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Volumn 350, Issue 2, 2005, Pages 310-318

Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch

Author keywords

Hydrophobic mismatch; NMR; PISA wheels; PISEMA; Vpu

Indexed keywords

MEMBRANE PROTEIN; VPU PROTEIN;

EID: 20444366208     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.004     Document Type: Article
Times cited : (145)

References (41)
  • 1
    • 0021379727 scopus 로고
    • The structure of proteins in biological membranes
    • N. Unwin, and R. Henderson The structure of proteins in biological membranes Sci. Am. 250 1984 78 94
    • (1984) Sci. Am. , vol.250 , pp. 78-94
    • Unwin, N.1    Henderson, R.2
  • 2
    • 0024376113 scopus 로고
    • Topography of membrane proteins
    • M.L. Jennings Topography of membrane proteins Annu. Rev. Biochem. 58 1989 999 1027
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 999-1027
    • Jennings, M.L.1
  • 3
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane α-helices as automomous folding domains
    • J.L. Popot Integral membrane protein structure: transmembrane α-helices as automomous folding domains Curr. Opin. Struct. Biol. 3 1993 532 540
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 532-540
    • Popot, J.L.1
  • 4
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza a M2 protein channel: Structural implications from helix tilt and orientation
    • F.A. Kovacs, and T.A. Cross Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation Biophys. J. 73 1997 2511 2517
    • (1997) Biophys. J. , vol.73 , pp. 2511-2517
    • Kovacs, F.A.1    Cross, T.A.2
  • 6
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • S.H. White, and W.C. Wimley Hydrophobic interactions of peptides with membrane interfaces Biochim. Biophys. Acta. 1376 1998 339 352
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 7
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • J.A. Killian Hydrophobic mismatch between proteins and lipids in membranes Biochim. Biophys. Acta. 1376 1998 401 415
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 401-415
    • Killian, J.A.1
  • 8
    • 0026442901 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
    • Y.P. Zhang, R.N. Lewis, R.S. Hodges, and R.N. McElhaney Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetric and FTIR spectroscopic studies Biochemistry 31 1992 11579 11588
    • (1992) Biochemistry , vol.31 , pp. 11579-11588
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 10
    • 0033783447 scopus 로고    scopus 로고
    • 31P solid-state NMR spectroscopy investigation
    • 31P solid-state NMR spectroscopy investigation Biochemistry 39 2000 13106 13114
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 13
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • K.C. Duong-ly, V. Nanda, W.F. Degrado, and K.P. Howard The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment Protein Sci. 14 2005 856 861
    • (2005) Protein Sci. , vol.14 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    Degrado, W.F.3    Howard, K.P.4
  • 14
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza a virus: An intrinsic property
    • F.A. Kovacs, J.F. Denny, Z. Song, J.R. Quine, and J.A. Cross Helix tilt of the M2 transmembrane peptide from influenza A virus: An intrinsic property J. Mol. Biol. 295 2000 117 125
    • (2000) J. Mol. Biol. , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.F.2    Song, Z.3    Quine, J.R.4    Cross, J.A.5
  • 15
    • 4444343863 scopus 로고    scopus 로고
    • Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy
    • R.B.M. Koehorst, R.B. Spruijt, F.J. Vergeldt, and M.A. Hemminga Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy Biophy. J. 87 2004 1445 1455
    • (2004) Biophy. J. , vol.87 , pp. 1445-1455
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Vergeldt, F.J.3    Hemminga, M.A.4
  • 17
    • 0036181837 scopus 로고    scopus 로고
    • Expression, purification, and activities of full-length and truncated versions of the integral membrane protein Vpu from HIV-1
    • C. Ma, F.M. Marassi, D.H. Jones, S.K. Straus, S. Bour, and K. Strebel Expression, purification, and activities of full-length and truncated versions of the integral membrane protein Vpu from HIV-1 Protein Sci. 11 2002 546 557
    • (2002) Protein Sci. , vol.11 , pp. 546-557
    • Ma, C.1    Marassi, F.M.2    Jones, D.H.3    Straus, S.K.4    Bour, S.5    Strebel, K.6
  • 18
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1 infected cells
    • U. Schubert, A.V. Ferrer-Montiel, M. Oblatt-Montal, P. Henklein, K. Strebel, and M. Montal Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1 infected cells FEBS Letters 398 1996 12 18
    • (1996) FEBS Letters , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 19
    • 0141645622 scopus 로고    scopus 로고
    • Three-dimonsional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1
    • S.H. Park, A.A. Mrse, A.A. Nevzorov, M.F. Mesleh, M. Oblatt-Montal, M. Montal, and S.J. Opella Three-dimonsional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1 J. Mol. Biol. 333 2003 409 424
    • (2003) J. Mol. Biol. , vol.333 , pp. 409-424
    • Park, S.H.1    Mrse, A.A.2    Nevzorov, A.A.3    Mesleh, M.F.4    Oblatt-Montal, M.5    Montal, M.6    Opella, S.J.7
  • 21
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • S.J. Opella, and F.M. Marassi Structure determination of membrane proteins by NMR spectroscopy Chem. Rev. 104 2004 3587 3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 22
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • F.M. Marassi, and S.J. Opella A solid-state NMR index of helical membrane protein structure and topology J. Magn. Reson. 144 2000 150 155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 26
    • 0042029753 scopus 로고    scopus 로고
    • Dipolar waves as NMR maps of helices in proteins
    • M.F. Mesleh, and S.J. Opella Dipolar waves as NMR maps of helices in proteins J. Magn. Reson. 163 2003 288 299
    • (2003) J. Magn. Reson. , vol.163 , pp. 288-299
    • Mesleh, M.F.1    Opella, S.J.2
  • 28
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • F.M. Marassi, and S.J. Opella Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints Protein Sci. 12 2003 403 411
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 29
    • 0036361158 scopus 로고    scopus 로고
    • Using pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins
    • F.M. Marassi, and S.J. Opella Using pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins J. Biomol. NMR 23 2002 239 242
    • (2002) J. Biomol. NMR , vol.23 , pp. 239-242
    • Marassi, F.M.1    Opella, S.J.2
  • 31
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron diffraction data III. Complete structure
    • M.C. Wiener, and S.H. White Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron diffraction data III. Complete structure Biophys. J. 61 1992 437 447
    • (1992) Biophys. J. , vol.61 , pp. 437-447
    • Wiener, M.C.1    White, S.H.2
  • 32
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • B.A. Lewis, and D.M. Engelman Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles J. Mol. Biol. 166 1983 211 217
    • (1983) J. Mol. Biol. , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 33
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • O.G. Mouritsen, and M. Bloom Mattress model of lipid-protein interactions in membranes Biophys. J. 46 1984 141 153
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 34
    • 0032988823 scopus 로고    scopus 로고
    • Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin
    • T.A. Harroun, W.T. Heller, T.M. Weiss, L. Yang, and H.W. Huang Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin Biophys. J. 76 1999 937 945
    • (1999) Biophys. J. , vol.76 , pp. 937-945
    • Harroun, T.A.1    Heller, W.T.2    Weiss, T.M.3    Yang, L.4    Huang, H.W.5
  • 35
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
    • J.A. Killian, I. Salemink, M.R. de Planque, G. Lindblom, R.E. Koeppe II, and D.V. Greathouse Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans Biochemistry 35 1996 1037 1045
    • (1996) Biochemistry , vol.35 , pp. 1037-1045
    • Killian, J.A.1    Salemink, I.2    De Planque, M.R.3    Lindblom, G.4    Koeppe II, R.E.5    Greathouse, D.V.6
  • 36
    • 0026795003 scopus 로고
    • Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance
    • N.J.P. Ryba, and D. Marsh Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance Biochemistry 31 1992 7511 7518
    • (1992) Biochemistry , vol.31 , pp. 7511-7518
    • Ryba, N.J.P.1    Marsh, D.2
  • 37
    • 0027362726 scopus 로고
    • A molecular model for lipid-protein interaction in membranes: The role of hydrophobic mismatch
    • D.R. Fattal, and A. Ben-Shaul A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch Biophys. J. 65 1993 1795 1809
    • (1993) Biophys. J. , vol.65 , pp. 1795-1809
    • Fattal, D.R.1    Ben-Shaul, A.2
  • 38
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: The case of the calcium pump
    • A.G. Lee How lipids interact with an intrinsic membrane protein: the case of the calcium pump Biochim. Biohpys. Acta 1367 1998 381 390
    • (1998) Biochim. Biohpys. Acta , vol.1367 , pp. 381-390
    • Lee, A.G.1
  • 39
    • 0034712674 scopus 로고    scopus 로고
    • Consequences of hydrophobic mismatch between lipids and melibiose permease on melibiose transport
    • F. Dumas, J.F. Tocanne, G. Leblanc, and M.C. Lebrun Consequences of hydrophobic mismatch between lipids and melibiose permease on melibiose transport Biochemistry 39 2000 4846 4854
    • (2000) Biochemistry , vol.39 , pp. 4846-4854
    • Dumas, F.1    Tocanne, J.F.2    Leblanc, G.3    Lebrun, M.C.4
  • 40
    • 0035902530 scopus 로고    scopus 로고
    • Effects of bilayer thickness on the activity of diacylglycerol kinase of Escherichia coli
    • J.D. Pilot, J.M. East, and A.G. Lee Effects of bilayer thickness on the activity of diacylglycerol kinase of Escherichia coli Biochemistry 40 2001 8188 8195
    • (2001) Biochemistry , vol.40 , pp. 8188-8195
    • Pilot, J.D.1    East, J.M.2    Lee, A.G.3
  • 41
    • 33846595904 scopus 로고
    • High resolution heteronuclear dipolar solid-state NMR spectroscopy
    • C.H. Wu, A. Ramamoorthy, and S.J. Opella High resolution heteronuclear dipolar solid-state NMR spectroscopy J. Magn. Reson. ser. A 109 1994 270 272
    • (1994) J. Magn. Reson. Ser. a , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3


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