Structural Investigations of a Human Calcitonin-Derived Carrier Peptide in a Membrane Environment by Solid-State NMR Biochemistry 2004, 43, 12459-12468
    • (2004) Biochemistry , vol.43 , pp. 12459-12468
    • Wagner, K.1    Beck-Sickinger, A.G.2    Huster, D.3
  • 48
    • 0001427112 scopus 로고    scopus 로고
    • Determination of the Solid-State Conformations of Polyalanine Using Magic-Angle Spinning NMR Spectroscopy
    • Lee, D. K.; Ramamoorthy, A. Determination of the Solid-State Conformations of Polyalanine Using Magic-Angle Spinning NMR Spectroscopy J. Phys. Chem. 1999, 103, 271-275
    • (1999) J. Phys. Chem. , vol.103 , pp. 271-275
    • Lee, D.K.1    Ramamoorthy, A.2
  • 49
    • 33750707584 scopus 로고    scopus 로고
    • Phospholamban and Its Phosphorylated Form Interact Differently with Lipid Bilayers: A(31)P, (2)H, and (13)C Solid-State NMR Spectroscopic Study
    • Abu-Baker, S.; Lorigan, G. A. Phospholamban and Its Phosphorylated Form Interact Differently with Lipid Bilayers: A(31)P, (2)H, and (13)C Solid-State NMR Spectroscopic Study Biochemistry 2006, 45, 13312-13322
    • (2006) Biochemistry , vol.45 , pp. 13312-13322
    • Abu-Baker, S.1    Lorigan, G.A.2
  • 50
    • 0023106948 scopus 로고
    • Dynamics of Fd-Coat Protein in the Bacteriophage
    • Colnago, L. A.; Valentine, K. G.; Opella, S. J. Dynamics of Fd-Coat Protein in the Bacteriophage Biochemistry 1987, 26, 847-854
    • (1987) Biochemistry , vol.26 , pp. 847-854
    • Colnago, L.A.1    Valentine, K.G.2    Opella, S.J.3
  • 51
    • 35448982019 scopus 로고    scopus 로고
    • Side Chain and Backbone Dynamics of Phospholamban in Phospholipid Bilayers Utilizing H-2 and N-15 Solid-State NMR Spectroscopy
    • Abu-Baker, S.; Lu, J. X.; Chu, S. D.; Brinn, C. C.; Makaroff, C. A.; Lorigan, G. A. Side Chain and Backbone Dynamics of Phospholamban in Phospholipid Bilayers Utilizing H-2 and N-15 Solid-State NMR Spectroscopy Biochemistry 2007, 46, 11695-11706
    • (2007) Biochemistry , vol.46 , pp. 11695-11706
    • Abu-Baker, S.1    Lu, J.X.2    Chu, S.D.3    Brinn, C.C.4    Makaroff, C.A.5    Lorigan, G.A.6
  • 52
    • 74249090971 scopus 로고    scopus 로고
    • Solid-State (2)H and (15)N NMR Studies of Side-Chain and Backbone Dynamics of Phospholamban in Lipid Bilayers: Investigation of the N27a Mutation
    • Chu, S.; Coey, A. T.; Lorigan, G. A. Solid-State (2)H and (15)N NMR Studies of Side-Chain and Backbone Dynamics of Phospholamban in Lipid Bilayers: Investigation of the N27a Mutation Biochim. Biophys. Acta 2010, 1798, 210-215
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 210-215
    • Chu, S.1    Coey, A.T.2    Lorigan, G.A.3
  • 53
    • 0034614541 scopus 로고    scopus 로고
    • Helix Tilt of the M2 Transmembrane Peptide from Influenza a Virus: An Intrinsic Property
    • Kovacs, F. A.; Denny, J. K.; Song, Z.; Quine, J. R.; Cross, T. A. Helix Tilt of the M2 Transmembrane Peptide from Influenza a Virus: An Intrinsic Property J. Mol. Biol. 2000, 295, 117-125
    • (2000) J. Mol. Biol. , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 54
    • 0028025665 scopus 로고
    • Solid-State NMR Structural Studies of Peptides and Proteins in Membranes
    • Cross, T. A.; Opella, S. J. Solid-State NMR Structural Studies of Peptides and Proteins in Membranes Curr. Opin. Struct. Biol. 1994, 4, 574-581
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 574-581
    • Cross, T.A.1    Opella, S.J.2
  • 56
    • 0028730634 scopus 로고
    • Magnetically-Oriented Phospholipid Micelles as a Tool for the Study of Membrane-Associated Molecules
    • Sanders, C. R.; Hare, B. J.; Howard, K. P.; Prestegard, J. H. Magnetically-Oriented Phospholipid Micelles as a Tool for the Study of Membrane-Associated Molecules Prog. Nucl. Magn. Reson. Spectrosc. 1994, 26, 421-444
    • (1994) Prog. Nucl. Magn. Reson. Spectrosc. , vol.26 , pp. 421-444
    • Sanders, C.R.1    Hare, B.J.2    Howard, K.P.3    Prestegard, J.H.4
  • 57
    • 35649016222 scopus 로고    scopus 로고
    • The Structural Topology of Wild-Type Phospholamban in Oriented Lipid Bilayers Using N-15 Solid-State NMR Spectroscopy
    • Abu-Baker, S.; Lu, J.-X.; Chu, S.; Shetty, K. K.; Gor'kov, P. L.; Lorigan, G. A. The Structural Topology of Wild-Type Phospholamban in Oriented Lipid Bilayers Using N-15 Solid-State NMR Spectroscopy Protein Sci. 2007, 16, 2345-2349
    • (2007) Protein Sci. , vol.16 , pp. 2345-2349
    • Abu-Baker, S.1    Lu, J.-X.2    Chu, S.3    Shetty, K.K.4    Gor'kov, P.L.5    Lorigan, G.A.6
  • 58
    • 76749091146 scopus 로고    scopus 로고
    • (15)N Solid-State NMR Spectroscopic Studies on Phospholamban at Its Phosphorylated Form at Ser-16 in Aligned Phospholipid Bilayers
    • Chu, S.; Abu-Baker, S.; Lu, J.; Lorigan, G. A. (15)N Solid-State NMR Spectroscopic Studies on Phospholamban at Its Phosphorylated Form at Ser-16 in Aligned Phospholipid Bilayers Biochim. Biophys. Acta 2010, 1798, 312-317
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 312-317
    • Chu, S.1    Abu-Baker, S.2    Lu, J.3    Lorigan, G.A.4
  • 59
    • 8344223023 scopus 로고    scopus 로고
    • Investigating the Dynamic Properties of the Transmembrane Segment of Phospholamban Incorporated into Phospholipid Bilayers Utilizing H-2 and N-15 Solid-State NMR Spectroscopy
    • Tiburu, E. K.; Karp, E. S.; Dave, P. C.; Damodaran, K.; Lorigan, G. A. Investigating the Dynamic Properties of the Transmembrane Segment of Phospholamban Incorporated into Phospholipid Bilayers Utilizing H-2 and N-15 Solid-State NMR Spectroscopy Biochemistry 2004, 43, 13899-13909
    • (2004) Biochemistry , vol.43 , pp. 13899-13909
    • Tiburu, E.K.1    Karp, E.S.2    Dave, P.C.3    Damodaran, K.4    Lorigan, G.A.5
  • 60
    • 3543102159 scopus 로고    scopus 로고
    • Solid-State NMR Spectroscopic Studies of an Integral Membrane Protein Inserted into Aligned Phospholipid Bilayer Nanotube Arrays
    • Lorigan, G. A.; Dave, P. C.; Tiburu, E. K.; Damodaran, K.; Abu-Baker, S.; Karp, E. S.; Gibbons, W. J.; Minto, R. E. Solid-State NMR Spectroscopic Studies of an Integral Membrane Protein Inserted into Aligned Phospholipid Bilayer Nanotube Arrays J. Am. Chem. Soc. 2004, 126, 9504-9505
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9504-9505
    • Lorigan, G.A.1    Dave, P.C.2    Tiburu, E.K.3    Damodaran, K.4    Abu-Baker, S.5    Karp, E.S.6    Gibbons, W.J.7    Minto, R.E.8
  • 61
    • 0029820642 scopus 로고    scopus 로고
    • Transmembrane Region of the Epidermal Growth Factor Receptor: Behavior and Interactions Via H-2 NMR
    • Rigby, A. C.; Barber, K. R.; Shaw, G. S.; Grant, C. W. M. Transmembrane Region of the Epidermal Growth Factor Receptor: Behavior and Interactions Via H-2 NMR Biochemistry 1996, 35, 12591-12601
    • (1996) Biochemistry , vol.35 , pp. 12591-12601
    • Rigby, A.C.1    Barber, K.R.2    Shaw, G.S.3    Grant, C.W.M.4
  • 63
    • 84864535546 scopus 로고    scopus 로고
    • Lethal, Hereditary Mutants of Phospholamban Elude Phosphorylation by Protein Kinase A
    • Ceholski, D. K.; Trieber, C. A.; Holmes, C. F. B.; Young, H. S. Lethal, Hereditary Mutants of Phospholamban Elude Phosphorylation by Protein Kinase A J. Biol. Chem. 2012, 287, 26596-26605
    • (2012) J. Biol. Chem. , vol.287 , pp. 26596-26605
    • Ceholski, D.K.1    Trieber, C.A.2    Holmes, C.F.B.3    Young, H.S.4
  • 64
    • 77956502772 scopus 로고    scopus 로고
    • Superinhibitory Phospholamban Mutants Compete with Ca(2+) for Binding to SERCA2a by Stabilizing a Unique Nucleotide-Dependent Conformational State
    • Akin, B. L.; Chen, Z.; Jones, L. R. Superinhibitory Phospholamban Mutants Compete with Ca(2+) for Binding to SERCA2a by Stabilizing a Unique Nucleotide-Dependent Conformational State J. Biol. Chem. 2010, 285, 28540-28552
    • (2010) J. Biol. Chem. , vol.285 , pp. 28540-28552
    • Akin, B.L.1    Chen, Z.2    Jones, L.R.3
  • 65
    • 84860863765 scopus 로고    scopus 로고
    • Hydrophobic Imbalance in the Cytoplasmic Domain of Phospholamban Is a Determinant for Lethal Dilated Cardiomyopathy
    • Ceholski, D. K.; Trieber, C. A.; Young, H. S. Hydrophobic Imbalance in the Cytoplasmic Domain of Phospholamban Is a Determinant for Lethal Dilated Cardiomyopathy J. Biol. Chem. 2012, 287, 16521-16529
    • (2012) J. Biol. Chem. , vol.287 , pp. 16521-16529
    • Ceholski, D.K.1    Trieber, C.A.2    Young, H.S.3
  • 66
    • 84863419025 scopus 로고    scopus 로고
    • Phospholamban Mutants Compete with Wild Type for SERCA Binding in Living Cells
    • Gruber, S. J.; Haydon, S.; Thomas, D. D. Phospholamban Mutants Compete with Wild Type for SERCA Binding in Living Cells Biochem. Biophys. Res. Commun. 2012, 420, 236-240
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 236-240
    • Gruber, S.J.1    Haydon, S.2    Thomas, D.D.3
  • 67
    • 84859912916 scopus 로고    scopus 로고
    • Membrane Protein Structure and Dynamics from NMR Spectroscopy
    • forthcoming.
    • Hong, M.; Zhang, Y.; Hu, F. Membrane Protein Structure and Dynamics from NMR Spectroscopy. Annu. Rev. Phys. Chem. 2012, 63, forthcoming.
    • (2012) Annu. Rev. Phys. Chem. , vol.63
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 69
    • 44149106414 scopus 로고    scopus 로고
    • Structure, Dynamics, and Assembly of Filamentous Bacteriophages by Nuclear Magnetic Resonance Spectroscopy
    • Opella, S. J.; Zeri, A. C.; Park, S. H. Structure, Dynamics, and Assembly of Filamentous Bacteriophages by Nuclear Magnetic Resonance Spectroscopy Annu. Rev. Phys. Chem. 2008, 59, 635-657
    • (2008) Annu. Rev. Phys. Chem. , vol.59 , pp. 635-657
    • Opella, S.J.1    Zeri, A.C.2    Park, S.H.3
  • 71
    • 0001250543 scopus 로고
    • C-13 Nuclear Magnetic-Resonance of Polymers Spinning at Magic Angle
    • Schaefer, J.; Stejskal, E. O. C-13 Nuclear Magnetic-Resonance of Polymers Spinning at Magic Angle J. Am. Chem. Soc. 1976, 98, 1031-1032
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 1031-1032
    • Schaefer, J.1    Stejskal, E.O.2
  • 72
    • 0017252285 scopus 로고
    • Molecular-Motion and Order in Single-Bilayer Vesicles and Multilamellar Dispersions of Egg Lecithin and Lecithin-Cholesterol Mixtures-Deuterium Nuclear Magnetic-Resonance Study of Specifically Labeled Lipids
    • Stockton, G. W.; Polnaszek, C. F.; Tulloch, A. P.; Hasan, F.; Smith, I. C. P. Molecular-Motion and Order in Single-Bilayer Vesicles and Multilamellar Dispersions of Egg Lecithin and Lecithin-Cholesterol Mixtures-Deuterium Nuclear Magnetic-Resonance Study of Specifically Labeled Lipids Biochemistry 1976, 15, 954-966
    • (1976) Biochemistry , vol.15 , pp. 954-966
    • Stockton, G.W.1    Polnaszek, C.F.2    Tulloch, A.P.3    Hasan, F.4    Smith, I.C.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.