메뉴 건너뛰기




Volumn 90, Issue 5, 2006, Pages 1650-1660

Evaluating tilt angles of membrane-associated helices: Comparison of computational and NMR techniques

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 33646138957     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.065367     Document Type: Article
Times cited : (51)

References (82)
  • 1
    • 0242696086 scopus 로고    scopus 로고
    • Membrane protein simulation: Ion channels and bacterial outer membrane proteins
    • Domene, C., P. J. Bond, and M. S. P. Sansom. 2003. Membrane protein simulation: ion channels and bacterial outer membrane proteins. Adv. Protein Chem. 66:159-193.
    • (2003) Adv. Protein Chem. , vol.66 , pp. 159-193
    • Domene, C.1    Bond, P.J.2    Sansom, M.S.P.3
  • 3
    • 0033066284 scopus 로고    scopus 로고
    • Interactions of alpha-helices with lipid bilayers: A review of simulation studies
    • Biggin, P. C., and M. S. P. Sansom. 1999. Interactions of alpha-helices with lipid bilayers: a review of simulation studies. Biophys. Chem. 76:161-183.
    • (1999) Biophys. Chem. , vol.76 , pp. 161-183
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 4
    • 0032032107 scopus 로고    scopus 로고
    • IMPALA: A simple restraint field to simulate the biological membrane in molecular structure studies
    • Ducarme, P., M. Rahman, and R. Brasseur. 1998. IMPALA: a simple restraint field to simulate the biological membrane in molecular structure studies. Proteins. 30:357-371.
    • (1998) Proteins , vol.30 , pp. 357-371
    • Ducarme, P.1    Rahman, M.2    Brasseur, R.3
  • 5
    • 0038675609 scopus 로고    scopus 로고
    • Effective energy function for proteins in lipid membranes
    • Lazaridis, T. 2003. Effective energy function for proteins in lipid membranes. Proteins. 52:176-192.
    • (2003) Proteins , vol.52 , pp. 176-192
    • Lazaridis, T.1
  • 6
    • 0036218972 scopus 로고    scopus 로고
    • A Monte Carlo study of peptide insertion into lipid bilayers: Equilibrium conformations and insertion mechanisms
    • Maddox, M. W., and M. L. Longo. 2002. A Monte Carlo study of peptide insertion into lipid bilayers: equilibrium conformations and insertion mechanisms. Biophys. J. 82:244-263.
    • (2002) Biophys. J. , vol.82 , pp. 244-263
    • Maddox, M.W.1    Longo, M.L.2
  • 7
    • 0037194983 scopus 로고    scopus 로고
    • Introducing an implicit membrane in generalized Born/solvent accessibility continuum solvent models
    • Spassov, V. Z., L. Yan, and S. Szalma. 2002. Introducing an implicit membrane in generalized Born/solvent accessibility continuum solvent models. J. Phys. Chem. B. 106:8726-8738.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 8726-8738
    • Spassov, V.Z.1    Yan, L.2    Szalma, S.3
  • 8
    • 0242322528 scopus 로고    scopus 로고
    • An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins
    • Im, W., M. Feig, and C. L. Brooks III. 2003. An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins. Biophys. J. 85:2900-2918.
    • (2003) Biophys. J. , vol.85 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks III, C.L.3
  • 9
    • 0035215186 scopus 로고    scopus 로고
    • Prediction of membrane protein orientation in lipid bilayers: A theoretical approach
    • Basyn, F., B. Charloteaux, A. Thomas, and R. Brasseur. 2001. Prediction of membrane protein orientation in lipid bilayers: a theoretical approach. J. Mol. Graph. 20:235-244.
    • (2001) J. Mol. Graph. , vol.20 , pp. 235-244
    • Basyn, F.1    Charloteaux, B.2    Thomas, A.3    Brasseur, R.4
  • 11
    • 13944255096 scopus 로고    scopus 로고
    • Understanding the energetics of helical peptide orientation in membranes
    • Sengupta, D., L. Meinhold, D. Langosch, G. M. Ullmann, and J. C. Smith. 2005. Understanding the energetics of helical peptide orientation in membranes. Proteins. 58:913-922.
    • (2005) Proteins , vol.58 , pp. 913-922
    • Sengupta, D.1    Meinhold, L.2    Langosch, D.3    Ullmann, G.M.4    Smith, J.C.5
  • 12
    • 1542358793 scopus 로고    scopus 로고
    • De novo folding of membrane proteins: An exploration of the structure and NMR properties of the FD coat protein
    • Im, W., and C. L. Brooks III. 2004. De novo folding of membrane proteins: an exploration of the structure and NMR properties of the FD coat protein. J. Mol. Biol. 337:513-519.
    • (2004) J. Mol. Biol. , vol.337 , pp. 513-519
    • Im, W.1    Brooks III, C.L.2
  • 13
    • 0034031680 scopus 로고    scopus 로고
    • Effective energy functions for protein structure prediction
    • Lazaridis, T., and M. Karplus. 2000. Effective energy functions for protein structure prediction. Curr. Opin. Struct. Biol. 10:139-145.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 139-145
    • Lazaridis, T.1    Karplus, M.2
  • 14
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., R. Casadio, P. Fariselli, and C. Sander. 1995. Transmembrane helices predicted at 95% accuracy. Protein Sci. 4:521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 15
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost, B., P. Fariselli, and R. Casadio. 1996. Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci. 5:1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 16
    • 0035812599 scopus 로고    scopus 로고
    • Energetics, stability, and prediction of transmembrane helices
    • Jayasinghe, S., K. Hristova, and S. H. White. 2001. Energetics, stability, and prediction of transmembrane helices. J. Mol. Biol. 312:927-934.
    • (2001) J. Mol. Biol. , vol.312 , pp. 927-934
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 17
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: Derivation of an implicit membrane potential
    • Ulmschneider, M. B., M. S. P. Sansom, and A. Di Nola. 2005. Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins. 59:252-265.
    • (2005) Proteins , vol.59 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.P.2    Di Nola, A.3
  • 18
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force - An approach to the knowledge-based prediction of local structures in globular-proteins
    • Sippl, M. J. 1990. Calculation of conformational ensembles from potentials of mean force - an approach to the knowledge-based prediction of local structures in globular-proteins. J. Mol. Biol. 213:859-883.
    • (1990) J. Mol. Biol. , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 19
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl, M. J. 1995. Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5:229-235.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 20
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and D. M. Engelman. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69:881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 22
    • 0344236133 scopus 로고    scopus 로고
    • Lipid/protein interactions and the membrane/water interfacial region
    • Domene, C., P. J. Bond, S. S. Deol, and M. S. Sansom. 2003. Lipid/protein interactions and the membrane/water interfacial region. J. Am. Chem. Soc. 125:14966-14967.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14966-14967
    • Domene, C.1    Bond, P.J.2    Deol, S.S.3    Sansom, M.S.4
  • 23
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 25
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella, S. J., and F. M. Marassi. 2004. Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104:3587-3606.
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 26
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem, R. R., W. Hu, and T. A. Cross. 1993. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science. 261:1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 27
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channellining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S. J., F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, and M. Montal. 1999. Structures of the M2 channellining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6:374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 28
    • 0034775070 scopus 로고    scopus 로고
    • Structure of the transmembrane region of the M2 protein H(+) channel
    • Wang, J., S. Kim, F. Kovacs, and T. A. Cross. 2001. Structure of the transmembrane region of the M2 protein H(+) channel. Protein Sci. 10:2241-2250.
    • (2001) Protein Sci. , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 29
    • 0035813019 scopus 로고    scopus 로고
    • Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers
    • Valentine, K. G., S. F. Liu, F. M. Marassi, G. Veglia, S. J. Opella, F. X. Ding, S. H. Wang, B. Arshava, J. M. Becker, and F. Naider. 2001. Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers. Biopolymers. 59:243-256.
    • (2001) Biopolymers , vol.59 , pp. 243-256
    • Valentine, K.G.1    Liu, S.F.2    Marassi, F.M.3    Veglia, G.4    Opella, S.J.5    Ding, F.X.6    Wang, S.H.7    Arshava, B.8    Becker, J.M.9    Naider, F.10
  • 30
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi, F. M., and S. J. Opella. 2003. Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci. 12:403-411.
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 31
    • 0141645622 scopus 로고    scopus 로고
    • Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1
    • Park, S. H., A. A. Mrse, A. A. Nevzorov, M. F. Mesleh, M. Oblatt-Montal, M. Montal, and S. J. Opella. 2003. Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1. J. Mol. Biol. 333:409-424.
    • (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
  • 32
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • Steiner, H., D. Andreu, and R. B. Merrifield. 1988. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta. 939:260-266.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 33
    • 0029398795 scopus 로고
    • Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers
    • Ramamoorthy, A., F. M. Marassi, M. Zasloff, and S. J. Opella. 1995. Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers. J. Biomol. NMR. 6:329-334.
    • (1995) J. Biomol. NMR , vol.6 , pp. 329-334
    • Ramamoorthy, A.1    Marassi, F.M.2    Zasloff, M.3    Opella, S.J.4
  • 34
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • Gazit, E., I. R. Miller, P. C. Biggin, M. S. P. Sansom, and Y. Shai. 1996. Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mol. Biol. 258:860-870.
    • (1996) J. Mol. Biol. , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.P.4    Shai, Y.5
  • 35
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • Yamaguchi, S., D. Huster, A. Waring, R. I. Lehrer, W. Kearney, B. F. Tack, and M. Hong. 2001. Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy. Biophys. J. 81:2203-2214.
    • (2001) Biophys. J. , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 36
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., M. Zasloff, and S. J. Opella. 1993. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2:2077-2084.
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 37
    • 0034601806 scopus 로고    scopus 로고
    • Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures
    • Oh, D., S. Y. Shin, S. Lee, J. H. Kang, S. D. Kim, P. D. Ryu, K. S. Hahm, and Y. Kim. 2000. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. Biochemistry. 39:11855-11864.
    • (2000) Biochemistry , vol.39 , pp. 11855-11864
    • Oh, D.1    Shin, S.Y.2    Lee, S.3    Kang, J.H.4    Kim, S.D.5    Ryu, P.D.6    Hahm, K.S.7    Kim, Y.8
  • 38
    • 0036231767 scopus 로고    scopus 로고
    • Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides
    • Sawai, M. V., A. J. Waring, W. R. Kearney, P. B. McCray Jr., W. R. Forsyth, R. I. Lehrer, and B. F. Tack. 2002. Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides. Protein Eng. 15:225-232.
    • (2002) Protein Eng. , vol.15 , pp. 225-232
    • Sawai, M.V.1    Waring, A.J.2    Kearney, W.R.3    McCray Jr., P.B.4    Forsyth, W.R.5    Lehrer, R.I.6    Tack, B.F.7
  • 39
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • Killian, J. A. 2003. Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett. 555:134-138.
    • (2003) FEBS Lett. , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 40
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R., and J. A. Killian. 2003. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol. Membr. Biol. 20:271-284.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 271-284
    • De Planque, M.R.1    Killian, J.A.2
  • 41
    • 0026011502 scopus 로고
    • Fluid bilayer structure determination by the combined use of x-ray and neutron diffraction. I. Fluid bilayer models and the limits of resolution
    • Wiener, M. C., and S. H. White. 1991. Fluid bilayer structure determination by the combined use of x-ray and neutron diffraction. I. Fluid bilayer models and the limits of resolution. Biophys. J. 59:162-173.
    • (1991) Biophys. J. , vol.59 , pp. 162-173
    • Wiener, M.C.1    White, S.H.2
  • 42
    • 0025964363 scopus 로고
    • Fluid bilayer structure determination by the combined use of x-ray and neutron diffraction. II. "Composition-space" refinement method
    • Wiener, M. C., and S. H. White. 1991. Fluid bilayer structure determination by the combined use of x-ray and neutron diffraction. II. "Composition-space" refinement method. Biophys. J. 59:174-185.
    • (1991) Biophys. J. , vol.59 , pp. 174-185
    • Wiener, M.C.1    White, S.H.2
  • 43
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • Wiener, M. C., and S. H. White. 1992. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys. J. 61:437-447.
    • (1992) Biophys. J. , vol.61 , pp. 437-447
    • Wiener, M.C.1    White, S.H.2
  • 44
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W. M., W. C. Wimley, K. Gawrisch, and S. H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37:14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 45
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R. E., and S. H. White. 1989. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry. 28:3421-3437.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 46
    • 0019496872 scopus 로고
    • Location of hexane in lipid bilayers determined by neutron diffraction
    • White, S. H., G. I. King, and J. I. Cain. 1981. Location of hexane in lipid bilayers determined by neutron diffraction. Nature. 290:161-163.
    • (1981) Nature , vol.290 , pp. 161-163
    • White, S.H.1    King, G.I.2    Cain, J.I.3
  • 47
    • 0033605318 scopus 로고    scopus 로고
    • Experimentally based orientational refinement of membrane protein models: A structure for the influenza A M2 H+ channel
    • Kukol, A., P. D. Adams, L. M. Rice, A. T. Brunger, and T. I. Arkin. 1999. Experimentally based orientational refinement of membrane protein models: a structure for the influenza A M2 H+ channel. J. Mol. Biol. 286:951-962.
    • (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, T.I.5
  • 48
    • 0032819359 scopus 로고    scopus 로고
    • vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching
    • Kukol, A., and I. T. Arkin. 1999. vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching. Biophys. J. 77:1594-1601.
    • (1999) Biophys. J. , vol.77 , pp. 1594-1601
    • Kukol, A.1    Arkin, I.T.2
  • 49
    • 0026716643 scopus 로고
    • Membrane-protein structure prediction - Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. 1992.Membrane-protein structure prediction - hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 50
    • 0347362806 scopus 로고    scopus 로고
    • Synthesis and biophysical characterization of a multidomain peptide from a Saccharomyces cerevisiae G protein-coupled receptor
    • Naider, F., F. X. Ding, N. C. VerBerkmoes, B. Arshava, and J. M. Becker. 2003. Synthesis and biophysical characterization of a multidomain peptide from a Saccharomyces cerevisiae G protein-coupled receptor. J. Biol. Chem. 278:52537-52545.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52537-52545
    • Naider, F.1    Ding, F.X.2    VerBerkmoes, N.C.3    Arshava, B.4    Becker, J.M.5
  • 51
    • 0031563818 scopus 로고    scopus 로고
    • Helix packing in membrane proteins
    • Bowie, J. U. 1997. Helix packing in membrane proteins. J. Mol. Biol. 272:780-789.
    • (1997) J. Mol. Biol. , vol.272 , pp. 780-789
    • Bowie, J.U.1
  • 52
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • Ulmschneider, M. B., and M. S. P. Sansom. 2001. Amino acid distributions in integral membrane protein structures. Biochim. Biophys. Acta. 1512:1-14.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 1-14
    • Ulmschneider, M.B.1    Sansom, M.S.P.2
  • 53
    • 0037213506 scopus 로고    scopus 로고
    • A common architecture for K+ channels and ionotropic glutamate receptors?
    • Kuner, T., P. H. Seeburg, and H. R. Guy. 2003. A common architecture for K+ channels and ionotropic glutamate receptors? Trends Neurosci. 26:27-32.
    • (2003) Trends Neurosci. , vol.26 , pp. 27-32
    • Kuner, T.1    Seeburg, P.H.2    Guy, H.R.3
  • 54
    • 0030723767 scopus 로고    scopus 로고
    • Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix
    • Hunt, J. F., P. Rath, K. J. Rothschild, and D. M. Engelman. 1997. Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix. Biochemistry. 36:15177-15192.
    • (1997) Biochemistry , vol.36 , pp. 15177-15192
    • Hunt, J.F.1    Rath, P.2    Rothschild, K.J.3    Engelman, D.M.4
  • 55
    • 0030589158 scopus 로고    scopus 로고
    • Towards membrane protein design: PH-sensitive topology of histidine-containing polypeptides
    • Bechinger, B. 1996. Towards membrane protein design: pH-sensitive topology of histidine-containing polypeptides. J. Mol. Biol. 263:768-775.
    • (1996) J. Mol. Biol. , vol.263 , pp. 768-775
    • Bechinger, B.1
  • 56
    • 0028577485 scopus 로고
    • Semisynthetic proteins: Model systems for the study of the insertion of hydrophobic peptides into preformed lipid bilayers
    • Moll, T. S., and T. E. Thompson. 1994. Semisynthetic proteins: model systems for the study of the insertion of hydrophobic peptides into preformed lipid bilayers. Biochemistry. 33:15469-15482.
    • (1994) Biochemistry , vol.33 , pp. 15469-15482
    • Moll, T.S.1    Thompson, T.E.2
  • 57
    • 0030050901 scopus 로고    scopus 로고
    • Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence
    • Soekarjo, M., M. Eisenhawer, A. Kuhn, and H. Vogel. 1996. Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence. Biochemistry. 35:1232-1241.
    • (1996) Biochemistry , vol.35 , pp. 1232-1241
    • Soekarjo, M.1    Eisenhawer, M.2    Kuhn, A.3    Vogel, H.4
  • 58
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White, S. H., and W. C. Wimley. 1998. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta. 1376:339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 59
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H., and W. C. Wimley. 1999. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28:319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 60
    • 4444343863 scopus 로고    scopus 로고
    • Lipid bilayer topology of the transmembrane alpha-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy
    • Koehorst, R. B. M., R. B. Spruijt, F. J. Vergeldt, and M. A. Hemminga. 2004. Lipid bilayer topology of the transmembrane alpha-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy. Biophys. J. 87:1445-1455.
    • (2004) Biophys. J. , vol.87 , pp. 1445-1455
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Vergeldt, F.J.3    Hemminga, M.A.4
  • 61
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza a virus: An intrinsic property
    • Kovacs, F. A., J. K. Denny, Z. Song, J. R. Quine, and T. A. Cross. 2000. Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property. J. Mol. Biol. 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
  • 62
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • Duong-Ly, K. C., V. Nanda, W. F. DeGrado, and K. P. Howard. 2005. The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci. 14:856-861.
    • (2005) Protein Sci. , vol.14 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    DeGrado, W.F.3    Howard, K.P.4
  • 63
    • 20444366208 scopus 로고    scopus 로고
    • Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch
    • Park, S. H., and S. J. Opella. 2005. Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch. J. Mol. Biol. 350:310-318.
    • (2005) J. Mol. Biol. , vol.350 , pp. 310-318
    • Park, S.H.1    Opella, S.J.2
  • 64
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • Baumann, G., and P. Mueller. 1974. A molecular model of membrane excitability. J. Supramol. Struct. 2:538-557.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 65
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y., D. Rapaport, A. Mor, P. Nicolas, and Y. Shai. 1992. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry. 31:12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 66
    • 0032763732 scopus 로고    scopus 로고
    • Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy
    • Marassi, F. M., S. J. Opella, P. Juvvadi, and R. B. Merrifield. 1999. Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy. Biophys. J. 77:3152-3155.
    • (1999) Biophys. J. , vol.77 , pp. 3152-3155
    • Marassi, F.M.1    Opella, S.J.2    Juvvadi, P.3    Merrifield, R.B.4
  • 67
    • 0345305860 scopus 로고    scopus 로고
    • Bilayer localization of membrane-active peptides studied in biomimetic vesicles by visible and fluorescence spectroscopies
    • Sheynis, T., J. Sykora, A. Benda, S. Kolusheva, M. Hof, and R. Jelinek. 2003. Bilayer localization of membrane-active peptides studied in biomimetic vesicles by visible and fluorescence spectroscopies. Eur. J. Biochem. 270:4478-4487.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4478-4487
    • Sheynis, T.1    Sykora, J.2    Benda, A.3    Kolusheva, S.4    Hof, M.5    Jelinek, R.6
  • 68
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • Matsuzaki, K., O. Murase, H. Tokuda, S. Funakoshi, N. Fujii, and K. Miyajima. 1994. Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry. 33:3342-3349.
    • (1994) Biochemistry , vol.33 , pp. 3342-3349
    • Matsuzaki, K.1    Murase, O.2    Tokuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyajima, K.6
  • 69
    • 0032738066 scopus 로고    scopus 로고
    • Simulation studies of the interaction of antimicrobial peptides and lipid bilayers
    • La Rocca, P., P. C. Biggin, D. P. Tieleman, and M. S. Sansom. 1999. Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. Biochim. Biophys. Acta. 1462:185-200.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 185-200
    • La Rocca, P.1    Biggin, P.C.2    Tieleman, D.P.3    Sansom, M.S.4
  • 70
    • 0347319182 scopus 로고    scopus 로고
    • Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: A site-directed spinlabeling study
    • Bhargava, K., and J. B. Feix. 2004. Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spinlabeling study. Biophys. J. 86:329-336.
    • (2004) Biophys. J. , vol.86 , pp. 329-336
    • Bhargava, K.1    Feix, J.B.2
  • 71
    • 0025249842 scopus 로고
    • Membrane-protein folding and oligomerization - The 2-stage model
    • Popot, J. L., and D. M. Engelman. 1990. Membrane-protein folding and oligomerization - the 2-stage model. Biochemistry. 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 74
    • 0026642866 scopus 로고
    • Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment
    • Kahn, T. W., and D. M. Engelman. 1992. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry. 31:6144-6151.
    • (1992) Biochemistry , vol.31 , pp. 6144-6151
    • Kahn, T.W.1    Engelman, D.M.2
  • 75
    • 0344551149 scopus 로고    scopus 로고
    • Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2delta
    • Kessel, A., D. Shental-Bechor, T. Haliloglu, and N. Ben-Tal. 2003. Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2delta. Biophys. J. 85:3431-3444.
    • (2003) Biophys. J. , vol.85 , pp. 3431-3444
    • Kessel, A.1    Shental-Bechor, D.2    Haliloglu, T.3    Ben-Tal, N.4
  • 76
    • 0344551098 scopus 로고    scopus 로고
    • Interactions of the M2delta segment of the acetylcholine receptor with lipid bilayers: A continuum-solvent model study
    • Kessel, A., T. Haliloglu, and N. Ben-Tal. 2003. Interactions of the M2delta segment of the acetylcholine receptor with lipid bilayers: a continuum-solvent model study. Biophys. J. 85:3687-3695.
    • (2003) Biophys. J. , vol.85 , pp. 3687-3695
    • Kessel, A.1    Haliloglu, T.2    Ben-Tal, N.3
  • 77
    • 0029669955 scopus 로고    scopus 로고
    • Free-energy determinants of alpha-helix insertion into lipid bilayers
    • Ben-Tal, N., A. Ben-Shaul, A. Nicholls, and B. Honig. 1996. Free-energy determinants of alpha-helix insertion into lipid bilayers. Biophys. J. 70:1803-1812.
    • (1996) Biophys. J. , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Ben-Shaul, A.2    Nicholls, A.3    Honig, B.4
  • 78
    • 1042267271 scopus 로고    scopus 로고
    • Implicit solvent model estimates of the stability of model structures of the alamethicin channel
    • Kessel, A., D. P. Tieleman, and N. Ben-Tal. 2004. Implicit solvent model estimates of the stability of model structures of the alamethicin channel. Eur. Biophys. J. 33:16-28.
    • (2004) Eur. Biophys. J. , vol.33 , pp. 16-28
    • Kessel, A.1    Tieleman, D.P.2    Ben-Tal, N.3
  • 79
    • 0030431744 scopus 로고    scopus 로고
    • Principles of membrane protein assembly and structure
    • von Heijne, G. 1997. Principles of membrane protein assembly and structure. Prog. Biophys. Mol. Biol. 66:113-139.
    • (1997) Prog. Biophys. Mol. Biol. , vol.66 , pp. 113-139
    • Von Heijne, G.1
  • 80
    • 0037062590 scopus 로고    scopus 로고
    • Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides
    • Strandberg, E., S. Morein, D. T. Rijkers, R. M. Liskamp, P. C. van der Wel, and J. A. Killian. 2002. Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides. Biochemistry. 41:7190-7198.
    • (2002) Biochemistry , vol.41 , pp. 7190-7198
    • Strandberg, E.1    Morein, S.2    Rijkers, D.T.3    Liskamp, R.M.4    Van Der Wel, P.C.5    Killian, J.A.6
  • 82
    • 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
    • Killian, J. A., I. Salemink, M. R. de Planque, G. Lindblom, R. E. Koeppe 2nd, and D. V. Greathouse. 1996. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. 35:1037-1045.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.