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Volumn 13, Issue 12, 2002, Pages 1376-1387

Hydrogen/deuterium exchange of hydrophobic peptides in model membranes by electrospray ionization mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON MICROSCOPY; HYDROPHOBICITY; MASS SPECTROMETRY; MEMBRANES; METHANOL; MICELLES;

EID: 0036884106     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1044-0305(02)00702-X     Document Type: Article
Times cited : (29)

References (52)
  • 1
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing Membrane Proteins
    • Bowie J.U. Stabilizing Membrane Proteins. Curr Opin Struct Biol. 11:2001;397-402.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 2
    • 0035443197 scopus 로고    scopus 로고
    • Biophysical Approaches to Membrane Protein Structure Determination
    • Arora A., Tamm L.K. Biophysical Approaches to Membrane Protein Structure Determination. Curr Opin Struct Biol. 11:2001;540-547.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 540-547
    • Arora, A.1    Tamm, L.K.2
  • 3
    • 0027787981 scopus 로고
    • Asp(96) Deprotonation and Transmembrane Alpha-Helical Structural-Changes in Bacteriorhodopsin
    • Rothschild K.J., Marti T., Sonar S., He Y.W., Rath P., Fischer W., Khorana H.G. Asp(96) Deprotonation and Transmembrane Alpha-Helical Structural-Changes in Bacteriorhodopsin. J Biol Chem. 268:1993;27046-27052.
    • (1993) J Biol Chem , vol.268 , pp. 27046-27052
    • Rothschild, K.J.1    Marti, T.2    Sonar, S.3    He, Y.W.4    Rath, P.5    Fischer, W.6    Khorana, H.G.7
  • 4
    • 0026746013 scopus 로고
    • Helical Structure and Orientation of Melittin in Dispersed Phospholipid Membranes from Amide Exchange Analysis in Situ
    • Dempsey C.E., Butler G.S. Helical Structure and Orientation of Melittin in Dispersed Phospholipid Membranes from Amide Exchange Analysis in Situ. Biochemistry. 31:1992;11973-11977.
    • (1992) Biochemistry , vol.31 , pp. 11973-11977
    • Dempsey, C.E.1    Butler, G.S.2
  • 5
    • 0036217488 scopus 로고    scopus 로고
    • Deuterium/Hydrogen Exchange Factors Measured by Solution Nuclear Magnetic Resonance Spectroscopy as Indicators of the Structure and Topology of Membrane Proteins
    • Veglia G., Zeri A.C., Ma C., Opella S.J. Deuterium/Hydrogen Exchange Factors Measured by Solution Nuclear Magnetic Resonance Spectroscopy as Indicators of the Structure and Topology of Membrane Proteins. Biophys J. 82:2002;2176-2183.
    • (2002) Biophys J , vol.82 , pp. 2176-2183
    • Veglia, G.1    Zeri, A.C.2    Ma, C.3    Opella, S.J.4
  • 6
    • 0034602452 scopus 로고    scopus 로고
    • Direct Evidence for the Cooperative Unfolding of Cytochrome c in Lipid Membranes from H-H-2 Exchange Kinetics
    • Pinheiro T.J.T., Cheng H., Seeholzer S.H., Roder H. Direct Evidence for the Cooperative Unfolding of Cytochrome c in Lipid Membranes from H-H-2 Exchange Kinetics. J Mol Biol. 303:2000;617-626.
    • (2000) J Mol Biol , vol.303 , pp. 617-626
    • Pinheiro, T.J.T.1    Cheng, H.2    Seeholzer, S.H.3    Roder, H.4
  • 7
    • 0033019673 scopus 로고    scopus 로고
    • Solid-State NMR and Hydrogen-Deuterium Exchange in a Bilayer-Solubilized Peptide: Structural and Mechanistic Implications
    • Cotten M., Fu R., Cross T.A. Solid-State NMR and Hydrogen-Deuterium Exchange in a Bilayer-Solubilized Peptide Structural and Mechanistic Implications . Biophys J. 76:1999;1179-1189.
    • (1999) Biophys J , vol.76 , pp. 1179-1189
    • Cotten, M.1    Fu, R.2    Cross, T.A.3
  • 8
    • 0035861570 scopus 로고    scopus 로고
    • Dynamic Protein Complexes: Insights from Mass Spectrometry
    • Hernandez H., Robinson C.V. Dynamic Protein Complexes Insights from Mass Spectrometry . J Biol Chem. 276:2001;46685-46688.
    • (2001) J Biol Chem , vol.276 , pp. 46685-46688
    • Hernandez, H.1    Robinson, C.V.2
  • 9
    • 0034118193 scopus 로고    scopus 로고
    • Solvent Effects on the Conformation of the Transmembrane Peptide Gramicidin A: Insights from Electrospray Ionization Mass Spectrometry
    • Bouchard M., Benjamin D.R., Tito P., Robinson C.V., Dobson C.M. Solvent Effects on the Conformation of the Transmembrane Peptide Gramicidin A Insights from Electrospray Ionization Mass Spectrometry . Biophys J. 78:2000;1010-1017.
    • (2000) Biophys J , vol.78 , pp. 1010-1017
    • Bouchard, M.1    Benjamin, D.R.2    Tito, P.3    Robinson, C.V.4    Dobson, C.M.5
  • 10
    • 0034724213 scopus 로고    scopus 로고
    • Electrospray Ionization Mass Spectrometry as a Tool to Analyze Hydrogen/Deuterium Exchange Kinetics of Transmembrane Peptides in Lipid Bilayers
    • Demmers J.A.A., Haverkamp J., Heck A.J.R., Koeppe R.E., Killian J.A. Electrospray Ionization Mass Spectrometry as a Tool to Analyze Hydrogen/Deuterium Exchange Kinetics of Transmembrane Peptides in Lipid Bilayers. Proc Natl Acad Sci USA. 97:2000;3189-3194.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3189-3194
    • Demmers, J.A.A.1    Haverkamp, J.2    Heck, A.J.R.3    Koeppe, R.E.4    Killian, J.A.5
  • 11
    • 0035860765 scopus 로고    scopus 로고
    • Interfacial Positioning and Stability of Transmembrane Peptides in Lipid Bilayers Studied by Combining Hydrogen/Deuterium Exchange and Mass Spectrometry
    • Demmers J.A.A., van Duijn E., Haverkamp J., Greathouse D.V., Koeppe R.E., Heck A.J.R., Killian J.A. Interfacial Positioning and Stability of Transmembrane Peptides in Lipid Bilayers Studied by Combining Hydrogen/Deuterium Exchange and Mass Spectrometry. J Biol Chem. 276:2001;34501-34508.
    • (2001) J Biol Chem , vol.276 , pp. 34501-34508
    • Demmers, J.A.A.1    Van Duijn, E.2    Haverkamp, J.3    Greathouse, D.V.4    Koeppe, R.E.5    Heck, A.J.R.6    Killian, J.A.7
  • 12
    • 0035567106 scopus 로고    scopus 로고
    • Structure of Melittin Bound to Phospholipid Micelles Studied Using Hydrogen-Deuterium Exchange and Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
    • Akashi S., Takio K. Structure of Melittin Bound to Phospholipid Micelles Studied Using Hydrogen-Deuterium Exchange and Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. J Am Soc Mass Spectrom. 12:2001;1247-1253.
    • (2001) J Am Soc Mass Spectrom , vol.12 , pp. 1247-1253
    • Akashi, S.1    Takio, K.2
  • 13
    • 0024604085 scopus 로고
    • Detergent Structure and Associated Lipid as Determinants in the Stabilization of Solubilized Ca2+-ATPase from Sarcoplasmic Reticulum
    • Lund S., Orlowski S., de Foresta B., le Champeil P., Maire M., Møller J.V. Detergent Structure and Associated Lipid as Determinants in the Stabilization of Solubilized Ca2+-ATPase from Sarcoplasmic Reticulum. J Biol Chem. 264:1989;4907-4915.
    • (1989) J Biol Chem , vol.264 , pp. 4907-4915
    • Lund, S.1    Orlowski, S.2    De Foresta, B.3    Le Champeil, P.4    Maire, M.5    Møller, J.V.6
  • 15
    • 0014940381 scopus 로고
    • The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes
    • Reynolds J.A., Tanford C. The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes. J Biol Chem. 245:1970;5161-5165.
    • (1970) J Biol Chem , vol.245 , pp. 5161-5165
    • Reynolds, J.A.1    Tanford, C.2
  • 16
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole Sequencing of Proteins from Polyacrylamide Gels by Nano-Electrospray Mass Spectrometry
    • Wilm M., Shevchenko A., Houthaeve T., Breit S., Schweigerer L., Fotsis T., Mann M. Femtomole Sequencing of Proteins from Polyacrylamide Gels by Nano-Electrospray Mass Spectrometry. Nature. 379:1996;466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 20
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of Membrane Proteins and Lipids with Solubilizing Detergents
    • le Maire M., Champeil P., Møller J.V. Interaction of Membrane Proteins and Lipids with Solubilizing Detergents. Biochim. Biophys. Acta. 1508:2000;86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 21
    • 0033473760 scopus 로고    scopus 로고
    • Matrix Assisted Laser Desorption Ionization Hydrogen/Deuterium Exchange Studies to Probe Peptide Conformational Changes
    • Figueroa I.D., Russell D.H. Matrix Assisted Laser Desorption Ionization Hydrogen/Deuterium Exchange Studies to Probe Peptide Conformational Changes. J Am Soc Mass Spec. 10:1999;719-731.
    • (1999) J Am Soc Mass Spec , vol.10 , pp. 719-731
    • Figueroa, I.D.1    Russell, D.H.2
  • 22
  • 23
    • 0035753065 scopus 로고    scopus 로고
    • High Resolution, High-Throughput Amide Deuterium Exchange-Mass Spectrometry (DXMS) Determination of Protein Binding Site Structure and Dynamics: Utility in Pharmaceutical Design
    • Woods V.L., Hamuro Y. High Resolution, High-Throughput Amide Deuterium Exchange-Mass Spectrometry (DXMS) Determination of Protein Binding Site Structure and Dynamics Utility in Pharmaceutical Design . J Cell Biochem. 37:(Suppl.):2001;89-98.
    • (2001) J Cell Biochem , vol.37 , Issue.SUPPL. , pp. 89-98
    • Woods, V.L.1    Hamuro, Y.2
  • 24
    • 0022157043 scopus 로고
    • The Molecular Basis of the Specific Anti-Influenza Action of Amantadine
    • Hay A., Wolstenholme A., Skehel J., Smith M. The Molecular Basis of the Specific Anti-Influenza Action of Amantadine. EMBO J. 4:1985;3021-3024.
    • (1985) EMBO J , vol.4 , pp. 3021-3024
    • Hay, A.1    Wolstenholme, A.2    Skehel, J.3    Smith, M.4
  • 25
    • 0037133750 scopus 로고    scopus 로고
    • Viral Ion Channels: Structure and Function
    • Fischer W.B., Sansom M.S.P. Viral Ion Channels Structure and Function . Biochim Biophys Acta. 1561:2002;27-43.
    • (2002) Biochim Biophys Acta , vol.1561 , pp. 27-43
    • Fischer, W.B.1    Sansom, M.S.P.2
  • 26
    • 0036007087 scopus 로고    scopus 로고
    • Influenza A Virus M2 Ion Channel Activity is Essential for Efficient Replication in Tissue Culture
    • Takeda M., Pekosz A., Shuck K., Pinto L.H., Lamb R.A. Influenza A Virus M2 Ion Channel Activity is Essential for Efficient Replication in Tissue Culture. J Virol. 76:2002;1391-1399.
    • (2002) J Virol , vol.76 , pp. 1391-1399
    • Takeda, M.1    Pekosz, A.2    Shuck, K.3    Pinto, L.H.4    Lamb, R.A.5
  • 27
    • 0023943222 scopus 로고    scopus 로고
    • Integration of a Small Integral Membrane-Protein, M2, of Influenza Virus into the Endoplasmic-Reticulum. Analysis of the Internal Signal-Anchor Domain of a Protein with an Ectoplasmic NH2 Terminus
    • Hull J.D., Gilmore R., Lamb R.A. Integration of a Small Integral Membrane-Protein, M2, of Influenza Virus into the Endoplasmic-Reticulum. Analysis of the Internal Signal-Anchor Domain of a Protein with an Ectoplasmic NH2 Terminus. J Cell Biol. 106:1998;1489-1498.
    • (1998) J Cell Biol , vol.106 , pp. 1489-1498
    • Hull, J.D.1    Gilmore, R.2    Lamb, R.A.3
  • 29
    • 0033605318 scopus 로고    scopus 로고
    • Experimentally Based Orientational Refinement of Membrane Protein Models: A Structure for the Influenza A M2 H+ Channel
    • Kukol A., Adams P.D., Rice L.M., Brunger A.T., Arkin I.T. Experimentally Based Orientational Refinement of Membrane Protein Models A Structure for the Influenza A M2 H+ Channel . J Mol Biol. 286:1999;951-962.
    • (1999) J Mol Biol , vol.286 , pp. 951-962
    • Kukol, A.1    Adams, P.D.2    Rice, L.M.3    Brunger, A.T.4    Arkin, I.T.5
  • 30
    • 0034775070 scopus 로고    scopus 로고
    • Structure of the Transmembrane Region of the M2 Protein H+ Channel
    • Wang J., Kim S., Kovacs F., Cross T.A. Structure of the Transmembrane Region of the M2 Protein H+ Channel. Protein Sci. 10:2001;2241-2250.
    • (2001) Protein Sci , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 31
    • 0034030929 scopus 로고    scopus 로고
    • Exploring Models of the Influenza A M2 Channel: MD Simulations in a Phospholipid Bilayer
    • Forrest L.R., Kukol A., Arkin I.T., Tieleman D.P., Sansom M.S.P. Exploring Models of the Influenza A M2 Channel MD Simulations in a Phospholipid Bilayer . Biophys J. 78:2000;55-69.
    • (2000) Biophys J , vol.78 , pp. 55-69
    • Forrest, L.R.1    Kukol, A.2    Arkin, I.T.3    Tieleman, D.P.4    Sansom, M.S.P.5
  • 36
    • 0019851083 scopus 로고
    • Effects of Octyl β-Glucoside on Insulin Binding to Solubilized Membrane-Receptors
    • Gould R.J., Ginsberg B.H., Spector A.A. Effects of Octyl β-Glucoside on Insulin Binding to Solubilized Membrane-Receptors. Biochemistry. 20:1981;6776-6781.
    • (1981) Biochemistry , vol.20 , pp. 6776-6781
    • Gould, R.J.1    Ginsberg, B.H.2    Spector, A.A.3
  • 37
    • 0023712988 scopus 로고
    • Liposomes - Preparation, Characterization, and Preservation
    • Lichtenberg D., Barenholz Y. Liposomes - Preparation, Characterization, and Preservation. Methods Biochem Anal. 33:1988;337-462.
    • (1988) Methods Biochem Anal , vol.33 , pp. 337-462
    • Lichtenberg, D.1    Barenholz, Y.2
  • 38
    • 0030846528 scopus 로고    scopus 로고
    • Preparation of Liposomes Encapsulating Water-Soluble Compounds Using Supercritical Carbon Dioxide
    • Frederiksen L., Anton K., van Hoogevest P., Keller H.R., Leuenberger H. Preparation of Liposomes Encapsulating Water-Soluble Compounds Using Supercritical Carbon Dioxide. J Pharm Sci. 86:1997;921-928.
    • (1997) J Pharm Sci , vol.86 , pp. 921-928
    • Frederiksen, L.1    Anton, K.2    Van Hoogevest, P.3    Keller, H.R.4    Leuenberger, H.5
  • 39
    • 0020485881 scopus 로고
    • Aggregation of Dipalmitoyl Phosphatidylcholine Vesicles
    • Wong M., Thompson T.E. Aggregation of Dipalmitoyl Phosphatidylcholine Vesicles. Biochem. 21:1982;4133-4139.
    • (1982) Biochem , vol.21 , pp. 4133-4139
    • Wong, M.1    Thompson, T.E.2
  • 40
    • 0031943486 scopus 로고    scopus 로고
    • Stabilization of Small Unilamellar DMPC-Liposomes by Uncharged Polymers
    • Grohmann F.L., Csempesz F., Szogyi M. Stabilization of Small Unilamellar DMPC-Liposomes by Uncharged Polymers. Colloid Polym Sci. 276:1998;66-71.
    • (1998) Colloid Polym Sci , vol.276 , pp. 66-71
    • Grohmann, F.L.1    Csempesz, F.2    Szogyi, M.3
  • 41
    • 0001191099 scopus 로고
    • Disintegration of Water Drops in an Electric Field
    • Taylor S.G. Disintegration of Water Drops in an Electric Field. Proc. Roy. Soc. A. 280:1964;383-397.
    • (1964) Proc. Roy. Soc. A , vol.280 , pp. 383-397
    • Taylor, S.G.1
  • 42
    • 0027950616 scopus 로고
    • On the Structure of an Electrostatic Spray of Monodisperse Droplets
    • Tang K., Gomez A. On the Structure of an Electrostatic Spray of Monodisperse Droplets. Phys. Fluids. 6:1994;2317-2332.
    • (1994) Phys. Fluids , vol.6 , pp. 2317-2332
    • Tang, K.1    Gomez, A.2
  • 43
    • 0031568759 scopus 로고    scopus 로고
    • Charge and Size Distributions of Electrospray Drops
    • de Juan L., de la Mora J.F. Charge and Size Distributions of Electrospray Drops. J Colloid Interf Sci. 186:1997;280-293.
    • (1997) J Colloid Interf Sci , vol.186 , pp. 280-293
    • De Juan, L.1    De la Mora, J.F.2
  • 44
    • 0032628157 scopus 로고    scopus 로고
    • Structure of Taylor Cone-Jets: Limit of Low Flow Rates
    • Cherney L.T. Structure of Taylor Cone-Jets Limit of Low Flow Rates . J Fluid Mech. 378:1999;167-196.
    • (1999) J Fluid Mech , vol.378 , pp. 167-196
    • Cherney, L.T.1
  • 45
    • 0028368708 scopus 로고
    • The Current Emitted by Highly Conducting Taylor Cones
    • de la Mora J.F., Loscertales I.G. The Current Emitted by Highly Conducting Taylor Cones. J Fluid Mech. 260:1994;155-184.
    • (1994) J Fluid Mech , vol.260 , pp. 155-184
    • De la Mora, J.F.1    Loscertales, I.G.2
  • 46
    • 4243507249 scopus 로고
    • Electron Microscopic Measure of Virus Particle Dispersions in Suspension
    • Sharp D.G., Buckingham M.J. Electron Microscopic Measure of Virus Particle Dispersions in Suspension. Biochim Biophys Acta. 19:1956;13-21.
    • (1956) Biochim Biophys Acta , vol.19 , pp. 13-21
    • Sharp, D.G.1    Buckingham, M.J.2
  • 47
    • 0030918033 scopus 로고    scopus 로고
    • Characterization of Phospholipids by Electron Impact, Field Desorption, and Liquid Secondary Ion Mass Spectrometry
    • Wu Y., Wang J.Z., Sui S.F. Characterization of Phospholipids by Electron Impact, Field Desorption, and Liquid Secondary Ion Mass Spectrometry. J Mass Spectrom. 32:1997;616-625.
    • (1997) J Mass Spectrom , vol.32 , pp. 616-625
    • Wu, Y.1    Wang, J.Z.2    Sui, S.F.3
  • 48
    • 0034066471 scopus 로고    scopus 로고
    • Membrane Proteins and Proteomics: Un amour impossible?
    • Santoni V., Molloy M., Rabilloud T. Membrane Proteins and Proteomics Un amour impossible? Electrophoresis. 21:2000;1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 49
    • 0027381687 scopus 로고
    • Separation of the Sticky Peptides from Membrane Proteins by High Performance Liquid Chromatography in a Normal Phase System
    • Lerro K.A., Orlando R., Zhang H.Z., Usherwood P.N.R., Nakanishi K. Separation of the Sticky Peptides from Membrane Proteins by High Performance Liquid Chromatography in a Normal Phase System. Anal Biochem. 215:1993;38-44.
    • (1993) Anal Biochem , vol.215 , pp. 38-44
    • Lerro, K.A.1    Orlando, R.2    Zhang, H.Z.3    Usherwood, P.N.R.4    Nakanishi, K.5
  • 50
    • 0023224412 scopus 로고
    • Fourier Transform Infrared Spectroscopic Study of the Structure and Conformational Changes of the Human Erythrocyte Glucose Transporter
    • Alvarez J., Lee D.C., Baldwin S.A., Chapman D. Fourier Transform Infrared Spectroscopic Study of the Structure and Conformational Changes of the Human Erythrocyte Glucose Transporter. J Biol Chem. 262:1987;3502-3509.
    • (1987) J Biol Chem , vol.262 , pp. 3502-3509
    • Alvarez, J.1    Lee, D.C.2    Baldwin, S.A.3    Chapman, D.4
  • 51
    • 0030885252 scopus 로고    scopus 로고
    • The Lipid Bilayer Determines Helical Title Angle and Function in Lactose Permease of Escherichia coli
    • le Coutre J., Narasimhan L.R., Patel C.K.N., Kaback H.R. The Lipid Bilayer Determines Helical Title Angle and Function in Lactose Permease of Escherichia coli. Proc Natl Acad Sci USA. 94:1997;10167-10171.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10167-10171
    • Le Coutre, J.1    Narasimhan, L.R.2    Patel, C.K.N.3    Kaback, H.R.4
  • 52
    • 0029999396 scopus 로고    scopus 로고
    • Determining the Secondary Structure and Orientation of EmrE, a Multi-Drug Transporter, Indicates a Transmembrane Four-Helix Bundle
    • Arkin I.T., Russ W.P., Lebendiker M., Schuldiner S. Determining the Secondary Structure and Orientation of EmrE, a Multi-Drug Transporter, Indicates a Transmembrane Four-Helix Bundle. Biochemistry. 35:1996;7233-7238.
    • (1996) Biochemistry , vol.35 , pp. 7233-7238
    • Arkin, I.T.1    Russ, W.P.2    Lebendiker, M.3    Schuldiner, S.4


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