메뉴 건너뛰기




Volumn 30, Issue 4, 1997, Pages 365-429

Infrared spectroscopy of proteins and peptides in lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; MEMBRANE PROTEIN; PEPTIDE; PROTEIN; SODIUM CHLORIDE;

EID: 0031402313     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0033583597003375     Document Type: Review
Times cited : (656)

References (253)
  • 1
    • 0030461703 scopus 로고    scopus 로고
    • Peptides modeled on the transmembrane region of the slow voltage-gated IsK potassium channel: Structural characterization of peptide assemblies in the β-strand conformation
    • AGGELI, A., BODEN, N., CHENG, Y.-L., FINDLAY, J. B. C., KNOWLES, P. F., KOVATCHEV, P., TURNBULL, P. J. H., HORVÁTH & MARSH, D. (1996). Peptides modeled on the transmembrane region of the slow voltage-gated IsK potassium channel: structural characterization of peptide assemblies in the β-strand conformation. Biochemistry 35, 16213-16221.
    • (1996) Biochemistry , vol.35 , pp. 16213-16221
    • Aggeli, A.1    Boden, N.2    Cheng, Y.-L.3    Findlay, J.B.C.4    Knowles, P.F.5    Kovatchev, P.6    Turnbull, P.J.H.7    Horvá, T.H.8    Marsh, D.9
  • 2
    • 0010446518 scopus 로고
    • Molecular structure and interaction of dipalmitoyl phosphatidylcholine in multilayers. Comparative study with phosphatidylethanolamine
    • AKUTSU, H., IKEMATSU, M. & KYOGOKU, Y. (1981). Molecular structure and interaction of dipalmitoyl phosphatidylcholine in multilayers. Comparative study with phosphatidylethanolamine. Chem. Phys. Lipids 28, 149-158.
    • (1981) Chem. Phys. Lipids , vol.28 , pp. 149-158
    • Akutsu, H.1    Ikematsu, M.2    Kyogoku, Y.3
  • 3
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodabacter sphaeroides R-26: The protein subunits
    • ALLEN, J. P., FEHER, G., YEATES, T. O., KOMIYA, H. & REES, D. C. (1987). Structure of the reaction center from Rhodabacter sphaeroides R-26: the protein subunits. Proc. Natl. Acad. Sci. USA 84, 6162-6166.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 4
    • 0024787356 scopus 로고
    • Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance
    • ALTENBACH, C., FRONCISZ, W., HYDE, J. S. & HUBBELL, W. L. (1989). Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance. Biophys. J. 56, 1183-1191.
    • (1989) Biophys. J. , vol.56 , pp. 1183-1191
    • Altenbach, C.1    Froncisz, W.2    Hyde, J.S.3    Hubbell, W.L.4
  • 5
    • 0023224412 scopus 로고
    • Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter
    • ALVAREZ, J., LEE, D. C., BALDWIN, S. A. & CHAPMAN, D. (1987). Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter. J. Biol. Chem. 262, 3502-3509.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3502-3509
    • Alvarez, J.1    Lee, D.C.2    Baldwin, S.A.3    Chapman, D.4
  • 8
    • 0029999396 scopus 로고    scopus 로고
    • Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle
    • ARKIN, I. T., RUSS, W. P., LEBENDIKER, M. & SCHULDINER, S. (1996a). Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle. Biochemistry 35, 7233-7238.
    • (1996) Biochemistry , vol.35 , pp. 7233-7238
    • Arkin, I.T.1    Russ, W.P.2    Lebendiker, M.3    Schuldiner, S.4
  • 10
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier transform infrared spectroscopy
    • ARRONDO, J. L. R., MUGA, A., CASTRESANA, J. & GOÑI, F. M. (1993). Quantitative studies of the structure of proteins in solution by Fourier transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59, 23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 11
    • 0000740930 scopus 로고
    • The structural basis of pancreatic amyloid formation: Isotope-edited spectroscopy in the solid state
    • ASHBURN, T. T., AUGER, M. & LANSBURY, JR., P. T. (1992). The structural basis of pancreatic amyloid formation: isotope-edited spectroscopy in the solid state. J. Am. Chem. Soc. 114, 790-791.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 790-791
    • Ashburn, T.T.1    Auger, M.2    Lansbury Jr., P.T.3
  • 13
    • 0030422901 scopus 로고    scopus 로고
    • Orientational order determination by internal reflection infrared spectroscopy
    • AXELSEN, P. H. & CITRA, M. J. (1996). Orientational order determination by internal reflection infrared spectroscopy. Prog. Biophys. molec. Biol. 66, 227-253.
    • (1996) Prog. Biophys. Molec. Biol. , vol.66 , pp. 227-253
    • Axelsen, P.H.1    Citra, M.J.2
  • 14
    • 0028879250 scopus 로고
    • The infrared dichroism of transmembrane helical polypeptides
    • AXELSEN, P. H., KAUFMAN, B. K., MCELHANEY, R. N. & LEWIS, R. N. A. H. (1995b). The infrared dichroism of transmembrane helical polypeptides. Biophys. J. 69, 2770-2781.
    • (1995) Biophys. J. , vol.69 , pp. 2770-2781
    • Axelsen, P.H.1    Kaufman, B.K.2    Mcelhaney, R.N.3    Lewis, R.N.A.H.4
  • 15
    • 0027525503 scopus 로고
    • Biophysical studies of the Pf1 coat protein in the filamentous phage, in detergent micelles, and in a membrane environment
    • AZPIAZU, I., GOMEZ-FERNANDEZ, J. C. & CHAPMAN, D. (1993). Biophysical studies of the Pf1 coat protein in the filamentous phage, in detergent micelles, and in a membrane environment. Biochemistry 32, 10720-10726.
    • (1993) Biochemistry , vol.32 , pp. 10720-10726
    • Azpiazu, I.1    Gomez-Fernandez, J.C.2    Chapman, D.3
  • 16
    • 0023615921 scopus 로고
    • A study of the structure of polymyxin B-dipalmitoylphosphatidyglycerol complexes by vibrational spectroscopy
    • BABIN, Y., D'AMOUR, J., PIGEON, M. & PÉZOLET, M. (1987). A study of the structure of polymyxin B-dipalmitoylphosphatidyglycerol complexes by vibrational spectroscopy. Biochim. Biophys. Acta 903, 78-88.
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 78-88
    • Babin, Y.1    D'Amour, J.2    Pigeon, M.3    Pézolet, M.4
  • 17
    • 0026577319 scopus 로고
    • Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: Characterization by fluorescence and Fourier transform infrared difference spectroscopy
    • BAENZIGER, J. E., MILLER, K. W. & ROTHSCHILD, K. J. (1992). Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopy. Biophys. J. 61, 983-992.
    • (1992) Biophys. J. , vol.61 , pp. 983-992
    • Baenziger, J.E.1    Miller, K.W.2    Rothschild, K.J.3
  • 18
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • BANDEKAR, J. (1992). Amide modes and protein conformation. Biochim. Biophys. Acta 1120, 123-143.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 19
    • 0026030935 scopus 로고
    • Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase
    • BARTH, A., MÄNTELE, W. & KREUTZ, W. (1991). Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase. Biochim. Biophys. Acta 1057, 115-123.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 115-123
    • Barth, A.1    Mäntele, W.2    Kreutz, W.3
  • 20
    • 0028130122 scopus 로고
    • Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FTIR spectroscopy
    • BAUER, H. H., MÜLLER, M., GOETTE, J., MERKLE, H. P. & FRINGELI, U. P. (1994). Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FTIR spectroscopy. Biochemistry 33, 12276-12282.
    • (1994) Biochemistry , vol.33 , pp. 12276-12282
    • Bauer, H.H.1    Müller, M.2    Goette, J.3    Merkle, H.P.4    Fringeli, U.P.5
  • 21
    • 0022373291 scopus 로고
    • Oriented secondary structure in integral membrane proteins. I. Circular dichroism and infrared spectroscopy of cytochrome oxidase in multilamellar films
    • BAZZI, M. & WOODY, R. W. (1985). Oriented secondary structure in integral membrane proteins. I. Circular dichroism and infrared spectroscopy of cytochrome oxidase in multilamellar films. Biophys. J. 48, 957-966.
    • (1985) Biophys. J. , vol.48 , pp. 957-966
    • Bazzi, M.1    Woody, R.W.2
  • 23
    • 0024291319 scopus 로고
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups. Biochemistry 27, 8239-8249.
    • (1988) Biochemistry , vol.27 , pp. 8239-8249
    • Blume, A.1    Hübner, W.2    Messner, G.3
  • 24
    • 0027142557 scopus 로고
    • Solvent history dependence of gramicidin-lipid interactions: A Raman and infrared spectroscopic study
    • BOUCHARD, M. & AUGER, M. (1993). Solvent history dependence of gramicidin-lipid interactions: A Raman and infrared spectroscopic study. Biophys. J. 65, 2484-2492.
    • (1993) Biophys. J. , vol.65 , pp. 2484-2492
    • Bouchard, M.1    Auger, M.2
  • 26
    • 0023776215 scopus 로고
    • Fourier transform infrared techniques for probing membrane protein structure
    • BRAIMAN, M. S. & ROTHSCHILD, K. J. (1988). Fourier transform infrared techniques for probing membrane protein structure. Ann. Rev. Biophys. Biophys. Chem. 17, 541-570.
    • (1988) Ann. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 541-570
    • Braiman, M.S.1    Rothschild, K.J.2
  • 27
    • 0023657247 scopus 로고
    • Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and δ-hemolysin with phosphatidylcholines
    • BRAUNER, J. W., MENDELSOHN, R. & PRENDERGAST, F. G. (1987). Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and δ-hemolysin with phosphatidylcholines. Biochemistry 26, 8151-8158.
    • (1987) Biochemistry , vol.26 , pp. 8151-8158
    • Brauner, J.W.1    Mendelsohn, R.2    Prendergast, F.G.3
  • 29
    • 0022475473 scopus 로고
    • Conformations of signal peptides induced by lipids suggest initial steps in protein export
    • BRIGGS, M. S., CORNELL, D. G., DLUHY, R. A. & GIERASCH, L. M. (1986). Conformations of signal peptides induced by lipids suggest initial steps in protein export. Science 233, 206-208.
    • (1986) Science , vol.233 , pp. 206-208
    • Briggs, M.S.1    Cornell, D.G.2    Dluhy, R.A.3    Gierasch, L.M.4
  • 30
    • 0030053808 scopus 로고    scopus 로고
    • The effect of increasing membrane curvature on the phase transition and mixing behavior of a dimyristoyl-sn-glycero-3-phosphatidylcholine/distearoyl-sn-glycero-3- phosphatidylcholine lipid mixture, as studied by Fourier transform infrared spectroscopy and differential scanning calorimetry
    • BRUMM, T., JORGENSEN, K., MOURITSEN, D. G. & BAYERL, T. M. (1996). The effect of increasing membrane curvature on the phase transition and mixing behavior of a dimyristoyl-sn-glycero-3-phosphatidylcholine/distearoyl-sn-glycero-3- phosphatidylcholine lipid mixture, as studied by Fourier transform infrared spectroscopy and differential scanning calorimetry. Biophys. J. 70, 1373-1379.
    • (1996) Biophys. J. , vol.70 , pp. 1373-1379
    • Brumm, T.1    Jorgensen, K.2    Mouritsen, D.G.3    Bayerl, T.M.4
  • 32
    • 85025725092 scopus 로고
    • Cholesterol-lipid interactions: An infrared and Raman spectroscopic study of the carbonyl stretching mode region of 1,2-dipalmitoyl phosphatidylcholine bilayers
    • BUSH, S. F., LEVIN, H. & LEVIN, I. W. (1980). Cholesterol-lipid interactions: An infrared and Raman spectroscopic study of the carbonyl stretching mode region of 1,2-dipalmitoyl phosphatidylcholine bilayers. Chem. Phys. Lipids 27, 101-111.
    • (1980) Chem. Phys. Lipids , vol.27 , pp. 101-111
    • Bush, S.F.1    Levin, H.2    Levin, I.W.3
  • 33
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • BYLER, D. M. & SUSI, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 35
    • 0019317514 scopus 로고
    • Characterization of the pretransition in 1,2-dipalmitoyl-sn-glycero-3-phosphocholine by Fourier transform infrared spectroscopy
    • CAMERON, D. G., CASAL, H. L. & MANTSCH, H. H. (1980). Characterization of the pretransition in 1,2-dipalmitoyl-sn-glycero-3-phosphocholine by Fourier transform infrared spectroscopy. Biochemistry 19, 3665-3672.
    • (1980) Biochemistry , vol.19 , pp. 3665-3672
    • Cameron, D.G.1    Casal, H.L.2    Mantsch, H.H.3
  • 36
    • 0021755229 scopus 로고
    • Polymorphic phase behavior of phospholipid membranes studied by infrared spectroscopy
    • CASAL, H. L. & MANTSCH, H. H. (1984). Polymorphic phase behavior of phospholipid membranes studied by infrared spectroscopy. Biochim. Biophys. Acta 779, 381-401.
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 381-401
    • Casal, H.L.1    Mantsch, H.H.2
  • 40
    • 0028301765 scopus 로고
    • Infrared study of the bilayer stability behavior of binary and ternary phospholipid mixtures containing unsaturated phosphatidylethanolamine
    • CHENG, K. H. (1994). Infrared study of the bilayer stability behavior of binary and ternary phospholipid mixtures containing unsaturated phosphatidylethanolamine. Chem. Phys. Lipids 70, 43-51.
    • (1994) Chem. Phys. Lipids , vol.70 , pp. 43-51
    • Cheng, K.H.1
  • 41
    • 0012504280 scopus 로고
    • 2 wagging modes of unsaturated acyl chains as IR probes of conformational order in methyl alkenoates and phospholipld bilayers
    • 2 wagging modes of unsaturated acyl chains as IR probes of conformational order in methyl alkenoates and phospholipld bilayers. J. Phys. Chem. 96, 10543-10547.
    • (1992) J. Phys. Chem. , vol.96 , pp. 10543-10547
    • Chia, N.-C.1    Mendelsohn, R.2
  • 42
    • 0022919895 scopus 로고
    • Structural basis of human erythrocyte glucose transporter function in reconstituted vesicles
    • CHIN, J. J., JUNG, E. K. Y. & JUNG, C. Y. (1986). Structural basis of human erythrocyte glucose transporter function in reconstituted vesicles. J. Biol. Chem. 261, 7101-7104.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7101-7104
    • Chin, J.J.1    Jung, E.K.Y.2    Jung, C.Y.3
  • 43
    • 0026658402 scopus 로고
    • Alcohols dehydrate lipid membranes: An infrared study on hydrogen bonding
    • CHIOU, J.-S., KRISHNA, P. R., KAMAYA, H. & UEDA, I. (1992). Alcohols dehydrate lipid membranes: an infrared study on hydrogen bonding. Biochim. Biophys. Acta 1110, 225-233.
    • (1992) Biochim. Biophys. Acta , vol.1110 , pp. 225-233
    • Chiou, J.-S.1    Krishna, P.R.2    Kamaya, H.3    Ueda, I.4
  • 44
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • CHIRGADZE, YU. N., FEDOROV, O. V. & TRUSHINA, N. P. (1975). Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers 14, 679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.U.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 45
    • 0015904265 scopus 로고
    • Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms
    • CHIRGADZE, YU. N., SHESTOPALOV, B. V. & VENYAMINOV, S. YU. (1973). Intensities and other spectral parameters of infrared amide bands of polypeptides in the β-and random forms. Biopolymers 12, 1337-1351.
    • (1973) Biopolymers , vol.12 , pp. 1337-1351
    • Chirgadze, Y.U.N.1    Shestopalov, B.V.2    Venyaminov, S.Y.U.3
  • 46
    • 0016290132 scopus 로고
    • Intensities and other spectral parameters of infrared amide bands of polypeptides in the α-helical form
    • CHIRGADZE, YU. N. & BRAZHNIKOV, E. V. (1974). Intensities and other spectral parameters of infrared amide bands of polypeptides in the α-helical form. Biopolymers 13, 1701-1712.
    • (1974) Biopolymers , vol.13 , pp. 1701-1712
    • Chirgadze, Y.U.N.1    Brazhnikov, E.V.2
  • 47
    • 0028968127 scopus 로고
    • Interaction of cytochrome c with cardiolipin: An infrared spectroscopic study
    • CHOI, S. & SWANSON, J. M. (1995). Interaction of cytochrome c with cardiolipin: an infrared spectroscopic study. Biophys. Chem. 54, 271-278.
    • (1995) Biophys. Chem. , vol.54 , pp. 271-278
    • Choi, S.1    Swanson, J.M.2
  • 48
    • 0026095096 scopus 로고
    • Infrared spectroscopic studies on the phosphatidylserine bilayer interacting with calcium ions: Effect of cholesterol
    • CHOI, S., WARE, W., JR., LAUTERBACH, S. R. & PHILLIPS, W. M. (1991). Infrared spectroscopic studies on the phosphatidylserine bilayer interacting with calcium ions: Effect of cholesterol. Biochemistry 30, 8563-8568.
    • (1991) Biochemistry , vol.30 , pp. 8563-8568
    • Choi, S.1    Ware Jr., W.2    Lauterbach, S.R.3    Phillips, W.M.4
  • 49
    • 0029818018 scopus 로고    scopus 로고
    • Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy
    • CITRA, M. J. & AXELSEN, P. H. (1996). Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy. Biophys. J. 71, 1796-1805.
    • (1996) Biophys. J. , vol.71 , pp. 1796-1805
    • Citra, M.J.1    Axelsen, P.H.2
  • 50
    • 0018851718 scopus 로고
    • Surface induced lamellar orientation of multilayer membrane arrays: Theoretical analysis and a new method with application to purple membrane fragments
    • CLARK, N. A., ROTHSCHILD, K. J., LUIPPOLD, D., & SIMONS, B. (1980). Surface induced lamellar orientation of multilayer membrane arrays: theoretical analysis and a new method with application to purple membrane fragments. Biophys. J. 31, 65-95.
    • (1980) Biophys. J. , vol.31 , pp. 65-95
    • Clark, N.A.1    Rothschild, K.J.2    Luippold, D.3    Simons, B.4
  • 51
    • 0028016112 scopus 로고
    • Use of an oriented transmembrane protein to probe the assembly of a supported phospholipid bilayer
    • CONTINO, P. B., HASSELBACHER, C. A., ROSS, J. B. A. & NEMERSON, Y. (1994). Use of an oriented transmembrane protein to probe the assembly of a supported phospholipid bilayer. Biophys. J. 67, 1113-1116.
    • (1994) Biophys. J. , vol.67 , pp. 1113-1116
    • Contino, P.B.1    Hasselbacher, C.A.2    Ross, J.B.A.3    Nemerson, Y.4
  • 52
    • 0024518247 scopus 로고
    • Conformations and orientations of a signal peptide interacting with phospholipid monolayers
    • CORNELL, D. G., DLUHY, R. A., BRIGGS, M. S., MCKNIGHT, C. J. & GIERASCH, L. M. (1989). Conformations and orientations of a signal peptide interacting with phospholipid monolayers. Biochemistry 28, 2789-2797.
    • (1989) Biochemistry , vol.28 , pp. 2789-2797
    • Cornell, D.G.1    Dluhy, R.A.2    Briggs, M.S.3    Mcknight, C.J.4    Gierasch, L.M.5
  • 55
    • 0001006658 scopus 로고
    • Interaction of a synthetic amphiphilic polypeptide and lipids in a bilayer structure
    • DAVIS, J. H., CLARE, D. M., HODGES, R. S. & BLOOM, M. (1983). Interaction of a synthetic amphiphilic polypeptide and lipids in a bilayer structure. Biochemistry 22, 5298-5305.
    • (1983) Biochemistry , vol.22 , pp. 5298-5305
    • Davis, J.H.1    Clare, D.M.2    Hodges, R.S.3    Bloom, M.4
  • 56
    • 0026621340 scopus 로고
    • Characterization by infrared spectroscopy of the interaction of a cardiotoxin with phosphatidic acid and with binary mixtures of phosphatidic acid and phosphatidylcholine
    • DÉSORMEAUX, A., LAROCHE, G., BOUGIS, P. E. & PÉZOLET, M. (1992). Characterization by infrared spectroscopy of the interaction of a cardiotoxin with phosphatidic acid and with binary mixtures of phosphatidic acid and phosphatidylcholine. Biochemistry 31, 12173-12182.
    • (1992) Biochemistry , vol.31 , pp. 12173-12182
    • Désormeaux, A.1    Laroche, G.2    Bougis, P.E.3    Pézolet, M.4
  • 57
    • 0029792683 scopus 로고    scopus 로고
    • Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activity
    • DIBBLE, A. R. G., HINDERLITER, A. K., SANDO, J. J. & BILTONEN, R. L. (1996). Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activity. Biophys. J. 71, 1877-1890.
    • (1996) Biophys. J. , vol.71 , pp. 1877-1890
    • Dibble, A.R.G.1    Hinderliter, A.K.2    Sando, J.J.3    Biltonen, R.L.4
  • 58
    • 0003874177 scopus 로고
    • Fourier transform infrared spectroscopic studies of the effect of calcium ions on phosphatidylserine
    • DLUHY, R. A., CAMERON, D. G., MANTSCH, H. H. & MENDELSOHN, R. (1983). Fourier transform infrared spectroscopic studies of the effect of calcium ions on phosphatidylserine. Biochemistry 22, 6318-6325.
    • (1983) Biochemistry , vol.22 , pp. 6318-6325
    • Dluhy, R.A.1    Cameron, D.G.2    Mantsch, H.H.3    Mendelsohn, R.4
  • 59
    • 0001339089 scopus 로고
    • Characterization of cooperative conformational transitions by Fourier transform infrared spectroscopy: Application to phospholipid binary mixtures
    • DLUHY, R. A., MOFFATT, D., CAMERON, D. G., MENDELSOHN, R. & MANTSCH, H. H. (1985). Characterization of cooperative conformational transitions by Fourier transform infrared spectroscopy: application to phospholipid binary mixtures. Can. J. Chem. 63, 1925-1932.
    • (1985) Can. J. Chem. , vol.63 , pp. 1925-1932
    • Dluhy, R.A.1    Moffatt, D.2    Cameron, D.G.3    Mendelsohn, R.4    Mantsch, H.H.5
  • 60
    • 0024832191 scopus 로고
    • Infrared spectroscopic investigations of pulmonary surfactant. Surface film transitions at the air-water interface and bulk phase thermotropism
    • DLUHY, R. A., REILLY, K. E., HUNT, R. D., MITCHELL, M. L., MAUTONE, A. J. & MENDELSOHN, R. (1989). Infrared spectroscopic investigations of pulmonary surfactant. Surface film transitions at the air-water interface and bulk phase thermotropism. Biophys. J. 56, 1173-1181.
    • (1989) Biophys. J. , vol.56 , pp. 1173-1181
    • Dluhy, R.A.1    Reilly, K.E.2    Hunt, R.D.3    Mitchell, M.L.4    Mautone, A.J.5    Mendelsohn, R.6
  • 61
    • 4243971422 scopus 로고
    • Vibrational spectroscopy of biophysical monolayers. Applications of IR and Raman spectroscopy to biomembrane model systems at interfaces
    • DLUHY, R. A., STEPHENS, S. A., WIDAYATI, S. & WILLIAMS, A. D. (1995). Vibrational spectroscopy of biophysical monolayers. Applications of IR and Raman spectroscopy to biomembrane model systems at interfaces. Spectrochim. Acta Part A 51, 1413-1447.
    • (1995) Spectrochim. Acta Part A , vol.51 , pp. 1413-1447
    • Dluhy, R.A.1    Stephens, S.A.2    Widayati, S.3    Williams, A.D.4
  • 62
    • 0024997389 scopus 로고
    • Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods
    • DOUSSEAU, F. & PÉZOLET, M. (1990). Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods. Biochemistry 29, 8771-8779.
    • (1990) Biochemistry , vol.29 , pp. 8771-8779
    • Dousseau, F.1    Pézolet, M.2
  • 63
    • 0022968813 scopus 로고
    • Infrared spectroscopic study of photoreceptor membrane and purple membrane
    • DOWNER, N. W., BRUCHMAN, T. J. & HAZZARD, J. H. (1986). Infrared spectroscopic study of photoreceptor membrane and purple membrane. J. Biol. Chem. 261, 3640-3647.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3640-3647
    • Downer, N.W.1    Bruchman, T.J.2    Hazzard, J.H.3
  • 64
    • 0000439352 scopus 로고
    • Optical constants of water in the infrared
    • DOWNING, H. D. & WILLIAMS, D. (1975). Optical constants of water in the infrared. J. Geophys. Res. 80, 1656-1661.
    • (1975) J. Geophys. Res. , vol.80 , pp. 1656-1661
    • Downing, H.D.1    Williams, D.2
  • 65
    • 0030010945 scopus 로고    scopus 로고
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region. J. Biol. Chem. 271, 13417-13421.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3    Corti, C.4    Glück Vorrherr, T.5    Brunner, J.6
  • 66
    • 0025608693 scopus 로고
    • Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange
    • EARNEST, T. N., HERZFELD, J. & ROTHSCHILD, K. J. (1990). Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. Biophys. J. 58, 1539-1546.
    • (1990) Biophys. J. , vol.58 , pp. 1539-1546
    • Earnest, T.N.1    Herzfeld, J.2    Rothschild, K.J.3
  • 67
    • 0030611604 scopus 로고    scopus 로고
    • Integrin αIIbβ3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding
    • ERB, E.-M., TANGEMANN, K., BOHRMANN, B., MÜLLER, B. & ENGEL, J. (1997). Integrin αIIbβ3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. Biochemistry 36, 7395-7402.
    • (1997) Biochemistry , vol.36 , pp. 7395-7402
    • Erb, E.-M.1    Tangemann, K.2    Bohrmann, B.3    Müller, B.4    Engel, J.5
  • 68
    • 0023646689 scopus 로고
    • Membrane structure of bombesin studied by infrared spectroscopy. Prediction of membrane interactions of gastrin-releasing peptide, neuromedinB, and neuromedin C
    • ERNE, D. & SCHWYZER, R. (1987). Membrane structure of bombesin studied by infrared spectroscopy. Prediction of membrane interactions of gastrin-releasing peptide, neuromedinB, and neuromedin C. Biochemistry 26, 6316-6319.
    • (1987) Biochemistry , vol.26 , pp. 6316-6319
    • Erne, D.1    Schwyzer, R.2
  • 69
    • 0021925404 scopus 로고
    • Preferred conformation, orientation, and accumulation of dynorphin A-(1-13)-tridecapeptide on the surface of neutral lipid membranes
    • ERNE, D., SARGENT, D. F., & SCHWYZER, R. (1985). Preferred conformation, orientation, and accumulation of dynorphin A-(1-13)-tridecapeptide on the surface of neutral lipid membranes. Biochemistry 24, 4261-4263.
    • (1985) Biochemistry , vol.24 , pp. 4261-4263
    • Erne, D.1    Sargent, D.F.2    Schwyzer, R.3
  • 70
    • 0027336894 scopus 로고
    • A new infrared spectroscopic marker for cochleate phases in phosphatidylserine-containing model membranes
    • FLACH, C. R. & MENDELSOHN, R. (1993). A new infrared spectroscopic marker for cochleate phases in phosphatidylserine-containing model membranes. Biophys. J. 64, 1113-1121.
    • (1993) Biophys. J. , vol.64 , pp. 1113-1121
    • Flach, C.R.1    Mendelsohn, R.2
  • 71
    • 0027448842 scopus 로고
    • Calcium ion interactions with insoluble phospholipid monolayer films at the A/W interface. External reflection-absorption IR studies
    • FLACH, C. R., BRAUNER, J. W. & MENDELSOHN, R. (1993). Calcium ion interactions with insoluble phospholipid monolayer films at the A/W interface. External reflection-absorption IR studies. Biophys. J. 65, 1994-2001.
    • (1993) Biophys. J. , vol.65 , pp. 1994-2001
    • Flach, C.R.1    Brauner, J.W.2    Mendelsohn, R.3
  • 72
    • 0028237335 scopus 로고
    • External reflection FTIR of peptide monolayer films in situ at the air/water interface: Experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange
    • FLACH, C. R., BRAUNER, J. W., TAYLOR, J. W., BALDWIN, R. C. & MENDELSOHN, R. (1994). External reflection FTIR of peptide monolayer films in situ at the air/water interface: Experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange. Biophys. J. 67, 402-410.
    • (1994) Biophys. J. , vol.67 , pp. 402-410
    • Flach, C.R.1    Brauner, J.W.2    Taylor, J.W.3    Baldwin, R.C.4    Mendelsohn, R.5
  • 73
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
    • FOX, JR., R. O. & RICHARDS, F. M. (1982). A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution. Nature 330, 325-330.
    • (1982) Nature , vol.330 , pp. 325-330
    • Fox Jr., R.O.1    Richards, F.M.2
  • 74
    • 0343854556 scopus 로고
    • A quantitative study of the Amide I vibrations in the infra-red spectrum of β-keratin
    • FRASER, R. D. B. & SUZUKI, E. (1970). A quantitative study of the Amide I vibrations in the infra-red spectrum of β-keratin. Spectrochim. Acta 26A, 426-428.
    • (1970) Spectrochim. Acta , vol.26 A , pp. 426-428
    • Fraser, R.D.B.1    Suzuki, E.2
  • 76
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • FREY, S. & TAMM, L. K. (1991). Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys J. 60, 922-930.
    • (1991) Biophys J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 77
    • 0000913232 scopus 로고
    • In situ infrared attenuated total reflection membrane spectroscopy
    • F. M. Mirabella, Jr. (Ed.) Marcel Dekker, Inc.: New York
    • FRINGELI, U. P. (1993). In situ infrared attenuated total reflection membrane spectroscopy. In Internal Reflection Spectroscopy, Theory and Applications. F. M. Mirabella, Jr. (Ed.) Marcel Dekker, Inc.: New York, pp. 255-324.
    • (1993) Internal Reflection Spectroscopy, Theory and Applications , pp. 255-324
    • Fringeli, U.P.1
  • 78
    • 0346481826 scopus 로고
    • Pore formation in lipid membranes by alamethicin
    • FRINGELI, U. P. & FRINGELI, M. (1979). Pore formation in lipid membranes by alamethicin. Proc. Natl. Acad. Sci. USA 76, 3852-3856.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3852-3856
    • Fringeli, U.P.1    Fringeli, M.2
  • 79
    • 0019479713 scopus 로고
    • Infrared membrane spectroscopy
    • (ed. E. Grell), Berlin: Springer-Verlag
    • FRINGELI, U. P. & GÜNTHARD, H. H. (1981). Infrared membrane spectroscopy. In Membrane Spectroscopy (ed. E. Grell), pp. 270-332. Berlin: Springer-Verlag.
    • (1981) Membrane Spectroscopy , pp. 270-332
    • Fringeli, U.P.1    Günthard, H.H.2
  • 80
    • 0024451546 scopus 로고
    • +-ATPase studied by attenuated total reflection spectroscopy. Biochim. biophys
    • +-ATPase studied by attenuated total reflection spectroscopy. Biochim. biophys. Acta 984, 301-312.
    • (1989) Acta , vol.984 , pp. 301-312
    • Fringeli, U.P.1    Apell, H.-J.2    Fringeli, M.3    Lauger, P.4
  • 81
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • GAZIT, E., MILLER, I. R., BIGGIN, P. C., SANSOM, M. S. P. & SHAI, Y. (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
  • 82
    • 0000541570 scopus 로고    scopus 로고
    • Characterization of biological samples by two-dimensional infrared spectroscopy: Simulation of frequency, bandwidth, and intensity changes
    • GERICKE, A., GADALETA, S. J., BRAUNER, J. W. & MENDELSOHN, R. (1996). Characterization of biological samples by two-dimensional infrared spectroscopy: simulation of frequency, bandwidth, and intensity changes. Biospectroscopy 2, 341-351.
    • (1996) Biospectroscopy , vol.2 , pp. 341-351
    • Gericke, A.1    Gadaleta, S.J.2    Brauner, J.W.3    Mendelsohn, R.4
  • 83
    • 0031006190 scopus 로고    scopus 로고
    • Structure and orientation of lung surfactant SP-C and L-α-dipalmitoylphosphatidylcholine in aqueous monolayers. Biophys
    • GERICKE, A., FLACH, C. R. & MENDELSOHN, R. (1997). Structure and orientation of lung surfactant SP-C and L-α-dipalmitoylphosphatidylcholine in aqueous monolayers. Biophys. J. 73, 492-499.
    • (1997) J. , vol.73 , pp. 492-499
    • Gericke, A.1    Flach, C.R.2    Mendelsohn, R.3
  • 84
    • 0024963567 scopus 로고
    • Signal sequences
    • GIERASCH, L. M. (1989). Signal sequences. Biochemistry 28, 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 85
    • 0003039141 scopus 로고
    • Polarized attenuated total reflection infrared spectroscopy as a tool to investigate the conformation and orientation of membrane components
    • (ed. R. Brasseur), (Chapter 1.B.3). Boca Raton, FL: CRC Press
    • GOORMAGHTIGH, E. & RUYSSCHAERT, J.-M. (1990). Polarized attenuated total reflection infrared spectroscopy as a tool to investigate the conformation and orientation of membrane components. In Molecular Description of Biological Membranes by Computer-Aided Conformational Analysis (ed. R. Brasseur), pp. 285-329 (Chapter 1.B.3). Boca Raton, FL: CRC Press.
    • (1990) Molecular Description of Biological Membranes by Computer-Aided Conformational Analysis , pp. 285-329
    • Goormaghtigh, E.1    Ruysschaert, J.-M.2
  • 86
    • 0026082895 scopus 로고
    • Secondary structure and orientation of the amphipathic peptide GALA in lipid structures. An infrared-spectroscopic approach
    • GOORMAGHTIGH, E., DE MEUTTER, J., SZOKA, F., CABIAUX, V., PARENTE, R. A. & RUYSSCHAERT, J.-M. (1991a). Secondary structure and orientation of the amphipathic peptide GALA in lipid structures. An infrared-spectroscopic approach. Eur. J. Biochem. 195, 421-429.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 421-429
    • Goormaghtigh, E.1    De Meutter, J.2    Szoka, F.3    Cabiaux, V.4    Parente, R.A.5    Ruysschaert, J.-M.6
  • 87
    • 0026322330 scopus 로고
    • Secondary structure of the membrane-bound form of the pore-forming domain of colicin A. An attenuated total-reflection polarized Fourier-transform infrared spectroscopy study
    • GOORMAGHTIGH, E., VIGNERON, L., KNIBIEHLER, M., LAZDUNSKI, C. & RUYSSCHAERT, J.-M. (1991b). Secondary structure of the membrane-bound form of the pore-forming domain of colicin A. An attenuated total-reflection polarized Fourier-transform infrared spectroscopy study. Eur. J. Biochem. 202, 1299-1305.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1299-1305
    • Goormaghtigh, E.1    Vigneron, L.2    Knibiehler, M.3    Lazdunski, C.4    Ruysschaert, J.-M.5
  • 88
    • 0027298811 scopus 로고
    • Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy
    • GOORMAGHTIGH, E., CABIAUX, V., DE MEUTTER, J., ROSSENEU, M. & RUYSSCHAERT, J.-M. (1993). Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy. Biochemistry 32, 6104-6110.
    • (1993) Biochemistry , vol.32 , pp. 6104-6110
    • Goormaghtigh, E.1    Cabiaux, V.2    De Meutter, J.3    Rosseneu, M.4    Ruysschaert, J.-M.5
  • 89
    • 0000582632 scopus 로고
    • Determinate of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds. II. Experimental aspects, side chain structure, and H/D exchange. III. Secondary structures
    • (ed. H. J. Hilderson and G. B. Ralston), (Chapters 8-10). New York: Plenum Press
    • GOORMAGHTIGH, E., CABIAUX, V. & RUYSSCHAERT, J.-M. (1994). Determinate of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds. II. Experimental aspects, side chain structure, and H/D exchange. III. Secondary structures. In Subcellular Biochemistry, Volume 23: Physicochemical Methods in the Study of Biomembranes (ed. H. J. Hilderson and G. B. Ralston), pp. 329-450 (Chapters 8-10). New York: Plenum Press.
    • (1994) Subcellular Biochemistry, Volume 23: Physicochemical Methods in the Study of Biomembranes , vol.23 , pp. 329-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 90
    • 0027954627 scopus 로고
    • The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures
    • GÖRNE-TSCHELNOKOW, U., STRECKER, A., KADUK, C., NAUMANN, D. & HUCHO, F. (1994). The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures. EMBO J. 13, 338-341.
    • (1994) EMBO J. , vol.13 , pp. 338-341
    • Görne-Tschelnokow, U.1    Strecker, A.2    Kaduk, C.3    Naumann, D.4    Hucho, F.5
  • 91
    • 0030670258 scopus 로고    scopus 로고
    • The effects of chainlength and thermal denaturation on helix-forming peptides: A mode-specific analysis using 2D FT-IR
    • GRAFF, D. F., PASTRANA-RIOS, B., VENYAMINOV, S. YU. & PRENDERGAST, F. G. (1997). The effects of chainlength and thermal denaturation on helix-forming peptides: a mode-specific analysis using 2D FT-IR. J. Am. Chem. Soc. 119, 11282-11294.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11282-11294
    • Graff, D.F.1    Pastrana-Rios, B.2    Venyaminov, S.Y.U.3    Prendergast, F.G.4
  • 92
    • 0030768271 scopus 로고    scopus 로고
    • Structural studies on membrane-embedded influenza hemagglutinin and its fragments
    • GRAY, C. & TAMM, L. K. (1997). Structural studies on membrane-embedded influenza hemagglutinin and its fragments. Protein Science 6, 1993-2006.
    • (1997) Protein Science , vol.6 , pp. 1993-2006
    • Gray, C.1    Tamm, L.K.2
  • 93
    • 0030012221 scopus 로고    scopus 로고
    • Effect of the N-terminal glycine on the secondary structure, orientation and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers
    • GRAY, C., TATULIAN, S. A., WHARTON, S. A. & TAMM, L. K. (1996). Effect of the N-terminal glycine on the secondary structure, orientation and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophys. J. 70, 2275-2286.
    • (1996) Biophys. J. , vol.70 , pp. 2275-2286
    • Gray, C.1    Tatulian, S.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 94
    • 0025783945 scopus 로고
    • Hydration of phosphatidylcholine reverse micelles and multilayers - An infrared spectroscopic study
    • GRDADOLNIK, J., KIDRIC, J. & HADZI, D. (1991). Hydration of phosphatidylcholine reverse micelles and multilayers - an infrared spectroscopic study. Chem. Phys. Lipids 59, 67-68.
    • (1991) Chem. Phys. Lipids , vol.59 , pp. 67-68
    • Grdadolnik, J.1    Kidric, J.2    Hadzi, D.3
  • 95
    • 0021115856 scopus 로고
    • Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • GREMLICH, H.-U., FRINGELI, U.-P. & SCHWYZER, R. (1983). Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry 22, 4257-4264.
    • (1983) Biochemistry , vol.22 , pp. 4257-4264
    • Gremlich, H.-U.1    Fringeli, U.-P.2    Schwyzer, R.3
  • 96
    • 0021327175 scopus 로고
    • Interaction of adrenocorticotrophin-(11-24)-tetradecapeptide with neutral lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • GREMLICH, H.-U., FRINGELI, U.-P. & SCHWYZER, R. (1984). Interaction of adrenocorticotrophin-(11-24)-tetradecapeptide with neutral lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry 23, 1808-1810.
    • (1984) Biochemistry , vol.23 , pp. 1808-1810
    • Gremlich, H.-U.1    Fringeli, U.-P.2    Schwyzer, R.3
  • 97
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • GRIGORIEFF, N., CESKA, T. A., DOWNING, K. H., BALDWIN, J. M. & HENDERSON, R. (1996). Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 99
    • 0024291269 scopus 로고
    • Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin. Biochim
    • HARIS, P. I. & CHAPMAN, D. (1988). Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin. Biochim. Biophys. Acta 943, 375-380.
    • (1988) Biophys. Acta , vol.943 , pp. 375-380
    • Haris, P.I.1    Chapman, D.2
  • 100
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • HARIS, P. I. & CHAPMAN, D. (1995). The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers (Peptide Science) 37, 251-263.
    • (1995) Biopolymers (Peptide Science) , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 101
    • 0024564561 scopus 로고
    • Fourier transform infrared spectroscopic investigation of rhodopsin structure and its comparison with bacteriorhodopsin
    • HARIS, P. I., COKE, M. & CHAPMAN, D. (1989). Fourier transform infrared spectroscopic investigation of rhodopsin structure and its comparison with bacteriorhodopsin. Biochim. Biophys. Acta 995, 160-167.
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 160-167
    • Haris, P.I.1    Coke, M.2    Chapman, D.3
  • 102
    • 0028029151 scopus 로고
    • Studies of the pore forming domain of a voltage-gated potassium channel protein
    • HARIS, P. I., RAMESH, B., SANSOM, M. S. P., KERR, I. D., SRAI, K. S. & CHAPMAN, D. (1994). Studies of the pore forming domain of a voltage-gated potassium channel protein. Prot. Eng. 7, 255-262.
    • (1994) Prot. Eng. , vol.7 , pp. 255-262
    • Haris, P.I.1    Ramesh, B.2    Sansom, M.S.P.3    Kerr, I.D.4    Srai, K.S.5    Chapman, D.6
  • 104
    • 0027145627 scopus 로고
    • Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: An FTIR study
    • HEIMBURG, T. & MARSH, D. (1993). Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. Biophys. J. 65, 2408-2417.
    • (1993) Biophys. J. , vol.65 , pp. 2408-2417
    • Heimburg, T.1    Marsh, D.2
  • 105
    • 0030019825 scopus 로고    scopus 로고
    • Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of Type III intermediate filament proteins
    • HEIMBURG, T., SCHUENEMANN, J., WEBER, K. & GEISLER, N. (1996). Specific recognition of coiled coils by infrared spectroscopy: analysis of the three structural domains of Type III intermediate filament proteins. Biochemistry 35, 1375-1382.
    • (1996) Biochemistry , vol.35 , pp. 1375-1382
    • Heimburg, T.1    Schuenemann, J.2    Weber, K.3    Geisler, N.4
  • 107
    • 0028043265 scopus 로고
    • Reconstitution of membrane fusion sites: A total internal reflection fluorescence microscopy study of influenza hemagglutinin-mediated membrane fusion
    • HINTERDORFER, P., BABER, G. & TAMM, L. K. (1994). Reconstitution of membrane fusion sites: a total internal reflection fluorescence microscopy study of influenza hemagglutinin-mediated membrane fusion. J. Biol. Chem. 269, 20360-20368.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20360-20368
    • Hinterdorfer, P.1    Baber, G.2    Tamm, L.K.3
  • 108
    • 0025922973 scopus 로고
    • 13C=O labeled phosphatidylcholine multilayers from polarized attenuated total reflection FT-IR spectroscopy
    • 13C=O labeled phosphatidylcholine multilayers from polarized attenuated total reflection FT-IR spectroscopy. Biophys. J. 59, 1261-1272.
    • (1991) Biophys. J. , vol.59 , pp. 1261-1272
    • Hübner, W.1    Mantsch, H.H.2
  • 109
    • 0028118681 scopus 로고
    • Conformation of phosphatidylserine in bilayers as studied by Fourier transform infrared spectroscopy
    • HÜBNER, W., MANTSCH, H. H., PALTAUF, F. & HAUSER, H. (1994). Conformation of phosphatidylserine in bilayers as studied by Fourier transform infrared spectroscopy. Biochemistry 33, 320-326.
    • (1994) Biochemistry , vol.33 , pp. 320-326
    • Hübner, W.1    Mantsch, H.H.2    Paltauf, F.3    Hauser, H.4
  • 110
    • 0024968216 scopus 로고
    • Orientation of α-helical peptides in a lipid bilayer
    • HUSCHILT, J. C., MILLMAN, B. M. & DAVIS, J. H. (1989). Orientation of α-helical peptides in a lipid bilayer. Biochim. Biophys. Acta 979, 139-141.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 139-141
    • Huschilt, J.C.1    Millman, B.M.2    Davis, J.H.3
  • 111
    • 0025978713 scopus 로고
    • Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation
    • IKURA, T., NOBUHIRO, G. & INAGAKI, F. (1991). Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation. Proteins 9, 81-89.
    • (1991) Proteins , vol.9 , pp. 81-89
    • Ikura, T.1    Nobuhiro, G.2    Inagaki, F.3
  • 112
    • 0027484593 scopus 로고
    • Orientation of fusion-active synthetic peptides in phospholipid bilayers: Determination by Fourier transform infrared spectroscopy
    • ISHIGURO, R., KIMURA, N. & TAKAHASHI, S. (1993). Orientation of fusion-active synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy. Biochemistry 32, 9792-9797.
    • (1993) Biochemistry , vol.32 , pp. 9792-9797
    • Ishiguro, R.1    Kimura, N.2    Takahashi, S.3
  • 113
    • 0029915994 scopus 로고    scopus 로고
    • Interaction of fusogenic synthetic peptide with phospholipid bilayers: Orientation of the peptide α-helix and binding isotherm
    • ISHIGURO, R., MATSUMOTO, M. & TAKAHASHI, S. (1996). Interaction of fusogenic synthetic peptide with phospholipid bilayers: orientation of the peptide α-helix and binding isotherm. Biochemistry 35, 4976-4983.
    • (1996) Biochemistry , vol.35 , pp. 4976-4983
    • Ishiguro, R.1    Matsumoto, M.2    Takahashi, S.3
  • 114
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • IWATA, S., OSTERMEIER, C., LUDWIG, B. & MICHEL, H. (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-668.
    • (1995) Nature , vol.376 , pp. 660-668
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 115
    • 0026228548 scopus 로고
    • Valinomycin and its interaction with ions in organic solvents, detergents, and lipids studied by Fourier transform IR spectroscopy
    • JACKSON, M. & MANTSCH, H. H. (1991a). Valinomycin and its interaction with ions in organic solvents, detergents, and lipids studied by Fourier transform IR spectroscopy. Biopolymers 31, 1205-1212.
    • (1991) Biopolymers , vol.31 , pp. 1205-1212
    • Jackson, M.1    Mantsch, H.H.2
  • 117
    • 0002336495 scopus 로고
    • Biomembrane structure from FT-IR spectroscopy
    • JACKSON, M. & MANTSCH, H. H. (1993). Biomembrane structure from FT-IR spectroscopy. Spectrochim. Acta Rev. 15, 53-69.
    • (1993) Spectrochim. Acta Rev. , vol.15 , pp. 53-69
    • Jackson, M.1    Mantsch, H.H.2
  • 118
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • JACKSON, M. & MANTSCH, H. H. (1995). The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 119
    • 0026731832 scopus 로고
    • Membrane environments probed by Fourier transform infrared spectroscopy
    • JACKSON, M., MANTSCH, H. H. & SPENCER, J. H. (1992). Membrane environments probed by Fourier transform infrared spectroscopy. Biochemistry 31, 7289-7293.
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Mantsch, H.H.2    Spencer, J.H.3
  • 120
    • 0026512750 scopus 로고
    • Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers
    • KALB, E., FREY, S. & TAMM, L. K. (1992). Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers. Biochim. Biophys. Acta 1103, 307-316.
    • (1992) Biochim. Biophys. Acta , vol.1103 , pp. 307-316
    • Kalb, E.1    Frey, S.2    Tamm, L.K.3
  • 122
    • 0025880710 scopus 로고
    • 10- and α-helices and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy
    • 10-and α-helices and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy. Biochemistry 30, 6541-6548.
    • (1991) Biochemistry , vol.30 , pp. 6541-6548
    • Kennedy, D.F.1    Crisma, M.2    Toniolo, C.3    Chapman, D.4
  • 123
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a β-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism
    • KLEINSCHMIDT, J. H. & TAMM, L. K. (1996). Folding intermediates of a β-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism. Biochemistry 35, 12993-13000.
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 124
    • 0031030031 scopus 로고    scopus 로고
    • Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: A spin-label electron spin resonance study
    • KLEINSCHMIDT, J. H., MAHANEY, J. E., THOMAS, D. D. & MARSH, D. (1997). Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: a spin-label electron spin resonance study. Biophys. J. 72, 767-778.
    • (1997) Biophys. J. , vol.72 , pp. 767-778
    • Kleinschmidt, J.H.1    Mahaney, J.E.2    Thomas, D.D.3    Marsh, D.4
  • 125
    • 0022085013 scopus 로고
    • Secondary structure of a channel-forming protein: Porin from E. coli outer membranes
    • KLEFFEL, B., GARAVITO, R. M., BAUMEISTER, W. & ROSENBUSCH, J. P. (1985). Secondary structure of a channel-forming protein: porin from E. coli outer membranes. EMBO J. 4, 1589-1592.
    • (1985) EMBO J. , vol.4 , pp. 1589-1592
    • Kleffel, B.1    Garavito, R.M.2    Baumeister, W.3    Rosenbusch, J.P.4
  • 126
    • 0015407488 scopus 로고
    • Intermolecular interaction effects in the Amide I vibrations of β polypeptides
    • KRIMM, S. & ABE, Y. (1972). Intermolecular interaction effects in the Amide I vibrations of β polypeptides. Proc. Natl. Acad. Sci. USA 69, 2788-2792.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2788-2792
    • Krimm, S.1    Abe, Y.2
  • 127
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • KRIMM, S. & BANDEKAR, J. (1986). Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Prot Chem. 38, 181-364.
    • (1986) Adv. Prot Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 128
    • 0020489247 scopus 로고
    • Infrared spectrum of the purple membrane: Clue to a proton conduction mechanism?
    • KRIMM, S. & DWIVEDI, A. M. (1982). Infrared spectrum of the purple membrane: Clue to a proton conduction mechanism? Science 216, 407-408.
    • (1982) Science , vol.216 , pp. 407-408
    • Krimm, S.1    Dwivedi, A.M.2
  • 129
    • 0019909438 scopus 로고
    • Functionalized monolayer assembly manipulation
    • KUHN, H. (1983). Functionalized monolayer assembly manipulation. Thin Solid Films 99, 1-16.
    • (1983) Thin Solid Films , vol.99 , pp. 1-16
    • Kuhn, H.1
  • 130
    • 84986847211 scopus 로고
    • Vibrational assignment of the sn1 and sn2 carbonyl stretching modes of membrane phospholipids
    • LEVIN, I. W., MUSHAYAKARARA, E. & BITTMAN, R. (1982). Vibrational assignment of the sn1 and sn2 carbonyl stretching modes of membrane phospholipids. J. Raman Spectrosc. 13, 231-234.
    • (1982) J. Raman Spectrosc. , vol.13 , pp. 231-234
    • Levin, I.W.1    Mushayakarara, E.2    Bittman, R.3
  • 131
    • 0027517401 scopus 로고
    • Studies of mixed-chain diacyl phosphatidylcholines with highly asymmetric acyl chains: A Fourier transform infrared spectroscopic study of interfacial hydration and hydrocarbon chain packing in the mixed interdigitated gel phase
    • LEWIS, R. N. A. H. & MCELHANEY, R. N. (1993a). Studies of mixed-chain diacyl phosphatidylcholines with highly asymmetric acyl chains: A Fourier transform infrared spectroscopic study of interfacial hydration and hydrocarbon chain packing in the mixed interdigitated gel phase. Biophys. J. 65, 1866-1877.
    • (1993) Biophys. J. , vol.65 , pp. 1866-1877
    • Lewis, R.N.A.H.1    Mcelhaney, R.N.2
  • 132
    • 0027292860 scopus 로고
    • Calorimetric and spectroscopic studies of the polymorphic phase behavior of a homologous series of n-saturated 1,2-diacyl phosphatidylethanolamines
    • LEWIS, R. N. A. H. & MCELHANEY, R. N. (1993b). Calorimetric and spectroscopic studies of the polymorphic phase behavior of a homologous series of n-saturated 1,2-diacyl phosphatidylethanolamines. Biophys. J. 64, 1081-1096.
    • (1993) Biophys. J. , vol.64 , pp. 1081-1096
    • Lewis, R.N.A.H.1    Mcelhaney, R.N.2
  • 133
    • 0001774382 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in the study of hydrated lipids and lipid bilayer membranes
    • (ed. H. H. Mantsch and D. Chapman), Wiley-Liss, Inc.
    • LEWIS, R. N. A. H. & MCELHANEY, R. N. (1996). Fourier transform infrared spectroscopy in the study of hydrated lipids and lipid bilayer membranes. In Infrared Spectroscopy of Biomolecules (ed. H. H. Mantsch and D. Chapman), pp. 159-202. Wiley-Liss, Inc.
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 159-202
    • Lewis, R.N.A.H.1    Mcelhaney, R.N.2
  • 134
    • 0028340235 scopus 로고
    • 2H NMR spectroscopic studies of hydrocarbon chain conformation and orientational order in the lipid-crystalline state
    • 2H NMR spectroscopic studies of hydrocarbon chain conformation and orientational order in the lipid-crystalline state. Biophys. J. 67, 197-207.
    • (1994) Biophys. J. , vol.67 , pp. 197-207
    • Lewis, R.N.A.H.1    Mcelhaney, R.N.2    Monck, M.A.3    Cullis, P.R.4
  • 135
    • 0027987329 scopus 로고
    • Components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: A reevaluation
    • LEWIS, R. N. A. H., MCELHANEY, R. N., POHLE, W. & MANTSCH, H. H. (1994b). Components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: a reevaluation. Biophys. J. 67, 2367-2375.
    • (1994) Biophys. J. , vol.67 , pp. 2367-2375
    • Lewis, R.N.A.H.1    Mcelhaney, R.N.2    Pohle, W.3    Mantsch, H.H.4
  • 136
    • 0029967328 scopus 로고    scopus 로고
    • The interfacial structure of phospholipid bilayers: Differential scanning calorimetry and Fourier transform infrared spectroscopic studies of 1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine and its dialkyl and acyl-alkyl analogs
    • LEWIS, R. N. A. H., POHLE, W. & MCELHANEY, R. N. (1996). The interfacial structure of phospholipid bilayers: differential scanning calorimetry and Fourier transform infrared spectroscopic studies of 1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine and its dialkyl and acyl-alkyl analogs. Biophys. J. 70, 2736-2746.
    • (1996) Biophys. J. , vol.70 , pp. 2736-2746
    • Lewis, R.N.A.H.1    Pohle, W.2    Mcelhaney, R.N.3
  • 137
    • 0029415097 scopus 로고
    • Apparent pKa of the fatty acids within ordered mixtures of model human stratum corneum lipids
    • LIECKFELD, R., VILLALAÍN, J., GÓMEZ-FERNÁNDEZ, J. C. & LEE, G. (1995). Apparent pKa of the fatty acids within ordered mixtures of model human stratum corneum lipids. Pharm. Res. 12, 1614-1617.
    • (1995) Pharm. Res. , vol.12 , pp. 1614-1617
    • Lieckfeld, R.1    Villalaín, J.2    Gómez-FERNÁNDEZ, J.C.3    Lee, G.4
  • 140
    • 0028263997 scopus 로고
    • The phase behavior of mixed aqueous dispersions of dipalmitoyl derivatives of phosphatidylcholine and diacylglycerol
    • LÓPEZ-GARCÍA, F., VILLALAÍN, J., GÓMEZ-FERNÁNDEZ, J. C. & QUINN, P. J. (1994). The phase behavior of mixed aqueous dispersions of dipalmitoyl derivatives of phosphatidylcholine and diacylglycerol. Biophys. J. 66, 1991-2004.
    • (1994) Biophys. J. , vol.66 , pp. 1991-2004
    • López-GARCÍA, F.1    Villalaín, J.2    Gómez-FERNÁNDEZ, J.C.3    Quinn, P.J.4
  • 141
    • 0029916523 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban
    • LUDLAM, C. F. C., ARKIN, I. T., LIU, X.-M., ROTHMAN, M. S., RATH, P., AIMOTO, S., SMITH, S. O., ENGELMAN, D. M. & ROTHSCHILD, K. J. (1996). Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophys. J. 70, 1728-1736.
    • (1996) Biophys. J. , vol.70 , pp. 1728-1736
    • Ludlam, C.F.C.1    Arkin, I.T.2    Liu, X.-M.3    Rothman, M.S.4    Rath, P.5    Aimoto, S.6    Smith, S.O.7    Engelman, D.M.8    Rothschild, K.J.9
  • 142
    • 0028840940 scopus 로고
    • Structure and topology of the influenza virus fusion peptide in lipid bilayers
    • LÜNEBERG, J., MARTIN, I., NÜßLER, RUYSSCHAERT, J.-M. & HERRMANN, A. (1995). Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270, 27606-27614.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27606-27614
    • Lüneberg, J.1    Martin, I.2    Nüßler3    Ruysschaert, J.-M.4    Herrmann, A.5
  • 143
    • 0000557789 scopus 로고
    • Infrared spectroscopy of the photosynthetic reaction center
    • (ed. H. Deisenhofer and J. R. Norris), San Diego: Academic Press
    • MÄNTELE, W. (1993). Infrared spectroscopy of the photosynthetic reaction center. The Photosynthetic Reaction Center, Vol. II (ed. H. Deisenhofer and J. R. Norris), pp. 239-283. San Diego: Academic Press.
    • (1993) The Photosynthetic Reaction Center , vol.2 , pp. 239-283
    • Mäntele, W.1
  • 144
    • 0026070508 scopus 로고
    • Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy
    • MANTSCH, H. H. & MCELHANEY, R. N. (1991). Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy. Chem. Phys. Lipids 57, 213-226.
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 213-226
    • Mantsch, H.H.1    Mcelhaney, R.N.2
  • 145
    • 0019889052 scopus 로고
    • Characterization by infrared spectroscopy of the bilayer to nonbilayer phase transition of phosphatidylethanolamines
    • MANTSCH, H. H., MARTIN, A. & CAMERON, D. G. (1981). Characterization by infrared spectroscopy of the bilayer to nonbilayer phase transition of phosphatidylethanolamines. Biochemistry 20, 3138-3145.
    • (1981) Biochemistry , vol.20 , pp. 3138-3145
    • Mantsch, H.H.1    Martin, A.2    Cameron, D.G.3
  • 146
    • 0030928208 scopus 로고    scopus 로고
    • Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of β-sheet structures
    • MARSH, D. (1997). Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of β-sheet structures. Biophys. J. 72, 2710-2718.
    • (1997) Biophys. J. , vol.72 , pp. 2710-2718
    • Marsh, D.1
  • 148
    • 0029655419 scopus 로고    scopus 로고
    • Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer
    • MARTIN, I., SCHAAL, H., SCHEID, A. & RUYSSCHAERT, J.-M. (1996). Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J. Virol. 70, 298-304.
    • (1996) J. Virol. , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.-M.4
  • 149
    • 0029064280 scopus 로고
    • FTIR spectroscopy of alanine-based peptides: Assignment of the amide I′ modes for random coil and helix
    • MARTINEZ, G. & MILLHAUSER, G. (1995). FTIR spectroscopy of alanine-based peptides: Assignment of the amide I′ modes for random coil and helix. J. Struct. Biol. 114, 23-27.
    • (1995) J. Struct. Biol. , vol.114 , pp. 23-27
    • Martinez, G.1    Millhauser, G.2
  • 150
    • 0026066649 scopus 로고
    • A comparative study on interactions of α-aminoisobutyric acid containing antibiotic peptides, trichopolyn I and hypelcin A with phosphatidylcholine bilayers
    • MATSUZAKI, K., SHIOYAMA, T., OKAMURA, E., UMEMURA, J., TAKENAKA, T., TAKAISHI, Y., FUJITA, T. & MIYAJIMA, K. (1991). A comparative study on interactions of α-aminoisobutyric acid containing antibiotic peptides, trichopolyn I and hypelcin A with phosphatidylcholine bilayers. Biochim. Biophys. Acta 1070, 419-428.
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 419-428
    • Matsuzaki, K.1    Shioyama, T.2    Okamura, E.3    Umemura, J.4    Takenaka, T.5    Takaishi, Y.6    Fujita, T.7    Miyajima, K.8
  • 152
    • 0002529507 scopus 로고
    • Fourier transform infrared studies of lipid-protein interaction
    • (ed. A. Watts and J. J. H. H. M. DePont), Amsterdam: Elsevier Science Publishers
    • MENDELSOHN, R. & MANTSCH, H. H. (1986). Fourier transform infrared studies of lipid-protein interaction. In Progress in Protein-Lipid Interactions 2 (ed. A. Watts and J. J. H. H. M. DePont), pp. 103-146. Amsterdam: Elsevier Science Publishers.
    • (1986) Progress in Protein-Lipid Interactions , vol.2 , pp. 103-146
    • Mendelsohn, R.1    Mantsch, H.H.2
  • 153
    • 0001780747 scopus 로고    scopus 로고
    • Infrared spectroscopic determination of conformational disorder and microphase separation in phospholipid acyl chains
    • (ed. K. M. Merz and B. Roux), Boston: Birkhäuser
    • MENDELSOHN, R. & SNYDER, R. G. (1996). Infrared spectroscopic determination of conformational disorder and microphase separation in phospholipid acyl chains. In Biological Membranes: A Molecular Perspective from Computation and Experiment (ed. K. M. Merz and B. Roux), pp. 145-174. Boston: Birkhäuser.
    • (1996) Biological Membranes: a Molecular Perspective from Computation and Experiment , pp. 145-174
    • Mendelsohn, R.1    Snyder, R.G.2
  • 154
    • 0019877716 scopus 로고
    • Raman and Fourier transform infrared spectroscopic studies of the interaction between glycophorin and dimyristoylphosphatidylcholine
    • MENDELSOHN, R., DLUHY, R., TARASCHI, T., CAMERON, D. G. & MANTSCH, H. H. (1981). Raman and Fourier transform infrared spectroscopic studies of the interaction between glycophorin and dimyristoylphosphatidylcholine. Biochemistry 20, 6699-6706.
    • (1981) Biochemistry , vol.20 , pp. 6699-6706
    • Mendelsohn, R.1    Dluhy, R.2    Taraschi, T.3    Cameron, D.G.4    Mantsch, H.H.5
  • 156
    • 0021771684 scopus 로고
    • Interaction of glycophorin with phosphatidylserine: A Fourier transform infrared investigation
    • MENDELSOHN, R., DLUHY, R. A., CRAWFORD, T. & MANTSCH, H. H. (1984b). Interaction of glycophorin with phosphatidylserine: A Fourier transform infrared investigation. Biochemistry 23, 1498-1504.
    • (1984) Biochemistry , vol.23 , pp. 1498-1504
    • Mendelsohn, R.1    Dluhy, R.A.2    Crawford, T.3    Mantsch, H.H.4
  • 157
    • 0024462478 scopus 로고
    • Quantitative determination of conformational disorder in the acyl chains of phospholipid bilayers by infrared spectroscopy
    • MENDELSOHN, R., DAVIES, M. A., BRAUNER, J. W., SCHUSTER, H. F. & DLUHY, R. A. (1989). Quantitative determination of conformational disorder in the acyl chains of phospholipid bilayers by infrared spectroscopy. Biochemistry 28, 8934-8939.
    • (1989) Biochemistry , vol.28 , pp. 8934-8939
    • Mendelsohn, R.1    Davies, M.A.2    Brauner, J.W.3    Schuster, H.F.4    Dluhy, R.A.5
  • 158
    • 0000110539 scopus 로고
    • External infrared reflection absorption spectrometry of monolayer films at the air-water interface
    • MENDELSOHN, R., BRAUNER, J. W. & GERICKE, A. (1995a). External infrared reflection absorption spectrometry of monolayer films at the air-water interface. Annu. Rev. Phys. Chem. 46, 305-334.
    • (1995) Annu. Rev. Phys. Chem. , vol.46 , pp. 305-334
    • Mendelsohn, R.1    Brauner, J.W.2    Gericke, A.3
  • 159
    • 0028825706 scopus 로고
    • IR spectroscopic determination of gel state miscibility in long-chain phosphatidylcholine mixtures
    • MENDELSOHN, R., LIANG, G. L., STRAUSS, H. L. & SNYDER, R. G. (1995b). IR spectroscopic determination of gel state miscibility in long-chain phosphatidylcholine mixtures. Biophys. J. 69, 1987-1998.
    • (1995) Biophys. J. , vol.69 , pp. 1987-1998
    • Mendelsohn, R.1    Liang, G.L.2    Strauss, H.L.3    Snyder, R.G.4
  • 160
    • 0018292890 scopus 로고
    • Orientation of rhodopsin α-helices in retinal rod outer segment membranes studied by infrared linear dichroism
    • MICHEL-VILLAZ, M., SAIBIL, H. R. & CHABRE, M. (1979). Orientation of rhodopsin α-helices in retinal rod outer segment membranes studied by infrared linear dichroism. Proc. Natl. Acad. Sci. USA 76, 4405-4408.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4405-4408
    • Michel-Villaz, M.1    Saibil, H.R.2    Chabre, M.3
  • 161
    • 0026783919 scopus 로고
    • Short alanine-based peptides may form 310 helices and not α-helices in aqueous solution
    • MIICK, S. M., MARTINEZ, G. V., FIORI, W. R., TODD, A. P. & MILLHAUSER, G. L. (1992). Short alanine-based peptides may form 310 helices and not α-helices in aqueous solution. Nature 359, 653-655.
    • (1992) Nature , vol.359 , pp. 653-655
    • Miick, S.M.1    Martinez, G.V.2    Fiori, W.R.3    Todd, A.P.4    Millhauser, G.L.5
  • 162
    • 4243898367 scopus 로고
    • Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations
    • MIYAZAWA, T. (1960). Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations. J. Chem. Phys. 32, 1647-1652.
    • (1960) J. Chem. Phys. , vol.32 , pp. 1647-1652
    • Miyazawa, T.1
  • 163
    • 0343532738 scopus 로고
    • The infrared spectra of polypeptides in various conformations: Amide I and II bands
    • MIYAZAWA, T. & BLOUT, E. R. (1961). The infrared spectra of polypeptides in various conformations: Amide I and II bands. J. Am. Chem. Soc. 83, 712-719.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 164
    • 0030066514 scopus 로고    scopus 로고
    • Conformational order of phospholipids incorporated into human erythrocytes: An FTIR spectroscopy study
    • MOORE, D. J., SILLS, R. H., PATEL, N. & MENDELSOHN, R. (1996). Conformational order of phospholipids incorporated into human erythrocytes: an FTIR spectroscopy study. Biochemistry 35, 229-235.
    • (1996) Biochemistry , vol.35 , pp. 229-235
    • Moore, D.J.1    Sills, R.H.2    Patel, N.3    Mendelsohn, R.4
  • 165
    • 0031033945 scopus 로고    scopus 로고
    • Conformational order of specific phospholipids in human erythrocytes: Correlations with changes in cell shape
    • MOORE, D. J., SILLS, R. H. & MENDELSOHN, R. (1997). Conformational order of specific phospholipids in human erythrocytes: correlations with changes in cell shape. Biochemistry 36, 660-664.
    • (1997) Biochemistry , vol.36 , pp. 660-664
    • Moore, D.J.1    Sills, R.H.2    Mendelsohn, R.3
  • 166
    • 0017027905 scopus 로고
    • Vibrational analysis of peptides, polypeptides, and proteins. II. β-poly(L-alanine) and β-poly(L-alanylglycine)
    • MOORE, W. H. & KRIMM, S. (1976). Vibrational analysis of peptides, polypeptides, and proteins. II. β-poly(L-alanine) and β-poly(L-alanylglycine). Biopolymers 15, 2465-2483.
    • (1976) Biopolymers , vol.15 , pp. 2465-2483
    • Moore, W.H.1    Krimm, S.2
  • 167
    • 0025841667 scopus 로고
    • Membrane binding induces destabilization of cytochrome c structure
    • MUGA, A., MANTSCH, H. H. & SUREWICZ, W. K. (1991a). Membrane binding induces destabilization of cytochrome c structure. Biochemistry 30, 7219-7224.
    • (1991) Biochemistry , vol.30 , pp. 7219-7224
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 168
    • 0025877054 scopus 로고
    • Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy
    • MUGA, A., MANTSCH, H. H. & SUREWICZ, W. K. (1991b). Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy. Biochemistry 30, 2629-2635.
    • (1991) Biochemistry , vol.30 , pp. 2629-2635
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 169
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • MUGA, A., NEUGEBAUER, W., HIRAMA, T. & SUREWICZ, W. K. (1994). Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry 33, 4444-4448.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 172
    • 0022642088 scopus 로고
    • Detection by high pressure infrared spectrometry of hydrogen-bonding between water and triacetyl glycerol
    • MUSHAYAKARARA, E. C., WONG, P. T. T. & MANTSCH, H. H. (1986). Detection by high pressure infrared spectrometry of hydrogen-bonding between water and triacetyl glycerol. Biochem. Biophys. Res. Comm. 134, 140-145.
    • (1986) Biochem. Biophys. Res. Comm. , vol.134 , pp. 140-145
    • Mushayakarara, E.C.1    Wong, P.T.T.2    Mantsch, H.H.3
  • 173
    • 0002859824 scopus 로고    scopus 로고
    • Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reactions centers
    • (ed. H. H. Mantsch & D. Chapman), Wiley-Liss, Inc.
    • NABEDRYK, E. (1996). Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reactions centers. In Infrared Spectroscopy of Biomolecules (ed. H. H. Mantsch & D. Chapman), pp. 39-81. Wiley-Liss, Inc.
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 39-81
    • Nabedryk, E.1
  • 174
    • 0019976513 scopus 로고
    • Orientation of gramidicin a transmembrane channel
    • NABEDRYK, E., GINGOLD, M. P. & BRETON, J. (1982a). Orientation of gramidicin A transmembrane channel. Biophys. J. 38, 243-249.
    • (1982) Biophys. J. , vol.38 , pp. 243-249
    • Nabedryk, E.1    Gingold, M.P.2    Breton, J.3
  • 175
    • 0001101821 scopus 로고
    • Conformation and orientation of the protein in the bacterial photosynthetic reaction center
    • NABEDRYK, E., TIEDE, D. M., DUTTON, P. L. & BRETON, J. (1982b). Conformation and orientation of the protein in the bacterial photosynthetic reaction center. Biochim. Biophys. Acta 682, 273-280.
    • (1982) Biochim. Biophys. Acta , vol.682 , pp. 273-280
    • Nabedryk, E.1    Tiede, D.M.2    Dutton, P.L.3    Breton, J.4
  • 176
    • 0022366086 scopus 로고
    • Further characterization of the protein secondary structure in purple membrane by circular dichroism and polarized infrared spectroscopies
    • NABEDRYK, E., BARDIN, A. M. & BRETON, J. (1985). Further characterization of the protein secondary structure in purple membrane by circular dichroism and polarized infrared spectroscopies. Biophys. J. 48, 873-876.
    • (1985) Biophys. J. , vol.48 , pp. 873-876
    • Nabedryk, E.1    Bardin, A.M.2    Breton, J.3
  • 177
    • 0024006622 scopus 로고
    • The orientation of β-sheets in porin. A polarized Fourier transform infrared spectroscopic investigation
    • NABEDRYK, E., GARAVITO, R. M. & BRETON, J. (1988). The orientation of β-sheets in porin. A polarized Fourier transform infrared spectroscopic investigation. Biophys. J. 53, 671-676.
    • (1988) Biophys. J. , vol.53 , pp. 671-676
    • Nabedryk, E.1    Garavito, R.M.2    Breton, J.3
  • 178
    • 0028577514 scopus 로고
    • Study by infrared spectroscopy of the interaction of bovine myelin basic protein with phosphatidic acid
    • NABET, A., BOGGS, J. M. & PÉZOLET, M. (1994). Study by infrared spectroscopy of the interaction of bovine myelin basic protein with phosphatidic acid. Biochemistry 33, 14792-14799.
    • (1994) Biochemistry , vol.33 , pp. 14792-14799
    • Nabet, A.1    Boggs, J.M.2    Pézolet, M.3
  • 179
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • NIEVA, J. L., NIR, S., MUGA, A., GOÑI, F. M. & WILSCHUT, J. (1994). Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry 33, 3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goñi, F.M.4    Wilschut, J.5
  • 180
    • 33745563365 scopus 로고
    • Generalized two-dimensional correlation method applicable to infrared, Raman, and other types of spectroscopy
    • NODA, I. (1993). Generalized two-dimensional correlation method applicable to infrared, Raman, and other types of spectroscopy. Applied Spectroscopy 47, 1329-1336.
    • (1993) Applied Spectroscopy , vol.47 , pp. 1329-1336
    • Noda, I.1
  • 181
    • 0022450049 scopus 로고
    • Orientation of gramicidin D incorporated into phospholipid multibilayers: A Fourier transform infrared-attenuated total reflection spectroscopic study
    • OKAMURA, E., UMEMURA, J. & TAKENAKA, T. (1986). Orientation of gramicidin D incorporated into phospholipid multibilayers: a Fourier transform infrared-attenuated total reflection spectroscopic study. Biochim. Biophys. Acta 856, 68-75.
    • (1986) Biochim. Biophys. Acta , vol.856 , pp. 68-75
    • Okamura, E.1    Umemura, J.2    Takenaka, T.3
  • 182
    • 0025321053 scopus 로고
    • Orientation studies of hydrated dipalmitoylphosphatidylcholine multibilayers by polarized FTIR-ATR spectroscopy
    • OKAMURA, E., UMEMURA, J. & TAKENAKA, T. (1990). Orientation studies of hydrated dipalmitoylphosphatidylcholine multibilayers by polarized FTIR-ATR spectroscopy. Biochim. Biophys. Acta 1025, 94-98.
    • (1990) Biochim. Biophys. Acta , vol.1025 , pp. 94-98
    • Okamura, E.1    Umemura, J.2    Takenaka, T.3
  • 183
    • 0025999791 scopus 로고
    • Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids
    • PASTRANA-RIOS, B., MAUTONE, A. J. & MENDELSOHN, R. (1991). Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids. Biochemistry 30, 10058-10064.
    • (1991) Biochemistry , vol.30 , pp. 10058-10064
    • Pastrana-Rios, B.1    Mautone, A.J.2    Mendelsohn, R.3
  • 184
    • 0028174249 scopus 로고
    • A direct test of the 'squeeze-out' hypothesis of lung surfactant function. External reflection FT-IR at the air/water interface
    • PASTRANA-RIOS, B., FLACH, C. R., BRAUNER, J. W., MAUTONE, A. J. & MENDELSOHN, R. (1994). A direct test of the 'squeeze-out' hypothesis of lung surfactant function. External reflection FT-IR at the air/water interface. Biochemistry 33, 5121-5127.
    • (1994) Biochemistry , vol.33 , pp. 5121-5127
    • Pastrana-Rios, B.1    Flach, C.R.2    Brauner, J.W.3    Mautone, A.J.4    Mendelsohn, R.5
  • 185
    • 0028791417 scopus 로고
    • External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface
    • PASTRANA-RIOS, B., TANEVA, S., KEOUGH, K. M. W., MAUTONE, A. J. & MENDELSOHN, R. (1995). External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface. Biophys. J. 69, 2531-2540.
    • (1995) Biophys. J. , vol.69 , pp. 2531-2540
    • Pastrana-Rios, B.1    Taneva, S.2    Keough, K.M.W.3    Mautone, A.J.4    Mendelsohn, R.5
  • 186
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • PEBAY-PEYROULA, E., RUMMEL, G., ROSENBUSCH, J. P. & LANDAU, E. M. (1997). X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 188
    • 0001672649 scopus 로고
    • Formation of multilayers of dipalmitoylphosphatidylcholine using the Langmuir-Blodgett technique
    • PENG, J. B., PRAKASH, M., MACDONALD, R., DUTTA, P. & KETTERSON, J. B. (1987). Formation of multilayers of dipalmitoylphosphatidylcholine using the Langmuir-Blodgett technique. Langmuir 3, 1096-1097.
    • (1987) Langmuir , vol.3 , pp. 1096-1097
    • Peng, J.B.1    Prakash, M.2    Macdonald, R.3    Dutta, P.4    Ketterson, J.B.5
  • 189
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • RAFALSKI, M., LEAR, J. D. & DEGRADO, W. F. (1990). Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. Biochemistry 29, 7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    Degrado, W.F.3
  • 190
    • 0027416654 scopus 로고
    • Surface chemistry of binary mixtures of phospholipids in monolayers. Infrared studies of surface composi ion at varying surface pressures in a pulmonary surfactant model system
    • RANA, F. R., MAUTONE, A. J. & DLUHY, R. A. (1993). Surface chemistry of binary mixtures of phospholipids in monolayers. Infrared studies of surface composi ion at varying surface pressures in a pulmonary surfactant model system. Biochemistry 32, 3169-3177.
    • (1993) Biochemistry , vol.32 , pp. 3169-3177
    • Rana, F.R.1    Mautone, A.J.2    Dluhy, R.A.3
  • 191
    • 0026025897 scopus 로고
    • Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1
    • RATH, P., BOUSCHÉ, MERRILL, A. R., CRAMER, W. A. & ROTHSCHILD, K. J. (1991). Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1. Biophys. J. 59, 516-522.
    • (1991) Biophys. J. , vol.59 , pp. 516-522
    • Rath, P.1    BOUSCHÉ2    Merrill, A.R.3    Cramer, W.A.4    Rothschild, K.J.5
  • 192
    • 0028073042 scopus 로고
    • Lipid transfer between small unilamellar vesicles and single bilayers on a solid support: Self-assembly of supported bilayers with asymmetric lipid distribution
    • REINL, H. M. & BAYERL, T. M. (1994). Lipid transfer between small unilamellar vesicles and single bilayers on a solid support: self-assembly of supported bilayers with asymmetric lipid distribution. Biochemistry 33, 14091-14099.
    • (1994) Biochemistry , vol.33 , pp. 14091-14099
    • Reinl, H.M.1    Bayerl, T.M.2
  • 193
    • 0030021044 scopus 로고    scopus 로고
    • The effect of high externa pressure on DPPC-cholesterol multilamellar vesicles: A pressive tuning Fourier transform infrared spectroscopy study
    • REIS, O., WINTER, R. & ZERDA, T. W. (1996). The effect of high externa pressure on DPPC-cholesterol multilamellar vesicles: a pressive tuning Fourier transform infrared spectroscopy study. Biochim. Biophys. Acta 1279, 5-16.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 5-16
    • Reis, O.1    Winter, R.2    Zerda, T.W.3
  • 195
    • 0030062907 scopus 로고    scopus 로고
    • Infrared amide I′ band of the coiled coil
    • REISDORF, JR., W. C. & KRIMM, S. (1996). Infrared amide I′ band of the coiled coil. Biochemistry 35, 1383-1386.
    • (1996) Biochemistry , vol.35 , pp. 1383-1386
    • Reisdorf Jr., W.C.1    Krimm, S.2
  • 197
    • 0018383292 scopus 로고
    • Polarized infrared spectroscopy of oriented purple membrane
    • ROTHSCHILD, K. J. & CLARK, N. A. (1979a). Polarized infrared spectroscopy of oriented purple membrane. Biophys. J. 25, 473-488.
    • (1979) Biophys. J. , vol.25 , pp. 473-488
    • Rothschild, K.J.1    Clark, N.A.2
  • 198
    • 0018347397 scopus 로고
    • Anomalous amide I infrared absorption of purple membrane
    • ROTHSCHILD, K. J. & CLARK, N. A. (1979b). Anomalous amide I infrared absorption of purple membrane. Science 204, 311-312.
    • (1979) Science , vol.204 , pp. 311-312
    • Rothschild, K.J.1    Clark, N.A.2
  • 199
    • 0018830249 scopus 로고
    • A spectroscopic study of rhodopsin alpha-helix orientation
    • ROTHSCHILD, K. J., SANCHES, R., HSIAO, T. L. & CLARK, N. A. (1980). A spectroscopic study of rhodopsin alpha-helix orientation. Biophys. J. 31, 53-64.
    • (1980) Biophys. J. , vol.31 , pp. 53-64
    • Rothschild, K.J.1    Sanches, R.2    Hsiao, T.L.3    Clark, N.A.4
  • 200
    • 0028823489 scopus 로고
    • Metastability of dimyristoylphosphatidylethanolamine as studied by FT-IR and the effect of α-tocopherol
    • SALGADO, J., VILLALAÍN, J. & GÓMEZ-FERNÁNDEZ, J. C. (1995). Metastability of dimyristoylphosphatidylethanolamine as studied by FT-IR and the effect of α-tocopherol. Biochim. Biophys. Acta 1239, 213-225.
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 213-225
    • Salgado, J.1    Villalaín, J.2    Gómez-FERNÁNDEZ, J.C.3
  • 201
    • 0029945388 scopus 로고    scopus 로고
    • Escherichia coli diacylglycerol kinase is an α-helical polytopic membrane protein and can spontaneously insert into preformed lipid vesicles
    • SANDERS II, C. R., CZERSKI, L., VINOGRADOVA, O., BADOLA, P., SONG, D. & SMITH, S. O. (1996). Escherichia coli diacylglycerol kinase is an α-helical polytopic membrane protein and can spontaneously insert into preformed lipid vesicles. Biochemistry 35, 8610-8618.
    • (1996) Biochemistry , vol.35 , pp. 8610-8618
    • Sanders II, C.R.1    Czerski, L.2    Vinogradova, O.3    Badola, P.4    Song, D.5    Smith, S.O.6
  • 202
    • 0018982584 scopus 로고
    • Lipid conformation in model membranes and biological membranes
    • SEELIG, J. & SEELIG, A. (1980). Lipid conformation in model membranes and biological membranes. Quart. Rev. Biophys. 13, 19-61.
    • (1980) Quart. Rev. Biophys. , vol.13 , pp. 19-61
    • Seelig, J.1    Seelig, A.2
  • 203
    • 0012507105 scopus 로고
    • 2 wagging progressions as IR probes of slightly disordered phospholipid acyl chain states
    • 2 wagging progressions as IR probes of slightly disordered phospholipid acyl chain states. J. Phys. Chem. 96, 2749-2754.
    • (1992) J. Phys. Chem. , vol.96 , pp. 2749-2754
    • Senak, L.1    Moore, D.2    Mendelsohn, R.3
  • 204
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • SIMMERMAN, H. K. B., KOBAYASHI, Y. M., AUTRY, J. M. & JONES, L. R. (1996). A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. J. Biol. Chem. 271, 5941-5946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5941-5946
    • Simmerman, H.K.B.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 205
    • 0026738175 scopus 로고
    • The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR
    • SIPOS, D., ANDERSSON, M. & EHRENBERG, A. (1992). The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR. Eur. J. Biochem. 209, 163-169.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 163-169
    • Sipos, D.1    Andersson, M.2    Ehrenberg, A.3
  • 206
    • 0028271855 scopus 로고
    • Structure and orientation of the transmembrane domain of glycophorin A in lipid bilayers
    • SMITH, S. O., JONAS, R., BRAIMAN, M. & BORMANN, B. J. (1994). Structure and orientation of the transmembrane domain of glycophorin A in lipid bilayers. Biochemistry 33, 6334-6341.
    • (1994) Biochemistry , vol.33 , pp. 6334-6341
    • Smith, S.O.1    Jonas, R.2    Braiman, M.3    Bormann, B.J.4
  • 207
    • 0001318861 scopus 로고
    • Detection and measurement of microaggregation in binary mixtures of esters and of phospholipid dispersions
    • SNYDER, R. G., STRAUSS, H. L. & CATES, D. A. (1995). Detection and measurement of microaggregation in binary mixtures of esters and of phospholipid dispersions. J. Phys. Chem. 99, 8432-8439.
    • (1995) J. Phys. Chem. , vol.99 , pp. 8432-8439
    • Snyder, R.G.1    Strauss, H.L.2    Cates, D.A.3
  • 208
    • 0029751082 scopus 로고    scopus 로고
    • IR spectroscopic study of the structure and phase behavior of long-chain diacylphosphatidylcholines in the gel state
    • SNYDER, R. G., LIANG, G. L., STRAUSS, H. L. & MENDELSOHN, R. (1996). IR spectroscopic study of the structure and phase behavior of long-chain diacylphosphatidylcholines in the gel state. Biophys. J. 71, 3186-3198.
    • (1996) Biophys. J. , vol.71 , pp. 3186-3198
    • Snyder, R.G.1    Liang, G.L.2    Strauss, H.L.3    Mendelsohn, R.4
  • 210
    • 0023934553 scopus 로고
    • Conformational properties of angiotensin II in aqueous solution and in a lipid environment: A Fourier transform infrared spectroscopic investigation
    • SUREWICZ, W. K. & MANTSCH, H. H. (1988). Conformational properties of angiotensin II in aqueous solution and in a lipid environment: a Fourier transform infrared spectroscopic investigation. J. Am. Chem. Soc. 110, 4412-4414.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4412-4414
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 211
    • 0023429305 scopus 로고
    • Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide
    • SUREWICZ, W. K., MANTSCH, H. H., STAHL, G. L. & EPAND, R. M. (1987a). Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide. Proc. Natl. Acad. Sci. USA 84, 7028-7030.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7028-7030
    • Surewicz, W.K.1    Mantsch, H.H.2    Stahl, G.L.3    Epand, R.M.4
  • 212
    • 0023218240 scopus 로고
    • Fourier transform infrared spectroscopic investigation of the interaction between myelin basic protein and dimyristoylphosphatidylglycerol bilayers
    • SUREWICZ, W. K., MOSCARELLO, M. A. & MANTSCH, H. H. (1987b). Fourier transform infrared spectroscopic investigation of the interaction between myelin basic protein and dimyristoylphosphatidylglycerol bilayers. Biochemistry 26, 3881-3886.
    • (1987) Biochemistry , vol.26 , pp. 3881-3886
    • Surewicz, W.K.1    Moscarello, M.A.2    Mantsch, H.H.3
  • 213
    • 0023847752 scopus 로고
    • Lipid-induced changes in the secondary structure of snake venom cardiotoxins
    • SUREWICZ, W. K., STEPANIK, T. M., SZABO, A. G. & MANTSCH, H. H. (1988). Lipid-induced changes in the secondary structure of snake venom cardiotoxins. J. Biol. Chem. 263, 786-790.
    • (1988) J. Biol. Chem. , vol.263 , pp. 786-790
    • Surewicz, W.K.1    Stepanik, T.M.2    Szabo, A.G.3    Mantsch, H.H.4
  • 214
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • SUREWICZ, W. K., MANTSCH, H. H. & CHAPMAN, D. (1993). Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment. Biochemistry 32, 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 215
    • 0040103801 scopus 로고
    • A quantitative study of the amide vibrations in the infra-red spectrum of silk fibroin
    • SUZUKI, E. (1967). A quantitative study of the amide vibrations in the infra-red spectrum of silk fibroin. Spetrochim. Acta 23A, 2303-2308.
    • (1967) Spetrochim. Acta , vol.23 A , pp. 2303-2308
    • Suzuki, E.1
  • 216
    • 0001345210 scopus 로고
    • Isotopically enhanced infrared spectroscopy: A novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides
    • TADESSE, L., NAZARBAGHI, R. & WALTERS, L. (1991). Isotopically enhanced infrared spectroscopy: a novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides. J. Am. Chem. Soc. 113, 7036-7037.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7036-7037
    • Tadesse, L.1    Nazarbaghi, R.2    Walters, L.3
  • 217
    • 0023873084 scopus 로고
    • Lateral diffusion and fluorescence microscope studies on a monoclonal antibody specifically bound to supported phospholipid bilayers
    • TAMM, L. K. (1988). Lateral diffusion and fluorescence microscope studies on a monoclonal antibody specifically bound to supported phospholipid bilayers. Biochemistry 27, 1450-1457.
    • (1988) Biochemistry , vol.27 , pp. 1450-1457
    • Tamm, L.K.1
  • 218
    • 0025913906 scopus 로고
    • Membrane insertion and lateral mobility of synthetic amphiphilic signal peptides in lipid model membranes
    • TAMM, L. K. (1991). Membrane insertion and lateral mobility of synthetic amphiphilic signal peptides in lipid model membranes. Biochim. Biophys. Acta 1071, 123-148.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 123-148
    • Tamm, L.K.1
  • 219
    • 0000907989 scopus 로고
    • Microspectrofluorometry on supported planar membranes
    • (ed. Stephen G. Schulman), Chemical Analysis Series, John Wiley & Sons, Inc.
    • TAMM, L. K. & KALB, E. (1993). Microspectrofluorometry on supported planar membranes. In Molecular Luminescence Spectroscopy, Part 3 (ed. Stephen G. Schulman), pp. 253-305. Chemical Analysis Series, Vol. 77. John Wiley & Sons, Inc.
    • (1993) Molecular Luminescence Spectroscopy , vol.77 , Issue.3 PART , pp. 253-305
    • Tamm, L.K.1    Kalb, E.2
  • 220
    • 0021947327 scopus 로고
    • Supported Phospholipid Bilayers
    • TAMM, L. K. & MCCONNELL, H. M. (1985). Supported Phospholipid Bilayers. Biophys. J. 47, 105-113.
    • (1985) Biophys. J. , vol.47 , pp. 105-113
    • Tamm, L.K.1    Mcconnell, H.M.2
  • 221
    • 0027240319 scopus 로고
    • Orientation of functional and non-functional PTS permease signal sequences in lipid bilayers. A polarized FTIR study
    • TAMM, L. K. & TATULIAN, S. A. (1993). Orientation of functional and non-functional PTS permease signal sequences in lipid bilayers. A polarized FTIR study. Biochemistry 32, 7720-7726.
    • (1993) Biochemistry , vol.32 , pp. 7720-7726
    • Tamm, L.K.1    Tatulian, S.A.2
  • 222
    • 0030593483 scopus 로고    scopus 로고
    • Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin
    • TATULIAN, S. A. & TAMM, L. K. (1996). Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin. J. Mol. Biol. 260, 312-316.
    • (1996) J. Mol. Biol. , vol.260 , pp. 312-316
    • Tatulian, S.A.1    Tamm, L.K.2
  • 223
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • TATULIAN, S. A., HINTERDORFER, P., BABER, G. & TAMM, L. K. (1995a). Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J. 14, 5514-5523.
    • (1995) EMBO J. , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 224
    • 0028950657 scopus 로고
    • Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy
    • TATULIAN, S. A., JONES, L. R., REDDY, L. G., STOKES, D. L. & TAMM, L. K. (1995b). Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy. Biochemistry 34, 4448-4456.
    • (1995) Biochemistry , vol.34 , pp. 4448-4456
    • Tatulian, S.A.1    Jones, L.R.2    Reddy, L.G.3    Stokes, D.L.4    Tamm, L.K.5
  • 225
    • 0031584275 scopus 로고    scopus 로고
    • 2 induced by membrane binding: A clue to interfacial activation?
    • 2 induced by membrane binding: A clue to interfacial activation? J. Mol. Biol. 268, 809-815.
    • (1997) J. Mol. Biol. , vol.268 , pp. 809-815
    • Tatulian, S.A.1    Biltonen, R.2    Tamm, L.K.3
  • 226
    • 0020079526 scopus 로고
    • The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities
    • TERWILLIGER, T. C., WEISSMAN, L. & EISENBERG, D. (1982). The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities. Biophys. J. 37, 353-361.
    • (1982) Biophys. J. , vol.37 , pp. 353-361
    • Terwilliger, T.C.1    Weissman, L.2    Eisenberg, D.3
  • 229
    • 0001242101 scopus 로고
    • Infrared dichroism and molecular conformation of α-form poly-γ-benzyl-L-glutamate
    • TSUBOI, M. (1962). Infrared dichroism and molecular conformation of α-form poly-γ-benzyl-L-glutamate. J. Polymer Sci. 59, 139-153.
    • (1962) J. Polymer Sci. , vol.59 , pp. 139-153
    • Tsuboi, M.1
  • 230
    • 0028564769 scopus 로고
    • 2H-NMR studies of phospholipids differing in headgroup structure and chain length
    • 2H-NMR studies of phospholipids differing in headgroup structure and chain length. Eur. Biophys. J. 23, 323-335.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 323-335
    • Tuchtenhagen, J.1    Ziegler, W.2    Blume, A.3
  • 231
    • 0026614786 scopus 로고
    • 2+ to sulfogalactosylglyceramide and the sequential effect on the lipid dynamics
    • 2+ to sulfogalactosylglyceramide and the sequential effect on the lipid dynamics. Biochemistry 31, 11902-11907.
    • (1992) Biochemistry , vol.31 , pp. 11902-11907
    • Tupper, S.1    Wong, P.T.T.2    Tanphaichitr, N.3
  • 232
    • 0028004022 scopus 로고
    • Interaction of divalent cations with germ cell specific sulfogalactosylglycerolipid and the effect on lipid chain dynamics
    • TUPPER, S., WONG, P. T. T., KATES, M. & TANPHAICHITR, N. (1994). Interaction of divalent cations with germ cell specific sulfogalactosylglycerolipid and the effect on lipid chain dynamics. Biochemistry 33, 13250-13258.
    • (1994) Biochemistry , vol.33 , pp. 13250-13258
    • Tupper, S.1    Wong, P.T.T.2    Kates, M.3    Tanphaichitr, N.4
  • 233
    • 0028297760 scopus 로고
    • Local anesthetics destabilize lipid membranes by breaking hydration and shell: Infrared and calorimetric studies
    • UEDA, I., CHIOU, J.-S., KRISHNA, P. R. & KAMAYA, H. (1994). Local anesthetics destabilize lipid membranes by breaking hydration and shell: infrared and calorimetric studies. Biochim. Biophys. Acta 1190, 421-429.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 421-429
    • Ueda, I.1    Chiou, J.-S.2    Krishna, P.R.3    Kamaya, H.4
  • 234
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • UNWIN, N. (1993). Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229, 1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 235
    • 0026795207 scopus 로고
    • Secondary structure and orientation of the surfactant protein SP-B in a lipid environment. A Fourier transform infrared spectroscopic study
    • VANDENBUSSCHE, G., CLERCX, A., CLERCX, M., CURSTEDT, T., JOHANSSON, J., JÖRNVALL, H. & RUYSSCHAERT, J.-M. (1992a). Secondary structure and orientation of the surfactant protein SP-B in a lipid environment. A Fourier transform infrared spectroscopic study. Biochemistry 31, 9169-9176.
    • (1992) Biochemistry , vol.31 , pp. 9169-9176
    • Vandenbussche, G.1    Clercx, A.2    Clercx, M.3    Curstedt, T.4    Johansson, J.5    Jörnvall, H.6    Ruysschaert, J.-M.7
  • 237
    • 0025613794 scopus 로고
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 30, 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.U.1    Kalnin, N.N.2
  • 238
    • 0025648652 scopus 로고
    • 2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-, β-, and random coil conformations
    • 2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-, β-, and random coil conformations. Biopolymers 30, 1259-1271.
    • (1990) Biopolymers , vol.30 , pp. 1259-1271
    • Venyaminov, S.Y.U.1    Kalnin, N.N.2
  • 241
    • 0026739750 scopus 로고
    • Fourier transform infrared spectroscopic study of mixtures of palmitic acid with dipalmitoylphosphatidylcholine using isotopic substitution
    • VILLALAÍN, J. & GÓMEZ-FERNÁNDEZ, J. C. (1992). Fourier transform infrared spectroscopic study of mixtures of palmitic acid with dipalmitoylphosphatidylcholine using isotopic substitution. Chem. Phys. Lipids 62, 19-29.
    • (1992) Chem. Phys. Lipids , vol.62 , pp. 19-29
    • Villalaín, J.1    Gómez-fernández, J.C.2
  • 242
    • 0023248806 scopus 로고
    • Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes
    • VOGEL, H. (1987). Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes. Biochemistry 26, 4562-4572.
    • (1987) Biochemistry , vol.26 , pp. 4562-4572
    • Vogel, H.1
  • 243
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • VOGEL, H. & JÄHNIG, F. (1986). The structure of melittin in membranes. Biophys. J. 50, 573-582.
    • (1986) Biophys. J. , vol.50 , pp. 573-582
    • Vogel, H.1    Jähnig, F.2
  • 244
    • 0021097003 scopus 로고
    • The orientation of melittin in lipid membranes. A polarized infrared spectroscopic study
    • VOGEL, H., JÄHNIG, F., HOFFMANN, V. & STÜMPEL, J. (1983). The orientation of melittin in lipid membranes. A polarized infrared spectroscopic study. Biochim. Biophys. Acta 733, 201-209.
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 201-209
    • Vogel, H.1    Jähnig, F.2    Hoffmann, V.3    Stümpel, J.4
  • 245
    • 0030458792 scopus 로고    scopus 로고
    • Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: A Fourier-transform infrared spectroscopy approach
    • WANG, X.-M., MOCK, M., RUYSSCHAERT, J.-M. & CABIAUX, V. (1996). Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: a Fourier-transform infrared spectroscopy approach. Biochemistry 35, 14939-14946.
    • (1996) Biochemistry , vol.35 , pp. 14939-14946
    • Wang, X.-M.1    Mock, M.2    Ruysschaert, J.-M.3    Cabiaux, V.4
  • 246
  • 247
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • WEISS, M. S., ABELE, U., WECKESSER, J., WELTE, W., SCHILTZ, E. & SCHULZ, G. E. (1991). Molecular architecture and electrostatic properties of a bacterial porin. Science 254, 1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 248
    • 0001436178 scopus 로고
    • Supported phospholipid bilayers prepared by the 'LB/vesicle method': A Fourier transform infrared attenuated total reflection spectroscopic study on structure and stability
    • WENZL, P., FRINGELI, M., GOETTE, J. & FRINGELI, U. P. (1994). Supported phospholipid bilayers prepared by the 'LB/vesicle method': A Fourier transform infrared attenuated total reflection spectroscopic study on structure and stability. Langmuir 10, 4253-4264.
    • (1994) Langmuir , vol.10 , pp. 4253-4264
    • Wenzl, P.1    Fringeli, M.2    Goette, J.3    Fringeli, U.P.4
  • 249
    • 0001603906 scopus 로고
    • High pressure infrared spectroscopic evidence of water binding sites in 1,2-diacyl phospholipids
    • WONG, P. T. T. & MANTSCH, H. H. (1988). High pressure infrared spectroscopic evidence of water binding sites in 1,2-diacyl phospholipids. Chem. Phys. Lipids 46, 213-224.
    • (1988) Chem. Phys. Lipids , vol.46 , pp. 213-224
    • Wong, P.T.T.1    Mantsch, H.H.2
  • 250
    • 0026482964 scopus 로고
    • FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins
    • ZHANG, Y.-P., LEWIS, R. N. A. H., HODGES, R. S. & MCELHANEY, R. N. (1992a). FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins. Biochemistry 31, 11572-11578.
    • (1992) Biochemistry , vol.31 , pp. 11572-11578
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    Mcelhaney, R.N.4
  • 251
    • 0026442901 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
    • ZHANG, Y.-P., LEWIS, R. N. A. H., HODGES, R. S. & MCELHANEY, R. N. (1992b). Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies. Biochemistry 31, 11579-11588.
    • (1992) Biochemistry , vol.31 , pp. 11579-11588
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    Mcelhaney, R.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.