메뉴 건너뛰기




Volumn 13, Issue 3, 2012, Pages 267-279

Determining the orientation and localization of membrane-bound peptides

Author keywords

Antimicrobial peptides; Immersion depth; Membrane bound peptides; NMR spectroscopy; Orientation; Paramagnetic relaxation enhancement; Peptide hormones; Toxins

Indexed keywords

DODECYL SULFATE SODIUM; DODECYLPHOSPHORYLCHOLINE; GADOXETIC ACID; MEMBRANE PROTEIN; N,N,N TRIMETHYLTEMPAMINE; NITROXIDE; TRYPTOPHAN;

EID: 84862507819     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312800785049     Document Type: Article
Times cited : (19)

References (120)
  • 1
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol., 2001, 305, 567-580.
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 3
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution, Annu
    • Popot, J. L.; Engelman, D. M. Helical membrane protein folding, stability, and evolution, Annu. Rev. Biochem., 2000, 69, 881-922.
    • (2000) Rev. Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 4
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol., 2005, 3, 238-250.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 5
    • 77955254296 scopus 로고    scopus 로고
    • Solution structure and membrane binding of the toxin fst of the par addiction module
    • Göbl, C.; Kosol, S.; Stockner, T.; Rückert, H. M.; Zangger, K. Solution structure and membrane binding of the toxin fst of the par addiction module. Biochemistry, 2010, 49, 6567-6575.
    • (2010) Biochemistry , vol.49 , pp. 6567-6575
    • Göbl, C.1    Kosol, S.2    Stockner, T.3    Rückert, H.M.4    Zangger, K.5
  • 6
    • 77955417391 scopus 로고    scopus 로고
    • The peptide hormone ghrelin binds to membrane-mimetics via its octanoyl chain and an adjacent phenylalanine
    • Grossauer, J.; Kosol, S.; Schrank, E.; Zangger, K. The peptide hormone ghrelin binds to membrane-mimetics via its octanoyl chain and an adjacent phenylalanine. Bioorg. Med. Chem., 2010, 18, 5483-5488.
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 5483-5488
    • Grossauer, J.1    Kosol, S.2    Schrank, E.3    Zangger, K.4
  • 7
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature (London, UK), 2002, 415, 389-395.
    • (2002) Nature (London, UK) , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 10
    • 65249114173 scopus 로고    scopus 로고
    • Peptide models of membrane protein folding
    • Rath, A.; Tulumello, D. V.; Deber, C. M. Peptide models of membrane protein folding, Biochemistry, 2009, 48, 3036-3045.
    • (2009) Biochemistry , vol.48 , pp. 3036-3045
    • Rath, A.1    Tulumello, D.V.2    Deber, C.M.3
  • 11
    • 77950576779 scopus 로고    scopus 로고
    • Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape
    • Göbl, C.; Dulle, M.; Hohlweg, W.; Grossauer, J.; Falsone, S. F.; Glatter, O.; Zangger, K. Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape. J. Phys. Chem. B., 2010, 114, 4717-4724.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4717-4724
    • Göbl, C.1    Dulle, M.2    Hohlweg, W.3    Grossauer, J.4    Falsone, S.F.5    Glatter, O.6    Zangger, K.7
  • 12
    • 0029381531 scopus 로고
    • The use of dodecylphosphocholine micelles in solution NMR
    • Kallick, D. A.; Tessmer, M. R.; Watts, C. R.; Li, C. Y. The use of dodecylphosphocholine micelles in solution NMR. J. Magn. Reson. B., 1995, 109, 60-65.
    • (1995) J. Magn. Reson. B , vol.109 , pp. 60-65
    • Kallick, D.A.1    Tessmer, M.R.2    Watts, C.R.3    Li, C.Y.4
  • 13
    • 3042746872 scopus 로고    scopus 로고
    • Effects of detergent alkyl chain length and chemical structure on the properties of a micellebound bacterial membrane targeting peptide
    • Keifer, P. A.; Peterkofsky, A.; Wang, G. Effects of detergent alkyl chain length and chemical structure on the properties of a micellebound bacterial membrane targeting peptide. Anal. Biochem., 2004, 331, 33-39.
    • (2004) Anal. Biochem , vol.331 , pp. 33-39
    • Keifer, P.A.1    Peterkofsky, A.2    Wang, G.3
  • 14
    • 33746045690 scopus 로고    scopus 로고
    • Current applications of bicelles in NMR studies of membraneassociated amphiphiles and proteins
    • Prosser, R. S.; Evanics, F.; Kitevski, J. L.; Al-Abdul-Wahid, M. S. Current applications of bicelles in NMR studies of membraneassociated amphiphiles and proteins. Biochemistry, 2006, 45, 8453-8465.
    • (2006) Biochemistry , vol.45 , pp. 8453-8465
    • Prosser, R.S.1    Evanics, F.2    Kitevski, J.L.3    Al-Abdul-Wahid, M.S.4
  • 16
    • 53249147452 scopus 로고    scopus 로고
    • Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study
    • Abbassi, F.; Galanth, C.; Amiche, M.; Saito, K.; Piesse, C.; Zargarian, L.; Hani, K.; Nicolas, P.; Lequin, O.; Ladram, A. Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study. Biochemistry, 2008, 47, 10513-10525.
    • (2008) Biochemistry , vol.47 , pp. 10513-10525
    • Abbassi, F.1    Galanth, C.2    Amiche, M.3    Saito, K.4    Piesse, C.5    Zargarian, L.6    Hani, K.7    Nicolas, P.8    Lequin, O.9    Ladram, A.10
  • 18
    • 77950519481 scopus 로고    scopus 로고
    • Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems
    • Kosol, S.; Zangger, K. Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems. J. Struct. Biol., 2010, 170, 172-179.
    • (2010) J. Struct. Biol , vol.170 , pp. 172-179
    • Kosol, S.1    Zangger, K.2
  • 19
    • 49449096526 scopus 로고    scopus 로고
    • Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4
    • Zangger, K.; Gossler, R.; Khatai, L.; Lohner, K.; Jilek, A. Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4. Toxicon, 2008, 52, 246-254.
    • (2008) Toxicon , vol.52 , pp. 246-254
    • Zangger, K.1    Gossler, R.2    Khatai, L.3    Lohner, K.4    Jilek, A.5
  • 20
    • 67651218994 scopus 로고    scopus 로고
    • Headgroup-dependent membrane catalysis of apelin-receptor interactions is likely
    • Langelaan, D. N.; Rainey, J. K. Headgroup-dependent membrane catalysis of apelin-receptor interactions is likely. J. Phys. Chem. B., 2009, 113, 10465-10471.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10465-10471
    • Langelaan, D.N.1    Rainey, J.K.2
  • 21
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon, A. M.; Curnow, P.; Booth, P. J. Membrane proteins, lipids and detergents: not just a soap opera. Biochim. Biophys. Acta., 2004, 1666, 105-117.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 22
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A.; Abildgaard, F.; Bushweller, J. H.; Tamm, L. K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol., 2001, 8, 334-338.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 23
    • 0034633264 scopus 로고    scopus 로고
    • Functionality of a Membrane Protein in Bicelles, Ana
    • Czerski, L.; Sanders, C. R. Functionality of a Membrane Protein in Bicelles, Ana. Biochem., 2000, 284, 327-333.
    • (2000) Biochem , vol.284 , pp. 327-333
    • Czerski, L.1    Sanders, C.R.2
  • 24
    • 0032060715 scopus 로고    scopus 로고
    • On choosing a detergent for solution NMR studies of membrane proteins
    • Vinogradova, O.; Sönnichsen, F.; Sanders, C. R. On choosing a detergent for solution NMR studies of membrane proteins. J. Biomol. NMR, 1998, 11, 381-386.
    • (1998) J. Biomol. NMR , vol.11 , pp. 381-386
    • Vinogradova, O.1    Sönnichsen, F.2    Sanders, C.R.3
  • 25
    • 0037109010 scopus 로고    scopus 로고
    • Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy
    • Fernandez, C.; Hilty, C.; Wider, G.; Wuthrich, K. Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy. Proc. Natl. Acad. Sci. USA, 2002, 99, 13533-13537.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13533-13537
    • Fernandez, C.1    Hilty, C.2    Wider, G.3    Wuthrich, K.4
  • 26
    • 3242655534 scopus 로고    scopus 로고
    • Membrane protein - lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents
    • Hilty, C.; Wider, G.; Fernandez, C.; Wuethrich, K. Membrane protein - lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents, ChemBioChem., 2004, 5, 467-473.
    • (2004) ChemBioChem , vol.5 , pp. 467-473
    • Hilty, C.1    Wider, G.2    Fernandez, C.3    Wuethrich, K.4
  • 27
    • 24744466153 scopus 로고    scopus 로고
    • Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles
    • Appelt, C.; Wessolowski, A.; Soderhall, J. A.; Dathe, M.; Schmieder, P. Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles, Chembiochem., 2005, 6, 1654-1662.
    • (2005) Chembiochem , vol.6 , pp. 1654-1662
    • Appelt, C.1    Wessolowski, A.2    Soderhall, J.A.3    Dathe, M.4    Schmieder, P.5
  • 28
    • 33646544424 scopus 로고    scopus 로고
    • Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: High resolution NMR studies of peptide.lipid discoidal complexes
    • Mishra, V. K.; Anantharamaiah, G. M.; Segrest, J. P.; Palgunachari, M. N.; Chaddha, M.; Sham, S. W.; Krishna, N. R. Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: high resolution NMR studies of peptide.lipid discoidal complexes. J. Biol. Chem., 2006, 281, 6511-6519.
    • (2006) J. Biol. Chem , vol.281 , pp. 6511-6519
    • Mishra, V.K.1    Anantharamaiah, G.M.2    Segrest, J.P.3    Palgunachari, M.N.4    Chaddha, M.5    Sham, S.W.6    Krishna, N.R.7
  • 29
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium [see comments]
    • published erratum appears in Science, 1997 Dec 5, 278(5344), 1697]
    • Tjandra, N.; Bax, A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium [see comments] [published erratum appears in Science, 1997 Dec 5, 278(5344), 1697], Science, 1997, 278, 1111-1114.
    • Science , vol.1997 , Issue.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 30
    • 7744243314 scopus 로고    scopus 로고
    • Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: Application to phospholamban
    • Mascioni, A.; Eggimann, B. L.; Veglia, G. Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: application to phospholamban. Chem. Phys. Lipids, 2004, 132, 133-144.
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 133-144
    • Mascioni, A.1    Eggimann, B.L.2    Veglia, G.3
  • 31
    • 0042029753 scopus 로고    scopus 로고
    • Dipolar Waves as NMR maps of helices in proteins
    • Mesleh, M. F.; Opella, S. J. Dipolar Waves as NMR maps of helices in proteins. J. Magn. Reson., 2003, 163, 288-299.
    • (2003) J. Magn. Reson , vol.163 , pp. 288-299
    • Mesleh, M.F.1    Opella, S.J.2
  • 33
    • 0141885396 scopus 로고    scopus 로고
    • Theoretical analysis of residual dipolar coupling patterns in regular secondary structures of proteins
    • Mascioni, A.; Veglia, G. Theoretical analysis of residual dipolar coupling patterns in regular secondary structures of proteins. J. Am. Chem. Soc., 2003, 125, 12520-12526.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 12520-12526
    • Mascioni, A.1    Veglia, G.2
  • 34
    • 30744447942 scopus 로고    scopus 로고
    • Orientation and conformational preference of leucine-enkephalin at the surface of a hydrated dimyristoylphosphatidylcholine bilayer: NMR and MD simulation
    • Chandrasekhar, I.; van Gunsteren, W. F.; Zandomeneghi, G.; Williamson, P. T.; Meier, B. H. Orientation and conformational preference of leucine-enkephalin at the surface of a hydrated dimyristoylphosphatidylcholine bilayer: NMR and MD simulation. J. Am. Chem. Soc., 2006, 128, 159-170.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 159-170
    • Chandrasekhar, I.1    van Gunsteren, W.F.2    Zandomeneghi, G.3    Williamson, P.T.4    Meier, B.H.5
  • 35
    • 34249856814 scopus 로고    scopus 로고
    • DNA-nanotube-induced alignment of membrane proteins for NMR structure determination
    • Douglas, S. M.; Chou, J. J.; Shih, W. M. DNA-nanotube-induced alignment of membrane proteins for NMR structure determination. Proc. Natl. Acad. Sci. USA, 2007, 104, 6644-6648.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6644-6648
    • Douglas, S.M.1    Chou, J.J.2    Shih, W.M.3
  • 36
    • 0019464732 scopus 로고
    • Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies
    • Brown, L. R.; Bosch, C.; Wuthrich, K. Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies. Biochim. Biophys. Acta., 1981, 642, 296-312.
    • (1981) Biochim. Biophys. Acta , vol.642 , pp. 296-312
    • Brown, L.R.1    Bosch, C.2    Wuthrich, K.3
  • 38
    • 0037181061 scopus 로고    scopus 로고
    • Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and 19F NMR spectroscopy
    • Luchette, P. A.; Prosser, R. S.; Sanders, C. R. Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and 19F NMR spectroscopy. J. Am. Chem. Soc., 2002, 124, 1778-1781.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 1778-1781
    • Luchette, P.A.1    Prosser, R.S.2    Sanders, C.R.3
  • 39
    • 36849003406 scopus 로고    scopus 로고
    • The measurement of immersion depth and topology of membrane proteins by solution state NMR
    • Prosser, R. S.; Evanics, F.; Kitevski, J. L.; Patel, S. The measurement of immersion depth and topology of membrane proteins by solution state NMR. Biochim. Biophys. Acta., 2007, 1768, 3044-3051.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3044-3051
    • Prosser, R.S.1    Evanics, F.2    Kitevski, J.L.3    Patel, S.4
  • 42
    • 0026608998 scopus 로고
    • Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering
    • Esposito, G.; Lesk, A. M.; Molinari, H.; Motta, A.; Niccolai, N.; Pastore, A. Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering. J. Mol. Biol., 1992, 224, 659-670.
    • (1992) J. Mol. Biol , vol.224 , pp. 659-670
    • Esposito, G.1    Lesk, A.M.2    Molinari, H.3    Motta, A.4    Niccolai, N.5    Pastore, A.6
  • 43
    • 0025153333 scopus 로고
    • NMR identification of protein surfaces using paramagnetic probes
    • Petros, A. M.; Mueller, L.; Kopple, K. D. NMR identification of protein surfaces using paramagnetic probes. Biochemistry, 1990, 29, 10041-10048.
    • (1990) Biochemistry , vol.29 , pp. 10041-10048
    • Petros, A.M.1    Mueller, L.2    Kopple, K.D.3
  • 44
    • 0034801470 scopus 로고    scopus 로고
    • Surface recognition of a protein using designed transition metal complexes
    • Fazal, M. A.; Roy, B. C.; Sun, S.; Mallik, S.; Rodgers, K. R. Surface recognition of a protein using designed transition metal complexes. J. Am. Chem. Soc., 2001, 123, 6283-6290.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 6283-6290
    • Fazal, M.A.1    Roy, B.C.2    Sun, S.3    Mallik, S.4    Rodgers, K.R.5
  • 46
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate
    • Pintacuda, G.; Otting, G. Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate. J. Am. Chem. Soc., 2002, 124, 372-373.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 48
    • 34247536274 scopus 로고    scopus 로고
    • Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves
    • Respondek, M.; Madl, T.; Göbl, C.; Golser, R.; Zangger, K. Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves. J. Am. Chem. Soc., 2007, 129, 5228-5234.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5228-5234
    • Respondek, M.1    Madl, T.2    Göbl, C.3    Golser, R.4    Zangger, K.5
  • 49
    • 70350536779 scopus 로고    scopus 로고
    • Quantitative use of paramagnetic relaxation enhancements for determining orientations and insertion depths of peptides in micelles
    • Franzmann, M.; Otzen, D.; Wimmer, R. Quantitative use of paramagnetic relaxation enhancements for determining orientations and insertion depths of peptides in micelles, Chembiochem., 2009, 10, 2339-2347.
    • (2009) Chembiochem , vol.10 , pp. 2339-2347
    • Franzmann, M.1    Otzen, D.2    Wimmer, R.3
  • 51
    • 7044224836 scopus 로고    scopus 로고
    • The alignment, structure and dynamics of membrane-associated polypeptides by solid-state NMR spectroscopy
    • Bechinger, B.; Aisenbrey, C.; Bertani, P. The alignment, structure and dynamics of membrane-associated polypeptides by solid-state NMR spectroscopy. Biochim. Biophys. Acta., 2004, 1666, 190-204.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 190-204
    • Bechinger, B.1    Aisenbrey, C.2    Bertani, P.3
  • 52
    • 0037077536 scopus 로고    scopus 로고
    • Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban
    • Mascioni, A.; Karim, C.; Zamoon, J.; Thomas, D. D.; Veglia, G. Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban. J. Am. Chem. Soc., 2002, 124, 9392-9393.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9392-9393
    • Mascioni, A.1    Karim, C.2    Zamoon, J.3    Thomas, D.D.4    Veglia, G.5
  • 53
    • 33745747109 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin
    • Ramamoorthy, A.; Thennarasu, S.; Lee, D. K.; Tan, A.; Maloy, L. Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophys. J., 2006, 91, 206-216.
    • (2006) Biophys. J , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.K.3    Tan, A.4    Maloy, L.5
  • 54
    • 33846595904 scopus 로고
    • High-Resolution Heteronuclear Dipolar Solid-State NMR Spectroscopy
    • Wu, C. H.; Ramamoorthy, A.; Opella, S. J. High-Resolution Heteronuclear Dipolar Solid-State NMR Spectroscopy. J. Magn. Reson. A., 1994, 109, 270-272.
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 55
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi, F. M.; Opella, S. J. A solid-state NMR index of helical membrane protein structure and topology. J. Magn. Reson., 2000, 144, 150-155.
    • (2000) J. Magn. Reson , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 57
    • 0035142956 scopus 로고    scopus 로고
    • A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy
    • Marassi, F. M. A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy. Biophys. J., 2001, 80, 994-1003.
    • (2001) Biophys. J , vol.80 , pp. 994-1003
    • Marassi, F.M.1
  • 58
    • 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., 2001, 10, 2241-2250.
    • (2001) Protein Sci , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 59
    • 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.; Mrse, A. A.; Nevzorov, A. A.; Mesleh, M. F.; Oblatt-Montal, M.; Montal, M.; Opella, S. J. Three-dimensional structure of the channel-forming trans-membrane domain of virus protein u (Vpu) from HIV-1. J. Mol. Biol., 2003, 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
  • 60
    • 20444366208 scopus 로고    scopus 로고
    • Tilt Angle of a Trans-membrane Helix is Determined by Hydrophobic Mismatch
    • Park, S. H.; Opella, S. J. Tilt Angle of a Trans-membrane Helix is Determined by Hydrophobic Mismatch. J. Mol. Biol., 2005, 350, 310-318.
    • (2005) J. Mol. Biol , vol.350 , pp. 310-318
    • Park, S.H.1    Opella, S.J.2
  • 61
    • 34247844400 scopus 로고    scopus 로고
    • Uniformly aligned full-length membrane proteins in liquid crystalline bilayers for structural characterization
    • Li, C.; Gao, P.; Qin, H.; Chase, R.; Gor'kov, P. L.; Brey, W. W.; Cross, T. A. Uniformly aligned full-length membrane proteins in liquid crystalline bilayers for structural characterization. J. Am. Chem. Soc., 2007, 129, 5304-5305.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5304-5305
    • Li, C.1    Gao, P.2    Qin, H.3    Chase, R.4    Gor'kov, P.L.5    Brey, W.W.6    Cross, T.A.7
  • 62
    • 33748775215 scopus 로고    scopus 로고
    • Structure determination of a membrane protein with two transmembrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy
    • De Angelis, A. A.; Howell, S. C.; Nevzorov, A. A.; Opella, S. J. Structure determination of a membrane protein with two transmembrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy. J. Am. Chem. Soc., 2006, 128, 12256-12267.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 12256-12267
    • de Angelis, A.A.1    Howell, S.C.2    Nevzorov, A.A.3    Opella, S.J.4
  • 63
    • 0042468159 scopus 로고    scopus 로고
    • A magic sandwich pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy
    • Nevzorov, A. A.; Opella, S. J. A magic sandwich pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy. J. Magn. Reson., 2003, 164, 182-186.
    • (2003) J. Magn. Reson , vol.164 , pp. 182-186
    • Nevzorov, A.A.1    Opella, S.J.2
  • 64
    • 67649865606 scopus 로고    scopus 로고
    • Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach
    • Traaseth, N. J.; Shi, L.; Verardi, R.; Mullen, D. G.; Barany, G.; Veglia, G. Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach. Proc. Natl. Acad. Sci. USA, 2009, 106, 10165-10170.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10165-10170
    • Traaseth, N.J.1    Shi, L.2    Verardi, R.3    Mullen, D.G.4    Barany, G.5    Veglia, G.6
  • 65
    • 0034167156 scopus 로고    scopus 로고
    • Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings
    • Al-Hashimi, H. M.; Valafar, H.; Terrell, M.; Zartler, E. R.; Eidsness, M. K.; Prestegard, J. H. Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings. J. Magn. Reson., 2000, 143, 402-406.
    • (2000) J. Magn. Reson , vol.143 , pp. 402-406
    • Al-Hashimi, H.M.1    Valafar, H.2    Terrell, M.3    Zartler, E.R.4    Eidsness, M.K.5    Prestegard, J.H.6
  • 66
    • 0038652081 scopus 로고    scopus 로고
    • Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
    • Zeri, A. C.; Mesleh, M. F.; Nevzorov, A. A.; Opella, S. J. Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy. Proc. Natl. Acad. Sci. USA, 2003, 100, 6458-6463.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6458-6463
    • Zeri, A.C.1    Mesleh, M.F.2    Nevzorov, A.A.3    Opella, S.J.4
  • 67
    • 4344702276 scopus 로고    scopus 로고
    • Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy
    • Thiriot, D. S.; Nevzorov, A. A.; Zagyanskiy, L.; Wu, C. H.; Opella, S. J. Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy. J. Mol. Biol., 2004, 341, 869-879.
    • (2004) J. Mol. Biol , vol.341 , pp. 869-879
    • Thiriot, D.S.1    Nevzorov, A.A.2    Zagyanskiy, L.3    Wu, C.H.4    Opella, S.J.5
  • 68
    • 0025194257 scopus 로고
    • Deuterium NMR of 2HCO-Val1 gramicidin A and 2HCO-Val1-DLeu2 gramicidin A in oriented DMPC bilayers
    • Hing, A. W.; Adams, S. P.; Silbert, D. F.; Norberg, R. E. Deuterium NMR of 2HCO-Val1 gramicidin A and 2HCO-Val1-DLeu2 gramicidin A in oriented DMPC bilayers, Biochemistry, 1990, 29, 4156-4166.
    • (1990) Biochemistry , vol.29 , pp. 4156-4166
    • Hing, A.W.1    Adams, S.P.2    Silbert, D.F.3    Norberg, R.E.4
  • 69
    • 0036708458 scopus 로고    scopus 로고
    • Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR
    • van der Wel, P. C.; Strandberg, E.; Killian, J. A.; Koeppe, R. E., 2nd. Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR. Biophys. J., 2002, 83, 1479-1488.
    • (2002) Biophys. J , vol.83 , pp. 1479-1488
    • van der Wel, P.C.1    Strandberg, E.2    Killian, J.A.3    Koeppe, R.E.4
  • 70
    • 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
    • Ozdirekcan, S.; Rijkers, D. T.; Liskamp, R. M.; Killian, J. A. Influence of flanking residues on tilt and rotation angles of transmembrane peptides in lipid bilayers. A solid-state 2H NMR study. Biochemistry, 2005, 44, 1004-1012.
    • (2005) Biochemistry , vol.44 , pp. 1004-1012
    • Ozdirekcan, S.1    Rijkers, D.T.2    Liskamp, R.M.3    Killian, J.A.4
  • 71
    • 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.; Ozdirekcan, S.; Rijkers, D. T.; van der Wel, P. C.; Koeppe, R. E., 2nd; Liskamp, R. M.; Killian, J. A. Tilt angles of transmembrane model peptides in oriented and non-oriented lipid bilayers as determined by 2H solid-state NMR. Biophys. J., 2004, 86, 3709-3721.
    • (2004) Biophys. J , vol.86 , pp. 3709-3721
    • Strandberg, E.1    Ozdirekcan, S.2    Rijkers, D.T.3    van der Wel, P.C.4    Koeppe, R.E.5    Liskamp, R.M.6    Killian, J.A.7
  • 72
    • 33845933103 scopus 로고    scopus 로고
    • Synergistic transmembrane alignment of the antimicrobial heterodimer PGLa/magainin
    • Tremouilhac, P.; Strandberg, E.; Wadhwani, P.; Ulrich, A. S. Synergistic transmembrane alignment of the antimicrobial heterodimer PGLa/magainin. J. Biol. Chem., 2006, 281, 32089-32094.
    • (2006) J. Biol. Chem , vol.281 , pp. 32089-32094
    • Tremouilhac, P.1    Strandberg, E.2    Wadhwani, P.3    Ulrich, A.S.4
  • 73
    • 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.; Grant, C. V.; Daily, A. E.; Opella, S. J.; Koeppe, R. E., 2nd. 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., 2008, 130, 12584-12585.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 12584-12585
    • Vostrikov, V.V.1    Grant, C.V.2    Daily, A.E.3    Opella, S.J.4    Koeppe, R.E.5
  • 74
    • 0031993272 scopus 로고    scopus 로고
    • Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies
    • Glaubitz, C.; Watts, A. Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies. J. Magn. Reson., 1998, 130, 305-316.
    • (1998) J. Magn. Reson , vol.130 , pp. 305-316
    • Glaubitz, C.1    Watts, A.2
  • 75
    • 0033597625 scopus 로고    scopus 로고
    • Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Applications to photointermediates of bacteriorhodopsin
    • Glaubitz, C.; Burnett, I. J.; Grobner, G.; Mason, A. J.; Watts, A. Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Applications to photointermediates of bacteriorhodopsin. J. Am. Chem. Soc., 1999, 121, 5787-5794.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 5787-5794
    • Glaubitz, C.1    Burnett, I.J.2    Grobner, G.3    Mason, A.J.4    Watts, A.5
  • 76
    • 0343185890 scopus 로고    scopus 로고
    • Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy
    • Glaubitz, C.; Grobner, G.; Watts, A. Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. Biochim. Biophys. Acta., 2000, 1463, 151-161.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 151-161
    • Glaubitz, C.1    Grobner, G.2    Watts, A.3
  • 77
    • 1542375277 scopus 로고    scopus 로고
    • Identifying anisotropic constraints in multiply labeled bacteriorhodopsin by 15N MAOSS NMR: A general approach to structural studies of membrane proteins
    • Mason, A. J.; Grage, S. L.; Straus, S. K.; Glaubitz, C.; Watts, A. Identifying anisotropic constraints in multiply labeled bacteriorhodopsin by 15N MAOSS NMR: a general approach to structural studies of membrane proteins. Biophys. J., 2004, 86, 1610-1617.
    • (2004) Biophys. J , vol.86 , pp. 1610-1617
    • Mason, A.J.1    Grage, S.L.2    Straus, S.K.3    Glaubitz, C.4    Watts, A.5
  • 79
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • Gullion, T.; Schaefer, J. Rotational-echo double-resonance NMR. J. Magn. Reson., 1989, 81, 196-200.
    • (1989) J. Magn. Reson , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 80
    • 33750692000 scopus 로고    scopus 로고
    • Membrane-bound conformation and topology of the antimicrobial peptide tachyplesin I by solid-state NMR
    • Doherty, T.; Waring, A. J.; Hong, M. Membrane-bound conformation and topology of the antimicrobial peptide tachyplesin I by solid-state NMR. Biochemistry, 2006, 45, 13323-13330.
    • (2006) Biochemistry , vol.45 , pp. 13323-13330
    • Doherty, T.1    Waring, A.J.2    Hong, M.3
  • 81
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • Tang, M.; Waring, A. J.; Hong, M. Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR. J. Am. Chem. Soc., 2007, 129, 11438-11446.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 82
    • 34447513002 scopus 로고    scopus 로고
    • The membrane alignment of helical peptides from non-oriented 15N chemical shift solid-state NMR spectroscopy
    • Prongidi-Fix, L.; Bertani, P.; Bechinger, B. The membrane alignment of helical peptides from non-oriented 15N chemical shift solid-state NMR spectroscopy. J. Am. Chem. Soc., 2007, 129, 8430-8431.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 8430-8431
    • Prongidi-Fix, L.1    Bertani, P.2    Bechinger, B.3
  • 83
    • 34548812858 scopus 로고    scopus 로고
    • Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy
    • Hong, M. Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy. J. Phys. Chem. B., 2007, 111, 10340-10351.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 10340-10351
    • Hong, M.1
  • 84
    • 0035208239 scopus 로고    scopus 로고
    • Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19FNMR
    • Salgado, J.; Grage, S. L.; Kondejewski, L. H.; Hodges, R. S.; McElhaney, R. N.; Ulrich, A. S. Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19FNMR. J. Biomol. NMR., 2001, 21, 191-208.
    • (2001) J. Biomol. NMR , vol.21 , pp. 191-208
    • Salgado, J.1    Grage, S.L.2    Kondejewski, L.H.3    Hodges, R.S.4    McElhaney, R.N.5    Ulrich, A.S.6
  • 85
    • 18244390978 scopus 로고    scopus 로고
    • A ruler for determining the position of proteins in membranes
    • Nielsen, R. D.; Che, K.; Gelb, M. H.; Robinson, B. H. A ruler for determining the position of proteins in membranes. J. Am. Chem. Soc., 2005, 127, 6430-6442.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 6430-6442
    • Nielsen, R.D.1    Che, K.2    Gelb, M.H.3    Robinson, B.H.4
  • 86
    • 0347319182 scopus 로고    scopus 로고
    • Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: A site-directed spinlabeling study
    • Bhargava, K.; Feix, J. B. Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: A site-directed spinlabeling study. Biophys. J., 2004, 86, 329-336.
    • (2004) Biophys. J , vol.86 , pp. 329-336
    • Bhargava, K.1    Feix, J.B.2
  • 87
    • 33746366529 scopus 로고    scopus 로고
    • Determining the topology of integral membrane peptides using EPR spectroscopy
    • Inbaraj, J. J.; Cardon, T. B.; Laryukhin, M.; Grosser, S. M.; Lorigan, G. A. Determining the topology of integral membrane peptides using EPR spectroscopy. J. Am. Chem. Soc., 2006, 128, 9549-9554.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 9549-9554
    • Inbaraj, J.J.1    Cardon, T.B.2    Laryukhin, M.3    Grosser, S.M.4    Lorigan, G.A.5
  • 88
    • 34347252219 scopus 로고    scopus 로고
    • Determining the helicaltilt angle of a transmembrane helix in mechanically aligned lipid bilayers using EPR spectroscopy
    • Inbaraj, J. J.; Laryukhin, M.; Lorigan, G. A. Determining the helicaltilt angle of a transmembrane helix in mechanically aligned lipid bilayers using EPR spectroscopy. J. Am. Chem. Soc., 2007, 129, 7710-7711.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 7710-7711
    • Inbaraj, J.J.1    Laryukhin, M.2    Lorigan, G.A.3
  • 89
    • 48249098474 scopus 로고    scopus 로고
    • Comparing the structural topology of integral and peripheral membrane proteins utilizing electron paramagnetic resonance spectroscopy
    • Mayo, D. J.; Inbaraj, J. J.; Subbaraman, N.; Grosser, S. M.; Chan, C. A.; Lorigan, G. A. Comparing the structural topology of integral and peripheral membrane proteins utilizing electron paramagnetic resonance spectroscopy. J. Am. Chem. Soc., 2008, 130, 9656-9657.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 9656-9657
    • Mayo, D.J.1    Inbaraj, J.J.2    Subbaraman, N.3    Grosser, S.M.4    Chan, C.A.5    Lorigan, G.A.6
  • 90
    • 63349105151 scopus 로고    scopus 로고
    • Determining the helical tilt of membrane peptides using electron paramagnetic resonance spectroscopy
    • Newstadt, J. P.; Mayo, D. J.; Inbaraj, J. J.; Subbaraman, N.; Lorigan, G. A. Determining the helical tilt of membrane peptides using electron paramagnetic resonance spectroscopy. J. Magn. Reson., 2009, 198, 1-7.
    • (2009) J. Magn. Reson , vol.198 , pp. 1-7
    • Newstadt, J.P.1    Mayo, D.J.2    Inbaraj, J.J.3    Subbaraman, N.4    Lorigan, G.A.5
  • 92
    • 77950351987 scopus 로고    scopus 로고
    • Quantitative analysis of protein-lipid interactions using tryptophan fluorescence
    • Kraft, C. A.; Garrido, J. L.; Leiva-Vega, L.; Romero, G. Quantitative analysis of protein-lipid interactions using tryptophan fluorescence. Sci. Signal, 2009, 2, p 14.
    • (2009) Sci. Signal , vol.2 , pp. 14
    • Kraft, C.A.1    Garrido, J.L.2    Leiva-Vega, L.3    Romero, G.4
  • 93
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin, A. S.; Jayasinghe, S.; White, S. H. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?. Anal. Biochem., 2000, 285, 235-245.
    • (2000) Anal. Biochem , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 95
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • De Kroon, A. I.; Soekarjo, M. W.; De Gier, J.; De Kruijff, B. The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry, 1990, 29, 8229-8240.
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • de Kroon, A.I.1    Soekarjo, M.W.2    de Gier, J.3    de Kruijff, B.4
  • 96
    • 0034635171 scopus 로고    scopus 로고
    • Determining the membrane topology of peptides by fluorescence quenching
    • Wimley, W. C.; White, S. H. Determining the membrane topology of peptides by fluorescence quenching. Biochemistry, 2000, 39, 161-170.
    • (2000) Biochemistry , vol.39 , pp. 161-170
    • Wimley, W.C.1    White, S.H.2
  • 97
    • 33646421139 scopus 로고    scopus 로고
    • Probing the kinetics of membranemediated helix folding
    • Tucker, M. J.; Tang, J.; Gai, F. Probing the kinetics of membranemediated helix folding. J. Phys. Chem. B., 2006, 110, 8105-8109.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 8105-8109
    • Tucker, M.J.1    Tang, J.2    Gai, F.3
  • 98
    • 0036042982 scopus 로고    scopus 로고
    • Solvent relaxation in phospholipid bilayers: Physical understanding and biophysical applications
    • Sykora, J.; Hof, M. Solvent relaxation in phospholipid bilayers: physical understanding and biophysical applications. Cell Mol. Biol. Lett., 2002, 7, 259-261.
    • (2002) Cell Mol. Biol. Lett , vol.7 , pp. 259-261
    • Sykora, J.1    Hof, M.2
  • 99
    • 33644547037 scopus 로고    scopus 로고
    • Solvent relaxation in phospholipid bilayers: Principles and recent applications
    • Jurkiewicz, P.; Sykora, J.; Olzynska, A.; Humpolickova, J.; Hof, M. Solvent relaxation in phospholipid bilayers: principles and recent applications. J. Fluoresc., 2005, 15, 883-894.
    • (2005) J. Fluoresc , vol.15 , pp. 883-894
    • Jurkiewicz, P.1    Sykora, J.2    Olzynska, A.3    Humpolickova, J.4    Hof, M.5
  • 100
    • 0345305860 scopus 로고    scopus 로고
    • Bilayer localization of membrane-active peptides studied in biomimetic vesicles by visible and fluorescence spectroscopies
    • Sheynis, T.; Sykora, J.; Benda, A.; Kolusheva, S.; Hof, M.; Jelinek, R. Bilayer localization of membrane-active peptides studied in biomimetic vesicles by visible and fluorescence spectroscopies. Eur. J. Biochem., 2003, 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
  • 101
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S.; Bandekar, J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem., 1986, 38, 181-364.
    • (1986) Adv. Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 102
    • 33748715411 scopus 로고    scopus 로고
    • Isotope-edited IR spectroscopy for the study of membrane proteins
    • Arkin, I. T. Isotope-edited IR spectroscopy for the study of membrane proteins. Curr. Opin. Chem. Biol., 2006, 10, 394-401.
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 394-401
    • Arkin, I.T.1
  • 103
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
    • Goormaghtigh, E.; Cabiaux, V.; Ruysschaert, J. M. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur. J. Biochem., 1990, 193, 409-420.
    • (1990) Eur. J. Biochem , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 104
    • 0032909033 scopus 로고    scopus 로고
    • Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra
    • Bechinger, B.; Ruysschaert, J. M.; Goormaghtigh, E. Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra. Biophys. J., 1999, 76, 552-563.
    • (1999) Biophys. J , vol.76 , pp. 552-563
    • Bechinger, B.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 106
    • 33846818748 scopus 로고    scopus 로고
    • Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies
    • Chen, X.; Wang, J.; Boughton, A. P.; Kristalyn, C. B.; Chen, Z. Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies, J. Am. Chem. Soc., 2007, 129, 1420-1427.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 1420-1427
    • Chen, X.1    Wang, J.2    Boughton, A.P.3    Kristalyn, C.B.4    Chen, Z.5
  • 107
    • 0036293994 scopus 로고    scopus 로고
    • Multiple site-specific infrared dichroism of CD3-zeta, a transmembrane helix bundle
    • Torres, J.; Briggs, J. A.; Arkin, I. T. Multiple site-specific infrared dichroism of CD3-zeta, a transmembrane helix bundle. J. Mol. Biol., 2002, 316, 365-374.
    • (2002) J. Mol. Biol , vol.316 , pp. 365-374
    • Torres, J.1    Briggs, J.A.2    Arkin, I.T.3
  • 109
    • 0035309358 scopus 로고    scopus 로고
    • Polymerized lipid vesicles as colorimetric biosensors for biotechnological applications
    • Jelinek, R.; Kolusheva, S. Polymerized lipid vesicles as colorimetric biosensors for biotechnological applications. Biotechnol. Adv., 2001, 19, 109-118.
    • (2001) Biotechnol. Adv , vol.19 , pp. 109-118
    • Jelinek, R.1    Kolusheva, S.2
  • 110
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W. Circular dichroism. Methods Enzymol., 1995, 246, 34-71.
    • (1995) Methods Enzymol , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 111
    • 0037379159 scopus 로고    scopus 로고
    • Analyses of circular dichroism spectra of membrane proteins
    • Wallace, B. A.; Lees, J. G.; Orry, A. J.; Lobley, A.; Janes, R. W. Analyses of circular dichroism spectra of membrane proteins. Protein Sci., 2003, 12, 875-884.
    • (2003) Protein Sci , vol.12 , pp. 875-884
    • Wallace, B.A.1    Lees, J.G.2    Orry, A.J.3    Lobley, A.4    Janes, R.W.5
  • 112
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Wu, Y.; Huang, H. W.; Olah, G. A. Method of oriented circular dichroism. Biophys. J., 1990, 57, 797-806.
    • (1990) Biophys. J , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 113
    • 77951093826 scopus 로고    scopus 로고
    • Impact of the antimicrobial peptide Novicidin on membrane structure and integrity
    • Nielsen, S. B.; Otzen, D. E. Impact of the antimicrobial peptide Novicidin on membrane structure and integrity. J. Colloid. Interface Sci., 2010.
    • (2010) J. Colloid. Interface Sci
    • Nielsen, S.B.1    Otzen, D.E.2
  • 114
    • 58949093974 scopus 로고    scopus 로고
    • Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs
    • Cheng, J. T.; Hale, J. D.; Elliot, M.; Hancock, R. E.; Straus, S. K. Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs. Biophys. J., 2009, 96, 552-565.
    • (2009) Biophys. J. , vol.96 , pp. 552-565
    • Cheng, J.T.1    Hale, J.D.2    Elliot, M.3    Hancock, R.E.4    Straus, S.K.5
  • 115
    • 0032510799 scopus 로고    scopus 로고
    • Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment
    • Karle, I. L.; Perozzo, M. A.; Mishra, V. K.; Balaram, P. Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment. Proc. Natl. Acad. Sci. USA, 1998, 95, 5501-5504.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5501-5504
    • Karle, I.L.1    Perozzo, M.A.2    Mishra, V.K.3    Balaram, P.4
  • 116
    • 33751545243 scopus 로고    scopus 로고
    • Crystal structures of human alpha-defensins HNP4, HD5, and HD6
    • Szyk, A.; Wu, Z.; Tucker, K.; Yang, D.; Lu, W.; Lubkowski, J. Crystal structures of human alpha-defensins HNP4, HD5, and HD6. Protein Sci., 2006, 15, 2749-2760.
    • (2006) Protein Sci , vol.15 , pp. 2749-2760
    • Szyk, A.1    Wu, Z.2    Tucker, K.3    Yang, D.4    Lu, W.5    Lubkowski, J.6
  • 117
    • 33748940257 scopus 로고    scopus 로고
    • Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering
    • Salditt, T.; Li, C.; Spaar, A. Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering. Biochim. Biophys. Acta., 2006, 1758, 1483-1498.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1483-1498
    • Salditt, T.1    Li, C.2    Spaar, A.3
  • 119
    • 67650021498 scopus 로고    scopus 로고
    • A novel heavy-atom label for side-specific peptide iodination: Synthesis, membrane incorporation and X-ray reflectivity
    • Schneggenburger, P. E.; Beerlink, A.; Worbs, B.; Salditt, T.; Diederichsen, U. A novel heavy-atom label for side-specific peptide iodination: synthesis, membrane incorporation and X-ray reflectivity. Chemphyschem, 2009, 10, 1567-1576.
    • (2009) Chemphyschem , vol.10 , pp. 1567-1576
    • Schneggenburger, P.E.1    Beerlink, A.2    Worbs, B.3    Salditt, T.4    Diederichsen, U.5
  • 120
    • 36849051354 scopus 로고    scopus 로고
    • Specific and selective peptide-membrane interactions revealed using quartz crystal microbalance
    • Mechler, A.; Praporski, S.; Atmuri, K.; Boland, M.; Separovic, F.; Martin, L. L. Specific and selective peptide-membrane interactions revealed using quartz crystal microbalance. Biophys. J., 2007, 93, 3907-3916.
    • (2007) Biophys. J , vol.93 , pp. 3907-3916
    • Mechler, A.1    Praporski, S.2    Atmuri, K.3    Boland, M.4    Separovic, F.5    Martin, L.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.