메뉴 건너뛰기




Volumn 71, Issue 5, 1996, Pages 2633-2644

High-resolution mono- and multidimensional magic angle spinning 1H nuclear magnetic resonance of membrane peptides in nondeuterated lipid membranes and H2O

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; HYDROPHOBICITY; LIPID ANALYSIS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PEPTIDE ANALYSIS; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; TOPOGRAPHY; WATER CONTENT;

EID: 0029998569     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79455-9     Document Type: Article
Times cited : (21)

References (51)
  • 1
    • 0021892874 scopus 로고
    • 1H-NMR study of gramicidin A transmembrane ion channel. Head-to-head right-handed, single-stranded helices
    • 1H-NMR study of gramicidin A transmembrane ion channel. Head-to-head right-handed, single-stranded helices. FEBS Lett. 186: 168-174.
    • (1985) FEBS Lett. , vol.186 , pp. 168-174
    • Arseniev, A.S.1    Barsukov, I.L.2    Lomize, A.L.3    Ovchinnikov, Y.A.4
  • 2
    • 0000905017 scopus 로고
    • Direct identification of relayed nuclear overhauser effect
    • Bax, A., V. Sklenár, and M. F. Summers. 1986. Direct identification of relayed nuclear overhauser effect. J. Magn. Reson. 70:327-331.
    • (1986) J. Magn. Reson. , vol.70 , pp. 327-331
    • Bax, A.1    Sklenár, V.2    Summers, M.F.3
  • 3
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., M. Zasloff, and S. J. Opella. 1993. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2:2077-2084
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 4
    • 0021744614 scopus 로고
    • Evidence for a folded conformation of methionine- and leucine-enkephalin in a membrane environment
    • Behnam, B. A., and C. M. Deber. 1984. Evidence for a folded conformation of methionine- and leucine-enkephalin in a membrane environment. J. Biol. Chem. 259:14935-14940.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14935-14940
    • Behnam, B.A.1    Deber, C.M.2
  • 5
    • 0001766053 scopus 로고
    • Observation of spin diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy
    • Boelens, R., G. H. Vuister, T. M. G. Koning, and R. Kaptein. 1989. Observation of spin diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy. J. Am. Chem. Soc. 111:8525-8526.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8525-8526
    • Boelens, R.1    Vuister, G.H.2    Koning, T.M.G.3    Kaptein, R.4
  • 6
    • 0028859424 scopus 로고
    • 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers
    • 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers. Biophys. J. 69:1933-1938.
    • (1995) Biophys. J. , vol.69 , pp. 1933-1938
    • Bouchard, M.1    Davis, J.H.2    Auger, M.3
  • 7
    • 0029883926 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of lipid hydration in monomethyldioleoylphosphatidylethanolamine dispersions
    • Chen, Z., L. C. M. Van Gorkom, R. M. Epand, and R. E. Stark. 1996. Nuclear magnetic resonance studies of lipid hydration in monomethyldioleoylphosphatidylethanolamine dispersions. Biophys. J. 70: 1412-1418.
    • (1996) Biophys. J. , vol.70 , pp. 1412-1418
    • Chen, Z.1    Van Gorkom, L.C.M.2    Epand, R.M.3    Stark, R.E.4
  • 9
    • 0028970552 scopus 로고
    • 1H nuclear magnetic resonance of a transmembrane peptide
    • 1H nuclear magnetic resonance of a transmembrane peptide. Biophys. J. 69:1917-1932.
    • (1995) Biophys. J. , vol.69 , pp. 1917-1932
    • Davis, J.H.1    Auger, M.2    Hodges, R.S.3
  • 10
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., S. Grzesiek, G. Vuister, G. Zhu, J. Pfeifer, and A. Bax. 1995. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 11
    • 0001501402 scopus 로고
    • Some new developments in solid-state nuclear magnetic resonance spectroscopic studies of lipids and biological membranes, including the effects of cholesterol in model and natural systems
    • Forbes, J., J. Bowers, X. Shan, L. Moran, E. Oldfield, and M. Moscarello. 1988a. Some new developments in solid-state nuclear magnetic resonance spectroscopic studies of lipids and biological membranes, including the effects of cholesterol in model and natural systems. J. Chem. Soc. (Faraday 1). 84:3821-3849.
    • (1988) J. Chem. Soc. (Faraday 1) , vol.84 , pp. 3821-3849
    • Forbes, J.1    Bowers, J.2    Shan, X.3    Moran, L.4    Oldfield, E.5    Moscarello, M.6
  • 12
    • 0023962259 scopus 로고
    • High-field, high-resolution proton "magic-angle" sample-spinning nuclear magnetic resonance spectroscopic studies of gel and liquid crystalline lipid bilayers and the effects of cholesterol
    • Forbes, J., C. Husted, and E. Oldfield. 1988b. High-field, high-resolution proton "magic-angle" sample-spinning nuclear magnetic resonance spectroscopic studies of gel and liquid crystalline lipid bilayers and the effects of cholesterol. J. Am. Chem. Soc. 110:1059-1065.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1059-1065
    • Forbes, J.1    Husted, C.2    Oldfield, E.3
  • 14
    • 0001210528 scopus 로고
    • FLATT- A new procedure for high-quality baseline correction of multidimensional NMR spectra
    • Güntert, P., and K. Wüthrich. 1992. FLATT- a new procedure for high-quality baseline correction of multidimensional NMR spectra. J. Magn. Reson. 96:403-407.
    • (1992) J. Magn. Reson. , vol.96 , pp. 403-407
    • Güntert, P.1    Wüthrich, K.2
  • 15
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • Henry, G. D., and B. D. Sykes. 1994. Methods to study membrane protein structure in solution. Methods Enzymol. 239:515-535.
    • (1994) Methods Enzymol. , vol.239 , pp. 515-535
    • Henry, G.D.1    Sykes, B.D.2
  • 16
    • 0028882402 scopus 로고
    • Tryptophan dynamics and structural refinement in a lipid bilayer environment: Solid state NMR of the gramicidin channel
    • Hu, W., N. D. Lazo, and T. A. Cross. 1995. Tryptophan dynamics and structural refinement in a lipid bilayer environment: solid state NMR of the gramicidin channel. Biochemistry. 34:14138-14146.
    • (1995) Biochemistry , vol.34 , pp. 14138-14146
    • Hu, W.1    Lazo, N.D.2    Cross, T.A.3
  • 17
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem, R. R., W. Hu, and T. A. Cross. 1993. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science. 261:1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 18
    • 0023733886 scopus 로고
    • The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes
    • Killian, J. A., K. U. Prasad, D. Hains, and D. W. Urry. 1988. The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes. Biochemistry. 27:4848-4855.
    • (1988) Biochemistry , vol.27 , pp. 4848-4855
    • Killian, J.A.1    Prasad, K.U.2    Hains, D.3    Urry, D.W.4
  • 20
    • 0028347590 scopus 로고
    • Side-chain structure and dynamics at the lipid-protein interface: Vall of the gramicidin A channel
    • Lee, K. C., and T. A. Cross, 1994. Side-chain structure and dynamics at the lipid-protein interface: Vall of the gramicidin A channel. Biophys. J. 66:1380-1387.
    • (1994) Biophys. J. , vol.66 , pp. 1380-1387
    • Lee, K.C.1    Cross, T.A.2
  • 21
    • 0030239096 scopus 로고    scopus 로고
    • Band-selective 3D NOESYTOCSY: Measurement of through-space correlations between aliphatic protons of membrane peptides and proteins in non-deuterated detergents
    • In press
    • Le Guernevé, C. and M. Seigneuret. 1996. Band-selective 3D NOESYTOCSY: measurement of through-space correlations between aliphatic protons of membrane peptides and proteins in non-deuterated detergents. J. Biomol. NMR. In press.
    • (1996) J. Biomol. NMR
    • Le Guernevé, C.1    Seigneuret, M.2
  • 22
    • 0000081715 scopus 로고
    • A direct approach of molecular structures determination from nuclear overhauser effect
    • Malliavin, T. E., A. Rouh, M. A. Delsuc, and J. Y. Lallemand. 1992. A direct approach of molecular structures determination from nuclear overhauser effect. C R. Acad. Sci. Paris Ser: II. 315:653-659.
    • (1992) C R. Acad. Sci. Paris Ser: II , vol.315 , pp. 653-659
    • Malliavin, T.E.1    Rouh, A.2    Delsuc, M.A.3    Lallemand, J.Y.4
  • 23
    • 0342955552 scopus 로고
    • 1, noise and solvent artifacts from NMR spectra
    • 1, noise and solvent artifacts from NMR spectra. J. Biomol. NMR. 2:485-494.
    • (1992) J. Biomol. NMR , vol.2 , pp. 485-494
    • Manoleras, N.1    Norton, R.S.2
  • 24
    • 0025105211 scopus 로고
    • 1H nuclear magnetic resonance: Correlation between activities and membrane-bound conformations
    • 1H nuclear magnetic resonance: correlation between activities and membrane-bound conformations. Biochemistry. 29:65-75.
    • (1990) Biochemistry , vol.29 , pp. 65-75
    • Milon, A.1    Miyazawa, T.2    Higashijima, T.3
  • 25
    • 0025743856 scopus 로고
    • Peptides that mimic the pseudosub-strate region of protein kinase C bind to acidic lipids in membranes
    • Mosior, M., and S. McLaughlin. 1991. Peptides that mimic the pseudosub-strate region of protein kinase C bind to acidic lipids in membranes. Biophys. J. 60:149-159.
    • (1991) Biophys. J. , vol.60 , pp. 149-159
    • Mosior, M.1    McLaughlin, S.2
  • 28
    • 0029024518 scopus 로고
    • Correlation between function and dynamics: Time scale coincidence for ion translocation and molecular dynamics in the gramicidin channel backbone
    • North, C. L., and T. A. Cross. 1995. Correlation between function and dynamics: time scale coincidence for ion translocation and molecular dynamics in the gramicidin channel backbone. Biochemistry. 34: 5883-5895.
    • (1995) Biochemistry , vol.34 , pp. 5883-5895
    • North, C.L.1    Cross, T.A.2
  • 29
    • 0023643423 scopus 로고
    • High-resolution proton and carbon-13 NMR of membranes: Why sonicate?
    • Oldfield, E., J. L. Bowers, and J. Forbes. 1987. High-resolution proton and carbon-13 NMR of membranes: why sonicate? Biochemistry. 26: 6919-6923.
    • (1987) Biochemistry , vol.26 , pp. 6919-6923
    • Oldfield, E.1    Bowers, J.L.2    Forbes, J.3
  • 30
    • 0028674168 scopus 로고
    • Experimental nuclear magnetic resonance studies of membrane proteins
    • Opella, S. J., Y. Kim, and P. McDonnell. 1994. Experimental nuclear magnetic resonance studies of membrane proteins. Methods Enzymol. 239:536-560.
    • (1994) Methods Enzymol. , vol.239 , pp. 536-560
    • Opella, S.J.1    Kim, Y.2    McDonnell, P.3
  • 31
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • Otting, G., E. Liepinsh, and K. Wüthrich. 1991. Protein hydration in aqueous solution. Science. 254:974-980.
    • (1991) Science , vol.254 , pp. 974-980
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 32
    • 0028019692 scopus 로고
    • Location of M13 coat protein in sodium dodecy sulfate micelles as determined by NMR
    • Papavoine, C. H. M., R. N. H. Konings, C. W. Hilbers, and F. J. M. van de Ven. 1994. Location of M13 coat protein in sodium dodecy sulfate micelles as determined by NMR. Biochemistry. 33:12990-12997.
    • (1994) Biochemistry , vol.33 , pp. 12990-12997
    • Papavoine, C.H.M.1    Konings, R.N.H.2    Hilbers, C.W.3    Van De Ven, F.J.M.4
  • 34
    • 33845555707 scopus 로고
    • Exchangeable protons NMR without baseline distortions using new strong pulse sequences
    • Plateau, P., and M. Guéron. 1992. Exchangeable protons NMR without baseline distortions using new strong pulse sequences. J Am. Chem. Soc. 104:7310-7311.
    • (1992) J Am. Chem. Soc. , vol.104 , pp. 7310-7311
    • Plateau, P.1    Guéron, M.2
  • 35
    • 0028210494 scopus 로고
    • The structure of an integral membrane peptide: A deuterium NMR study of gramicidin
    • Prosser, R. S., S. I. Daleman, and J. H. Davis. 1994. The structure of an integral membrane peptide: a deuterium NMR study of gramicidin. Biophys J. 66:1415-1428.
    • (1994) Biophys J. , vol.66 , pp. 1415-1428
    • Prosser, R.S.1    Daleman, S.I.2    Davis, J.H.3
  • 36
    • 0028330797 scopus 로고
    • Dynamics of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin
    • Prosser, R. S., and J. H. Davis, 1994. Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin. Biophys. J. 66:1429-1440.
    • (1994) Biophys. J. , vol.66 , pp. 1429-1440
    • Prosser, R.S.1    Davis, J.H.2
  • 37
    • 58149363595 scopus 로고
    • The use of band filtering multidimensional NMR. Evaluation of two "user-friendly" techniques
    • Roumestand, C., J. Mispelter, C. Austruy, and D. Canet. 1995. The use of band filtering multidimensional NMR. Evaluation of two "user-friendly" techniques. J. Magn. Reson. B109:153-163.
    • (1995) J. Magn. Reson. , vol.B109 , pp. 153-163
    • Roumestand, C.1    Mispelter, J.2    Austruy, C.3    Canet, D.4
  • 38
    • 0028947465 scopus 로고
    • Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies
    • Sanders, C. R., and G. C. Landis. 1995. Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies. Biochemistry. 34:4030-4040.
    • (1995) Biochemistry , vol.34 , pp. 4030-4040
    • Sanders, C.R.1    Landis, G.C.2
  • 39
    • 0029314345 scopus 로고
    • 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: Application to mastoparan X solubilized in noctylglucoside
    • 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in noctylglucoside. J. Biomol. NMR 5:345-352
    • (1995) J. Biomol. NMR , vol.5 , pp. 345-352
    • Seigneuret, M.1    Lévy, D.2
  • 40
    • 0000840974 scopus 로고
    • 1H magic angle spinning nuclear magnetic resonance spectra
    • 1H magic angle spinning nuclear magnetic resonance spectra. Chem. Phys. Lett. 171:155-160.
    • (1990) Chem. Phys. Lett. , vol.171 , pp. 155-160
    • Sekine, S.1    Kubo, A.2    Sano, H.3
  • 41
    • 38249017383 scopus 로고
    • Acquisition schemes and quadrature artifacts in phase-sensitive two dimensional NMR
    • Simorre, J. P., and D. Marion. 1990. Acquisition schemes and quadrature artifacts in phase-sensitive two dimensional NMR. J. Magn. Reson. 89:191-197.
    • (1990) J. Magn. Reson. , vol.89 , pp. 191-197
    • Simorre, J.P.1    Marion, D.2
  • 42
    • 0027517644 scopus 로고
    • Magic angle spinning NMR methods for internuclear distance measurements
    • Smith, S. O. 1993. Magic angle spinning NMR methods for internuclear distance measurements. Curr. Opin. Struct. Biol. 3:755-759.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 755-759
    • Smith, S.O.1
  • 43
    • 0028814024 scopus 로고
    • Determination of helix-helix interactions in membranes by rotational resonance NMR
    • Smith, S. O., and B. J. Borman. 1995. Determination of helix-helix interactions in membranes by rotational resonance NMR. Proc. Natl. Acad. Sci. USA. 92:488-491.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 488-491
    • Smith, S.O.1    Borman, B.J.2
  • 44
    • 0028332081 scopus 로고
    • Rotational resonance NMR determination of intra- and intermolecular distance constraints in dipalmitoylphosphatidylcholine bilayers
    • Smith, S. O., J. Hamilton, and A. Salmon, and B. J. Bormann. 1994. Rotational resonance NMR determination of intra- and intermolecular distance constraints in dipalmitoylphosphatidylcholine bilayers. Biochemistry. 33:6327-6333.
    • (1994) Biochemistry , vol.33 , pp. 6327-6333
    • Smith, S.O.1    Hamilton, J.2    Salmon, A.3    Bormann, B.J.4
  • 45
    • 0026695584 scopus 로고
    • Solid-state NMR approaches for studying membrane protein structure
    • Smith, S. O., and O. B. Peersen. 1992. Solid-state NMR approaches for studying membrane protein structure. Annu. Rev. Biophys. Biomol. Struct. 21:25-47.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 25-47
    • Smith, S.O.1    Peersen, O.B.2
  • 47
    • 0029204438 scopus 로고
    • 1H MASS NMR spectra of lipids and biological membranes
    • 1H MASS NMR spectra of lipids and biological membranes. J. Magn. Reson. B106:76-79.
    • (1995) J. Magn. Reson. , vol.B106 , pp. 76-79
    • Warschawski, D.1    Devaux, P.2
  • 48
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Woolf, T. B., and B. Roux. 1996. Structure, energetics and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins. 24:92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 50
    • 0027359226 scopus 로고
    • The antiviral peptide carbobenzoxy-D-phenylalanyl-L-phenylalanylglycine changes the average conformation of phospholipids in membranes
    • Yeagle, P. L., A. R. Dentino, F. T. Smith, P. Spooner, and A. Watts, 1993. The antiviral peptide carbobenzoxy-D-phenylalanyl-L-phenylalanylglycine changes the average conformation of phospholipids in membranes. Biochemistry. 32:12197-12202.
    • (1993) Biochemistry , vol.32 , pp. 12197-12202
    • Yeagle, P.L.1    Dentino, A.R.2    Smith, F.T.3    Spooner, P.4    Watts, A.5
  • 51
    • 0000198241 scopus 로고
    • Improved linear prediction of damped NMR signals using modified "forward-backward" linear prediction
    • Zhu, G., and A. Bax. 1992. Improved linear prediction of damped NMR signals using modified "forward-backward" linear prediction. J. Magn. Reson. 100:202-207.
    • (1992) J. Magn. Reson. , vol.100 , pp. 202-207
    • Zhu, G.1    Bax, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.