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Volumn 98, Issue 9, 2010, Pages 1864-1872

Order parameters of a transmembrane helix in a fluid bilayer: Case study of a WALP peptide

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EID: 77952257688     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.01.016     Document Type: Article
Times cited : (50)

References (56)
  • 1
    • 34548812858 scopus 로고    scopus 로고
    • Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy
    • DOI 10.1021/jp073652j
    • 1. Hong, M. 2007. Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy. J. Phys. Chem. B. 111:10340-10351. (Pubitemid 47441837)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.35 , pp. 10340-10351
    • Hong, M.1
  • 2
    • 33846963172 scopus 로고    scopus 로고
    • How protein transmembrane segments sense the lipid environment
    • Nyholm, T. K. M., S. Özdirekcan, and J. A. Killian. 2007. How protein transmembrane segments sense the lipid environment. Biochemistry. 46:1457-1465.
    • (2007) Biochemistry. , vol.46 , pp. 1457-1465
    • Nyholm, T.K.M.1    Özdirekcan, S.2    Killian, J.A.3
  • 3
    • 0028025665 scopus 로고
    • Solid-state NMR structural studies of peptides and proteins in membranes
    • Cross, T. A., and S. J. Opella. 1994. Solid-state NMR structural studies of peptides and proteins in membranes. Curr. Opin. Struct. Biol. 4:574-581.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 574-581
    • Cross, T.A.1    Opella, S.J.2
  • 4
    • 0032564387 scopus 로고    scopus 로고
    • Epidermal growth factor receptor transmembrane domain: 2H NMR implications for orientation and motion in a bilayer environment
    • Jones, D. H., K. R. Barber, C.W.Grant. 1998. Epidermal growth factor receptor transmembrane domain: 2H NMR implications for orientation and motion in a bilayer environment. Biochemistry. 37:16780-16787.
    • (1998) Biochemistry. , vol.37 , pp. 16780-16787
    • Jones, D.H.1    Barber, K.R.2    Grant, C.W.3
  • 6
    • 2942662220 scopus 로고    scopus 로고
    • Tilt angles of transmembrane model peptides in oriented and non-oriented lipid bilayers as determined by 2H solid-state NMR
    • Strandberg, E., S. Özdirekcan, J. A, Killian. 2004. Tilt angles of transmembrane model peptides in oriented and non-oriented lipid bilayers as determined by 2H solid-state NMR. Biophys. J. 86:3709-3721.
    • (2004) Biophys. J. , vol.86 , pp. 3709-3721
    • Strandberg, E.1    Özdirekcan, S.2    Killian, J.A.3
  • 7
    • 52449125325 scopus 로고    scopus 로고
    • Comparison of "Polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment
    • Vostrikov, V. V., C. V. Grant, R. E. Koeppe 2nd. 2008. Comparison of "Polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment. J. Am. Chem. Soc. 130:12584-12585.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12584-12585
    • Vostrikov, V.V.1    Grant, C.V.2    Koeppe II, R.E.3
  • 8
    • 0033597858 scopus 로고    scopus 로고
    • Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane α-helical peptides
    • de Planque, M. R. R., J. A. Kruijtzer, J. A. Killian. 1999. Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane α-helical peptides. J. Biol. Chem. 274:20839-20846.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20839-20846
    • De Planque, M.R.R.1    Kruijtzer, J.A.2    Killian, J.A.3
  • 9
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning a-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation, and extent of membrane incorporation
    • de Planque, M. R. R., E. Goormaghtigh, J. A. Killian. 2001. Sensitivity of single membrane-spanning a-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry. 40:5000-5010.
    • (2001) Biochemistry. , vol.40 , pp. 5000-5010
    • De Planque, M.R.R.1    Goormaghtigh, E.2    Killian, J.A.3
  • 10
    • 37349011230 scopus 로고    scopus 로고
    • The dynamic orientation of membrane-bound peptides: Bridging simulations and experiments
    • Esteban-Martín, S., and J. Salgado. 2007. The dynamic orientation of membrane-bound peptides: bridging simulations and experiments. Biophys. J. 93:4278-4288.
    • (2007) Biophys. J. , vol.93 , pp. 4278-4288
    • Esteban-Martín, S.1    Salgado, J.2
  • 11
    • 37049023237 scopus 로고    scopus 로고
    • On the orientation of a designed transmembrane peptide: Toward the right tilt angle?
    • Özdirekcan, S., C. Etchebest, P. F. Fuchs. 2007. On the orientation of a designed transmembrane peptide: toward the right tilt angle? J. Am. Chem. Soc. 129:15174-15181.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15174-15181
    • Özdirekcan, S.1    Etchebest, C.2    Fuchs, P.F.3
  • 12
    • 0038048507 scopus 로고    scopus 로고
    • Assessing the effects of time and spatial averaging in 15N chemical shift/15N-1H dipolar correlation solid state NMR experiments
    • Straus, S. K., W. R. Scott, and A. Watts. 2003. Assessing the effects of time and spatial averaging in 15N chemical shift/15N-1H dipolar correlation solid state NMR experiments. J. Biomol. NMR. 26:283-295.
    • (2003) J. Biomol. NMR. , vol.26 , pp. 283-295
    • Straus, S.K.1    Scott, W.R.2    Watts, A.3
  • 13
    • 67649405180 scopus 로고    scopus 로고
    • Orientation and dynamics of peptides in membranes calculated from 2H-NMR data
    • Strandberg, E., S. Esteban-Martín, A. S. Ulrich. 2009. Orientation and dynamics of peptides in membranes calculated from 2H-NMR data. Biophys. J. 96:3223-3232.
    • (2009) Biophys. J. , vol.96 , pp. 3223-3232
    • Strandberg, E.1    Esteban-Martín, S.2    Ulrich, A.S.3
  • 14
    • 0028330797 scopus 로고
    • Dynamics of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin
    • Prosser, R. S., and J. H. Davis. 1994. Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin. Biophys. J. 66:1429-1440.
    • (1994) Biophys. J. , vol.66 , pp. 1429-1440
    • Prosser, R.S.1    Davis, J.H.2
  • 15
    • 85004805818 scopus 로고
    • Rapid and efficient method for the preparation of Fmoc-amino acids starting from 9-fluorenylmethanol
    • ten Kortenaar, P. B. W., B. G. Vandijk, G. I. Tesser. 1986. Rapid and efficient method for the preparation of Fmoc-amino acids starting from 9-fluorenylmethanol. Int. J. Pept. Protein Res. 27:398-400.
    • (1986) Int. J. Pept. Protein Res. , vol.27 , pp. 398-400
    • Ten Kortenaar, P.B.W.1    Vandijk, B.G.2    Tesser, G.I.3
  • 16
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • Gullion, T., and J. Schaefer. 1989. Rotational-echo double-resonance NMR. J. Magn. Reson. 81:196-200.
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 17
    • 85011817347 scopus 로고
    • Detection of weak heteronuclear dipolar coupling by rotational-echo double-resonance nuclear magnetic resonance
    • Gullion, T., and J. Schaefer. 1989. Detection of weak heteronuclear dipolar coupling by rotational-echo double-resonance nuclear magnetic resonance. Adv. Magn. Reson. 13:57-83.
    • (1989) Adv. Magn. Reson. , vol.13 , pp. 57-83
    • Gullion, T.1    Schaefer, J.2
  • 19
    • 42649130559 scopus 로고
    • New, compensated Carr-Purcell sequences
    • Gullion, T., D. B. Baker, and M. S. Conradi. 1990. New, compensated Carr-Purcell sequences. J. Magn. Reson. 89:479-484.
    • (1990) J. Magn. Reson. , vol.89 , pp. 479-484
    • Gullion, T.1    Baker, D.B.2    Conradi, M.S.3
  • 20
    • 0038626673 scopus 로고    scopus 로고
    • Revision E.01, Gaussian, Inc., Wallingford, CT
    • Frisch, M. J, . J. A. Pople. 2004. Gaussian 03 Revision E.01, Gaussian, Inc., Wallingford, CT.
    • (2004) Gaussian 03
    • Frisch, J.M.1    Pople, J.A.2
  • 21
    • 84986527758 scopus 로고
    • IMOMM a new integrated ab-initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition-states
    • Maseras, F., and K. Morokuma. 1995. IMOMM a new integrated ab-initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition-states. J. Comput. Chem. 16:1170-1179.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1170-1179
    • Maseras, F.1    Morokuma, K.2
  • 22
    • 0041468782 scopus 로고    scopus 로고
    • On the application of the IMOMO (integrated molecular orbital plus molecular orbital) method
    • Vreven, T., and K. Morokuma. 2000. On the application of the IMOMO (integrated molecular orbital plus molecular orbital) method. J. Comput. Chem. 21:1419-1432.
    • (2000) J. Comput. Chem. , vol.21 , pp. 1419-1432
    • Vreven, T.1    Morokuma, K.2
  • 23
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. 3. the role of exact exchange
    • Becke, A. D. 1993. Density-functional thermochemistry. 3. The role of exact exchange. J. Chem. Phys. 98:5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 24
    • 0345491105 scopus 로고
    • Development of the ColleSalvetti correlation-energy formula into a functional of the electron density
    • Lee, C., W. Yang, and R. G. Parr. 1988. Development of the ColleSalvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B. 37:785-789.
    • (1988) Phys. Rev. B. , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 26
    • 33947094791 scopus 로고
    • MNDO parameters for third-period elements
    • Dewar, M. J. S., M. L. McKee, and S. Rzepa. 1978. MNDO parameters for third-period elements. J. Am. Chem. Soc: 100:3607.
    • (1978) J. Am. Chem. Soc , vol.100 , pp. 3607
    • Dewar, M.J.S.1    McKee, M.L.2    Rzepa, S.3
  • 27
    • 33847088641 scopus 로고
    • MINDO/3 study of addition of singlet oxygen δ-G-lo-2 to 1, 3-butadiene
    • Dewar, M.J.S., and W.Thiel. 1977. MINDO/3 study of addition of singlet oxygen δ-G-lo-2 to 1, 3-butadiene. J. Am. Chem. Soc. 99:2338-2339.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 2338-2339
    • Dewar, M.J.S.1    Thiel, W.2
  • 28
    • 84913536475 scopus 로고
    • Optimization and application of lithium parameters for PM3
    • Anders, E., R. Koch, and P. Freunscht. 1993. Optimization and application of lithium parameters for PM3. J. Comput. Chem. 14:1301-1312.
    • (1993) J. Comput. Chem. , vol.14 , pp. 1301-1312
    • Anders, E.1    Koch, R.2    Freunscht, P.3
  • 29
    • 84857628114 scopus 로고
    • Self-consistent perturbationtheory: Open-shell states in perturbation-dependent non-orthogonal basis-sets
    • Wolinski, K., and A. J. Sadlej. 1980. Self-consistent perturbationtheory: open-shell states in perturbation-dependent non-orthogonal basis-sets. Mol. Phys. 41:1419-1430.
    • (1980) Mol. Phys. , vol.41 , pp. 1419-1430
    • Wolinski, K.1    Sadlej, A.J.2
  • 30
    • 11744305193 scopus 로고
    • Efficient implementation of the gauge-independent atomic orbital, method for NMR chemicalshift calculations
    • Wolinski, K., J. F. Hinton, and P. Pulay. 1990. Efficient implementation of the gauge-independent atomic orbital, method for NMR chemicalshift calculations. J. Am. Chem. Soc. 112:8251-8260.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 8251-8260
    • Wolinski, K.1    Hinton, J.F.2    Pulay, P.3
  • 31
    • 40749094858 scopus 로고
    • Self-consistent perturbation theory of diamagnetism I. A gauge-invariant LCAO method for NMR chemical shifts
    • Ditchfield, R. 1974. Self-consistent perturbation theory of diamagnetism I. A gauge-invariant LCAO method for NMR chemical shifts. Mol. Phys. 27:789-807.
    • (1974) Mol. Phys. , vol.27 , pp. 789-807
    • Ditchfield, R.1
  • 32
    • 33750181960 scopus 로고
    • Perturbation theory for the Fock-Dirac density matrix
    • McWeeny, R. 1962. Perturbation theory for the Fock-Dirac density matrix. Phys. Rev. 126:1028-1034.
    • (1962) Phys. Rev. , vol.126 , pp. 1028-1034
    • McWeeny, R.1
  • 33
    • 0000719180 scopus 로고
    • Théorie quantique des courants interatomiques dans les combinaisons aromatiques
    • London, F. J. 1937. Théorie quantique des courants interatomiques dans les combinaisons aromatiques. J. Phys. Radium. 8:397-409.
    • (1937) J. Phys. Radium. , vol.8 , pp. 397-409
    • London, F.J.1
  • 35
    • 33744788872 scopus 로고    scopus 로고
    • GOSA, a simulated annealing-based program for global optimization of nonlinear problems, also reveals transyears
    • Czaplicki, J., G. Comélissen, and F. F. Halberg. 2006. GOSA, a simulated annealing-based program for global optimization of nonlinear problems, also reveals transyears. J. Appl. Biomed. 4:87-94.
    • (2006) J. Appl. Biomed. , vol.4 , pp. 87-94
    • Czaplicki, J.1    Comélissen, G.2    Halberg, F.F.3
  • 37
    • 18444371457 scopus 로고    scopus 로고
    • CUBA: A library for multidimensional numerical integration
    • Hahn, T. 2005. CUBA: a library for multidimensional numerical integration, Comput. Phys. Commun. 168:78-95.
    • (2005) Comput. Phys. Commun. , vol.168 , pp. 78-95
    • Hahn, T.1
  • 38
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
    • Killian., J. A., I. Salemink, D. V. Greathouse. 1996. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. 35:1037-1045.
    • (1996) Biochemistry. , vol.35 , pp. 1037-1045
    • Salemink, I.1    Greathouse, D.V.2
  • 39
    • 38349054743 scopus 로고    scopus 로고
    • Helical distortion in tryptophan- And lysine-anchored membrane-spanning α-helices as a function, of hydrophobic mismatch: A solid-state deuterium NMR investigation using the geometric analysis of labeled alanines method
    • Daily, A. E., D. V. Greathouse, R. E. Koeppe 2nd. 2008. Helical distortion in tryptophan- and lysine-anchored membrane-spanning α-helices as a function, of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines method. Biophys. J. 94:480-491.
    • (2008) Biophys. J. , vol.94 , pp. 480-491
    • Daily, A.E.1    Greathouse, D.V.2    Koeppe II, R.E.3
  • 41
    • 0037435555 scopus 로고    scopus 로고
    • Phospholipid flop induced by transmembrane peptides in model membranes is modulated by lipid composition
    • Kol, M. A., A. N. C. van Laak, B. de Kruijff. 2003. Phospholipid flop induced by transmembrane peptides in model membranes is modulated by lipid composition. Biochemistry. 42:231-237.
    • (2003) Biochemistry. , vol.42 , pp. 231-237
    • Kol, M.A.1    Van Laak, A.N.C.2    De Kruijff, B.3
  • 44
    • 0023261246 scopus 로고
    • Determination of the N-15 and C-13 chemical-shift tensors of L-C-13 alanyl-L- N-15 alanine from the dipole-coupled powder patterns
    • Hartzell, C. J., M. Whitfield, G. P. Drobny. 1987. Determination of the N-15 and C-13 chemical-shift tensors of L-C-13 alanyl-L- N-15 alanine from the dipole-coupled powder patterns. J. Am. Chem. Soc. 109:5966-5969.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5966-5969
    • Hartzell, C.J.1    Whitfield, M.2    Drobny, G.P.3
  • 45
    • 0013039776 scopus 로고    scopus 로고
    • NMR of peptides and proteins in oriented membranes
    • Marassi, F. M. 2002. NMR of peptides and proteins in oriented membranes. Concepts Magn. Reson. 14:212-224.
    • (2002) Concepts Magn. Reson. , vol.14 , pp. 212-224
    • Marassi, F.M.1
  • 46
    • 0001125152 scopus 로고
    • Simultaneous characterization of the amide H-1 chemical shift, H-1-N-15 dipolar, and N-15 chemical-shift interaction tensors in a peptide bond by 3-dimensional solid-state NMR spectroscopy
    • Wu, C. H., A. Ramamoorthy, S. J. Opella. 1995. Simultaneous characterization of the amide H-1 chemical shift, H-1-N-15 dipolar, and N-15 chemical-shift interaction tensors in a peptide bond by 3-dimensional solid-state NMR spectroscopy. J. Am. Chem. Soc. 117:6148-6149.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6148-6149
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 47
    • 34247847729 scopus 로고    scopus 로고
    • 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle
    • 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle. J. Am. Chem. Soc. 129:5719-5729.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5719-5729
    • Cady, S.D.1    Goodman, C.2    Hong, M.3
  • 49
    • 70449125771 scopus 로고    scopus 로고
    • Tilt and rotation angles of a transmembrane model peptide as studied by fluorescence spectroscopy
    • Holt, A., R. B. M. Koehorst, J. A. Killian. 2009. Tilt and rotation angles of a transmembrane model peptide as studied by fluorescence spectroscopy. Biophys. J. 97:2258-2266.
    • (2009) Biophys. J. , vol.97 , pp. 2258-2266
    • Holt, A.1    Koehorst, R.B.M.2    Killian, J.A.3
  • 50
    • 12344266698 scopus 로고    scopus 로고
    • Influence of flanking residues on tilt and rotation, angles of transmembrane peptides in lipid bilayers. A solid-state 2H NMR study
    • Özdirekcan, S., D. T. S. Rijkers, J. A. Killian. 2005. Influence of flanking residues on tilt and rotation, angles of transmembrane peptides in lipid bilayers. A solid-state 2H NMR study. Biochemistry. 44:1004-1012.
    • (2005) Biochemistry. , vol.44 , pp. 1004-1012
    • Özdirekcan, S.1    Rijkers, D.T.S.2    Killian, J.A.3
  • 51
    • 67650357429 scopus 로고    scopus 로고
    • Tilt and azimuthal angles of a transmembrane peptide: A comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes
    • Shi, L., A. Cembran, G. Veglia. 2009. Tilt and azimuthal angles of a transmembrane peptide: a comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes. Biophys. J. 96:3648-3662.
    • (2009) Biophys. J. , vol.96 , pp. 3648-3662
    • Shi, L.1    Cembran, A.2    Veglia, G.3
  • 52
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh, E., V. Raussens, and J. M. Ruysschaert. 1999. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta. 1422:105-185.
    • (1999) Biochim. Biophys. Acta. , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 53
    • 0026793754 scopus 로고
    • Deuterium NMR relaxation studies of peptide-lipid interactions
    • Prosser, R.S., J.H.Davis, G.Kothe. 1992. Deuterium NMR relaxation studies of peptide-lipid interactions. Biochemistry. 31:9355-9363.
    • (1992) Biochemistry. , vol.31 , pp. 9355-9363
    • Prosser, R.S.1    Davis, J.H.2    Kothe, G.3
  • 54
    • 0001977233 scopus 로고
    • Orientation-dependent deuteron, spin-lattice relaxation, times in bilayer membranes: Characterization, of the overall, lipid motion
    • Mayer, C., G. Grobner, G. Kothe. 1990. Orientation-dependent deuteron, spin-lattice relaxation, times in bilayer membranes: characterization, of the overall, lipid motion. Chem. Phys. Lett. 165:155-161.
    • (1990) Chem. Phys. Lett. , vol.165 , pp. 155-161
    • Mayer, C.1    Grobner, G.2    Kothe, G.3
  • 55
    • 77952093470 scopus 로고    scopus 로고
    • Orientation and dynamics of transmembrane peptides: The power of simple models
    • Holt, A., and J. A. Killian. 2010. Orientation and dynamics of transmembrane peptides: the power of simple models. Eur. Biophys. J. 39:209-621.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 209-621
    • Holt, A.1    Killian, J.A.2
  • 56
    • 21444450972 scopus 로고    scopus 로고
    • Magic angle spinning and static oriented sample NMR studies of the relaxation in the rotating frame of membrane peptides
    • Fares, C., J. Qian, and J. H. Davis. 2005. Magic angle spinning and static oriented sample NMR studies of the relaxation in the rotating frame of membrane peptides. J. Chem. Phys. 122:194908.
    • (2005) J. Chem. Phys. , vol.122 , pp. 194908
    • Fares, C.1    Qian, J.2    Davis, J.H.3


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