메뉴 건너뛰기




Volumn 1808, Issue 3, 2011, Pages 784-791

Structure and dynamics of the lipid modifications of a transmembrane α-helical peptide determined by 2H solid-state NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; ACYLLYSYLLYSYLLYSYLTRYPTOPHYLLEUCYLVALYLLEUCYLVALYLLEUCYLVALYLLEUCYLVALYLLEUCYLVALYLLEUCYLVALYLLEUCYLVALYLLEUCYLVALYLLYSYLLYSYLLYSINE; AMPHOLYTE; DILAUROYLPHOSPHATIDYLCHOLINE; PEPTIDE; PHOSPHORYLCHOLINE; UNCLASSIFIED DRUG;

EID: 78651252937     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.12.015     Document Type: Article
Times cited : (14)

References (57)
  • 2
    • 34247169946 scopus 로고    scopus 로고
    • The role of transmembrane domains in membrane fusion
    • DOI 10.1007/s00018-007-6439-x
    • D. Langosch, M. Hofmann, and C. Ungermann The role of transmembrane domains in membrane fusion Cell Mol. Life Sci. 64 2007 850 864 (Pubitemid 46597757)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.7-8 , pp. 850-864
    • Langosch, D.1    Hofmann, M.2    Ungermann, C.3
  • 3
    • 34547128385 scopus 로고    scopus 로고
    • Mode of membrane interaction and fusogenic properties of a de novo transmembrane model peptide depend on the length of the hydrophobic core
    • DOI 10.1074/jbc.M700099200
    • A. Lorin, B. Charloteaux, Y. Fridmann-Sirkis, A. Thomas, Y. Shai, and R. Brasseur Mode of membrane interaction and fusogenic properties of a de novo transmembrane model peptide depend on the length of the hydrophobic core J. Biol. Chem. 282 2007 18388 18396 (Pubitemid 47100240)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18388-18396
    • Lorin, A.1    Charloteaux, B.2    Fridmann-Sirkis, Y.3    Thomas, A.4    Shai, Y.5    Brasseur, R.6
  • 5
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • DOI 10.1073/pnas.95.7.3425
    • D.Z. Cleverley, and J. Lenard The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein Proc. Natl. Acad. Sci. U. S. A. 95 1998 3425 3430 (Pubitemid 28173144)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.7 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 6
    • 0035943407 scopus 로고    scopus 로고
    • Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity
    • DOI 10.1006/jmbi.2001.4889
    • D. Langosch, J.M. Crane, B. Brosig, A. Hellwig, L.K. Tamm, and J. Reed Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity J. Mol. Biol. 311 2001 709 721 (Pubitemid 32803730)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.4 , pp. 709-721
    • Langosch, D.1    Crane, J.M.2    Brosig, B.3    Hellwig, A.4    Tamm, L.K.5    Reed, J.6
  • 8
    • 34047197811 scopus 로고    scopus 로고
    • pH-activated fusogenic transmembrane LV-peptides
    • DOI 10.1021/bi602539n
    • M.W. Hofmann, B.C. Poschner, S. Hauser, and D. Langosch pH-Activated fusogenic transmembrane LV-peptides Biochemistry 46 2007 4204 4209 (Pubitemid 46536081)
    • (2007) Biochemistry , vol.46 , Issue.13 , pp. 4204-4209
    • Hofmann, M.W.1    Poschner, B.C.2    Hauser, S.3    Langosch, D.4
  • 10
    • 0029042360 scopus 로고
    • Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate
    • A. Couve, V. Protopopov, and J.E. Gerst Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate Proc. Natl. Acad. Sci. U. S. A. 92 1995 5987 5991
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5987-5991
    • Couve, A.1    Protopopov, V.2    Gerst, J.E.3
  • 11
    • 23044444831 scopus 로고    scopus 로고
    • Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation
    • DOI 10.1038/sj.emboj.7600724
    • J. Valdez-Taubas, and H. Pelham Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation EMBO J. 24 2005 2524 2532 (Pubitemid 41076309)
    • (2005) EMBO Journal , vol.24 , Issue.14 , pp. 2524-2532
    • Valdez-Taubas, J.1    Pelham, H.2
  • 12
    • 58149197889 scopus 로고    scopus 로고
    • Membrane binding of lipidated Ras peptides and proteins-the structural point of view
    • L. Brunsveld, H. Waldmann, and D. Huster Membrane binding of lipidated Ras peptides and proteins-the structural point of view Biochim. Biophys. Acta 1788 2009 273 288
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 273-288
    • Brunsveld, L.1    Waldmann, H.2    Huster, D.3
  • 13
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • DOI 10.1021/bi00090a020
    • R.M. Peitzsch, and S. McLaughlin Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins Biochemistry 32 1993 10436 10443 (Pubitemid 23320168)
    • (1993) Biochemistry , vol.32 , Issue.39 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 14
    • 0028968896 scopus 로고
    • Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes
    • S. Shahinian, and J.R. Silvius Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes Biochemistry 34 1995 3813 3822
    • (1995) Biochemistry , vol.34 , pp. 3813-3822
    • Shahinian, S.1    Silvius, J.R.2
  • 15
    • 77952395696 scopus 로고    scopus 로고
    • Solvent-exposed tails as prestalk transition states for membrane fusion at low hydration
    • Y.G. Smirnova, S.J. Marrink, R. Lipowsky, and V. Knecht Solvent-exposed tails as prestalk transition states for membrane fusion at low hydration J. Am. Chem. Soc. 132 2010 6710 6718
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6710-6718
    • Smirnova, Y.G.1    Marrink, S.J.2    Lipowsky, R.3    Knecht, V.4
  • 16
    • 0001726193 scopus 로고    scopus 로고
    • Investigation of lipid organization in biological membranes by two-dimensional nuclear overhauser enhancement spectroscopy
    • D. Huster, K. Arnold, and K. Gawrisch Investigation of lipid organization in biological membranes by two-dimensional nuclear Overhauser enhancement spectroscopy J. Phys. Chem. B 103 1999 243 251 (Pubitemid 129680317)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.1 , pp. 243-251
    • Huster, D.1    Arnold, K.2    Gawrisch, K.3
  • 17
    • 0033541114 scopus 로고    scopus 로고
    • NOESY NMR crosspeaks between lipid headgroups and hydrocarbon chains: Spin diffusion or molecular disorder? [20]
    • DOI 10.1021/ja9838413
    • D. Huster, and K. Gawrisch NOESY NMR crosspeaks between lipid headgroups and hydrocarbon chains: spin diffusion or molecular disorder? J. Am. Chem. Soc. 121 1999 1992 1993 (Pubitemid 29132073)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.9 , pp. 1992-1993
    • Huster, D.1    Gawrisch, K.2
  • 18
    • 72049094534 scopus 로고    scopus 로고
    • Structural features of fusogenic model transmembrane domains that differentially regulate inner and outer leaflet mixing in membrane fusion
    • B.C. Poschner, K. Fischer, J.R. Herrmann, M.W. Hofmann, and D. Langosch Structural features of fusogenic model transmembrane domains that differentially regulate inner and outer leaflet mixing in membrane fusion Mol. Membr. Biol. 27 2010 1 11
    • (2010) Mol. Membr. Biol. , vol.27 , pp. 1-11
    • Poschner, B.C.1    Fischer, K.2    Herrmann, J.R.3    Hofmann, M.W.4    Langosch, D.5
  • 19
    • 67749120313 scopus 로고    scopus 로고
    • Stabilization of conformationally dynamic helices by covalently attached acyl chains
    • B.C. Poschner, and D. Langosch Stabilization of conformationally dynamic helices by covalently attached acyl chains Protein Sci. 18 2009 1801 1805
    • (2009) Protein Sci. , vol.18 , pp. 1801-1805
    • Poschner, B.C.1    Langosch, D.2
  • 20
    • 0036229532 scopus 로고    scopus 로고
    • Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation
    • DOI 10.1128/JVI.76.9.4603-4611.2002
    • T. Sakai, R. Ohuchi, and M. Ohuchi Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation J. Virol. 76 2002 4603 4611 (Pubitemid 34309595)
    • (2002) Journal of Virology , vol.76 , Issue.9 , pp. 4603-4611
    • Sakai, T.1    Ohuchi, R.2    Ohuchi, M.3
  • 21
    • 18144395402 scopus 로고    scopus 로고
    • Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity
    • DOI 10.1128/JVI.79.10.6449-6458.2005
    • R. Wagner, A. Herwig, N. Azzouz, and H.D. Klenk Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity J. Virol. 79 2005 6449 6458 (Pubitemid 40617248)
    • (2005) Journal of Virology , vol.79 , Issue.10 , pp. 6449-6458
    • Wagner, R.1    Herwig, A.2    Azzouz, N.3    Klenk, H.D.4
  • 22
    • 0032169620 scopus 로고    scopus 로고
    • Acylation of the influenza hemagglutinin modulates fusion activity
    • DOI 10.1006/viro.1998.9286
    • C. Fischer, B. Schroth-Diez, A. Herrmann, W. Garten, and H.D. Klenk Acylation of the influenza hemagglutinin modulates fusion activity Virology 248 1998 284 294 (Pubitemid 28417715)
    • (1998) Virology , vol.248 , Issue.2 , pp. 284-294
    • Fischer, C.1    Schroth-Diez, B.2    Herrmann, A.3    Garten, W.4    Klenk, H.-D.5
  • 23
    • 0030848463 scopus 로고    scopus 로고
    • The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores
    • DOI 10.1006/viro.1997.8686
    • G.B. Melikyan, H. Jin, R.A. Lamb, and F.S. Cohen The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores Virology 235 1997 118 128 (Pubitemid 27380812)
    • (1997) Virology , vol.235 , Issue.1 , pp. 118-128
    • Melikyan, G.B.1    Jin, H.2    Lamb, R.A.3    Cohen, F.S.4
  • 24
    • 0032516482 scopus 로고    scopus 로고
    • Chain length and temperature dependence of the reversible association of model acylated proteins with lipid bilayers
    • DOI 10.1021/bi980385m
    • C.T. Pool, and T.E. Thompson Chain length and temperature dependence of the reversible association of model acylated proteins with lipid bilayers Biochemistry 37 1998 10246 10255 (Pubitemid 28366381)
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 10246-10255
    • Pool, C.T.1    Thompson, T.E.2
  • 29
    • 0018510430 scopus 로고
    • Deuterium magnetic resonance study of the gel and liquid crystalline phases of dipalmitoyl phosphocholine
    • J.H. Davis Deuterium magnetic resonance study of the gel and liquid crystalline phases of dipalmitoyl phosphocholine Biophys. J. 27 1979 339 358
    • (1979) Biophys. J. , vol.27 , pp. 339-358
    • Davis, J.H.1
  • 30
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: Theory and application to lipid membranes
    • J. Seelig Deuterium magnetic resonance: theory and application to lipid membranes Q. Rev. Biophys. 10 1977 353 418 (Pubitemid 8203096)
    • (1977) Quarterly Reviews of Biophysics , vol.10 , Issue.3 , pp. 353-418
    • Seelig, J.1
  • 33
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • J.H. Davis, K.R. Jeffrey, M. Bloom, M.I. Valic, and T.P. Higgs Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains Chem. Phys. Lett. 42 1976 390 394
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 35
    • 0037116518 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids in lipid bilayers: Intrinsic and environmental contributions to their unique physical properties
    • DOI 10.1021/ja0118340
    • S.E. Feller, K. Gawrisch, and A.D. MacKerell Jr. Polyunsaturated fatty acids in lipid bilayers: intrinsic and environmental contributions to their unique physical properties J. Am. Chem. Soc. 124 2002 318 326 (Pubitemid 34062762)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.2 , pp. 318-326
    • Feller, S.E.1    Gawrisch, K.2    MacKerell Jr., A.D.3
  • 36
    • 36849092841 scopus 로고    scopus 로고
    • 2H solid-state NMR spectroscopy
    • DOI 10.1016/j.bbamem.2007.08.024, PII S0005273607003355
    • A. Vogel, T. Schroder, C. Lange, and D. Huster Characterization of the myristoyl lipid modification of membrane-bound GCAP-2 by H-2 solid-state NMR spectroscopy Biochim. Biophys. Acta 1768 2007 3171 3181 (Pubitemid 350236086)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.12 , pp. 3171-3181
    • Vogel, A.1    Schroder, T.2    Lange, C.3    Huster, D.4
  • 37
    • 74249107842 scopus 로고    scopus 로고
    • A solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate cyclase-activating protein-2
    • S. Theisgen, H.A. Scheidt, A. Magalhaes, T.J. Bonagamba, and D. Huster A solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate cyclase-activating protein-2 Biochim. Biophys. Acta. 1798 2010 266 274
    • (2010) Biochim. Biophys. Acta. , vol.1798 , pp. 266-274
    • Theisgen, S.1    Scheidt, H.A.2    Magalhaes, A.3    Bonagamba, T.J.4    Huster, D.5
  • 38
    • 0033615312 scopus 로고    scopus 로고
    • Interpretation of NOESY cross-relaxation rates from molecular dynamics simulation of a lipid bilayer [12]
    • DOI 10.1021/ja991456n
    • S.E. Feller, D. Huster, and K. Gawrisch Interpretation of NOESY cross-relaxation rates from molecular dynamics simulations of a lipid bilayer J. Am. Chem. Soc. 121 1999 8963 8964 (Pubitemid 29461555)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.38 , pp. 8963-8964
    • Feller, S.E.1    Huster, D.2    Gawrisch, K.3
  • 39
    • 0001137403 scopus 로고
    • Angular dependence of deuterium spin-lattice relaxation rates of macroscopically oriented dilauroylphosphatidylcholine in the liquid-crystalline state
    • T.P. Trouard, T.M. Alam, and M.F. Brown Angular dependence of deuterium spin-lattice relaxation rates of macroscopically oriented dilauroylphosphatidylcholine in the liquid-crystalline state J. Chem. Phys. 101 1994 5229 5261
    • (1994) J. Chem. Phys. , vol.101 , pp. 5229-5261
    • Trouard, T.P.1    Alam, T.M.2    Brown, M.F.3
  • 40
    • 0000934428 scopus 로고
    • 14N quadrupolar relaxation
    • 14N quadrupolar relaxation J. Chem. Phys. 77 1982 1576 1799
    • (1982) J. Chem. Phys. , vol.77 , pp. 1576-1799
    • Brown, M.F.1
  • 47
    • 0000702940 scopus 로고
    • Configurational statistics of acyl chains in polyunsaturated lipid bilayers from deuterium NMR
    • A. Salmon, S.W. Dodd, G.D. Williams, J.M. Beach, and M.F. Brown Configurational statistics of acyl chains in polyunsaturated lipid bilayers from deuterium NMR J. Am. Chem. Soc. 109 1987 2600 2609
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2600-2609
    • Salmon, A.1    Dodd, S.W.2    Williams, G.D.3    Beach, J.M.4    Brown, M.F.5
  • 48
    • 9344238828 scopus 로고    scopus 로고
    • Membrane localization and flexibility of a lipidated ras peptide studied by molecular dynamics simulations
    • DOI 10.1021/ja046607n
    • A.A. Gorfe, R. Pellarin, and A. Caflisch Membrane localization and flexibility of a lipidated ras peptide studied by molecular dynamics simulations J. Am. Chem. Soc. 126 2004 15277 15286 (Pubitemid 39557285)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.46 , pp. 15277-15286
    • Gorfe, A.A.1    Pellarin, R.2    Caflisch, A.3
  • 49
    • 0041320842 scopus 로고    scopus 로고
    • The distribution of lipid attached spin probes in bilayers: Application to membrane protein topology
    • A. Vogel, H.A. Scheidt, and D. Huster The distribution of lipid attached EPR probes in bilayers. Application to membrane protein topology Biophys. J. 85 2003 1691 1701 (Pubitemid 37052252)
    • (2003) Biophysical Journal , vol.85 , Issue.3 , pp. 1691-1701
    • Vogel, A.1    Scheidt, H.A.2    Huster, D.3
  • 50
  • 51
    • 0028285033 scopus 로고
    • Structure and dynamics of the acyl chain of a transmembrane polypeptide
    • T.C. Vogt, J.A. Killian, and B. de Kruijff Structure and dynamics of the acyl chain of a transmembrane polypeptide Biochemistry 33 1994 2063 2070 (Pubitemid 24099601)
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2063-2070
    • Vogt, T.C.B.1    Killian, J.A.2    De Kruijff, B.3
  • 53
    • 0028929692 scopus 로고
    • Restatement of order parameters in biomembranes-calculation of C-C bond order parameters from C-D quadrupolar splittings
    • J.P. Douliez, A. Leonard, and E.J. Dufourc Restatement of order parameters in biomembranes-calculation of C-C bond order parameters from C-D quadrupolar splittings Biophys. J. 68 1995 1727 1739
    • (1995) Biophys. J. , vol.68 , pp. 1727-1739
    • Douliez, J.P.1    Leonard, A.2    Dufourc, E.J.3
  • 54
    • 0028988796 scopus 로고
    • 2H nuclear magnetic resonance order parameter profiles suggest a change of molecular shape for phosphatidylcholines containing a polyunsaturated acyl chain
    • 2H nuclear magnetic resonance order parameter profiles suggest a change of molecular shape for phosphatidylcholines containing a polyunsaturated acyl chain Biophys. J. 68 1995 2396 2403
    • (1995) Biophys. J. , vol.68 , pp. 2396-2403
    • Holte, L.L.1    Peter, S.A.2    Sinnwell, T.M.3    Gawrisch, K.4
  • 56
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • DOI 10.1038/42408
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572 (Pubitemid 27248754)
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 57
    • 0029981549 scopus 로고    scopus 로고
    • Nuclear magnetic resonance investigations of hydrocarbon chain packing in bilayers of polyunsaturated phospholipids
    • L.L. Holte, F. Separovic, and K. Gawrisch Nuclear magnetic resonance investigations of hydrocarbon chain packing in bilayers of polyunsaturated phospholipids Lipids 31 1996 S-199-S-203.
    • (1996) Lipids , vol.31
    • Holte, L.L.1    Separovic, F.2    Gawrisch, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.