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Volumn 135, Issue 1, 1998, Pages 227-231

Orientational Constraints Derived from Hydrated Powder Samples by Two-Dimensional PISEMA

Author keywords

[No Author keywords available]

Indexed keywords

GRAMICIDIN;

EID: 0032209501     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1998.1544     Document Type: Editorial
Times cited : (18)

References (30)
  • 1
    • 43949172938 scopus 로고
    • Local-field measurements on powder samples from polarization inversion of the rare-spin magnetization
    • P. Palmas, P. Tekely, and D. Canet, Local-field measurements on powder samples from polarization inversion of the rare-spin magnetization, J. Magn. Reson. A 104, 26-36 (1993).
    • (1993) J. Magn. Reson. A , vol.104 , pp. 26-36
    • Palmas, P.1    Tekely, P.2    Canet, D.3
  • 2
    • 0017902280 scopus 로고
    • 31 P Nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • 31 P Nuclear magnetic resonance and the head group structure of phospholipids in membranes, Biochim. Biophys. Acta 515, 105-140 (1978).
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 3
    • 33846595904 scopus 로고
    • High-resolution heteronuclear dipolar solid-state NMR spectroscopy
    • C. H. Wu, A. Ramamoorthy, and S. J. Opella, High-resolution heteronuclear dipolar solid-state NMR spectroscopy, J. Magn. Reson. A 109, 270-272 (1994).
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 4
    • 0028025665 scopus 로고
    • Solid-state NMR structural studies of peptides and proteins in membrane
    • T. A. Cross and S. J. Opella, Solid-state NMR structural studies of peptides and proteins in membrane, Curr. Opin. Struct. Biol. 4, 574-581 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 574-581
    • Cross, T.A.1    Opella, S.J.2
  • 5
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • R. R. Ketchem, W. Hu, and T. A. Cross, High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR, Science 261, 1457-1460 (1993).
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 6
    • 0031574382 scopus 로고    scopus 로고
    • High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints
    • R. R. Ketchem, B. Roux, and T. A. Cross, High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints, Structure 5, 1655-1669 (1997).
    • (1997) Structure , vol.5 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 7
    • 77956819892 scopus 로고
    • Structural biology of peptide and proteins in synthetic membrane environments by solid-state NMR spectroscopy
    • T. A. Cross, Structural biology of peptide and proteins in synthetic membrane environments by solid-state NMR spectroscopy, Annu. Rep. NMR Spectrosc. 29, 124-158 (1994).
    • (1994) Annu. Rep. NMR Spectrosc. , vol.29 , pp. 124-158
    • Cross, T.A.1
  • 8
    • 0030861070 scopus 로고    scopus 로고
    • NMR and membrane proteins
    • S. J. Opella, NMR and membrane proteins, Nat. Struct. Biol. 4, (Suppl.) 845-848 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , Issue.SUPPL. , pp. 845-848
    • Opella, S.J.1
  • 10
    • 0031891529 scopus 로고    scopus 로고
    • Solid-state NMR-studies of the membrane-bound closed state of the Colicin E1 channel domain in lipid bilayers
    • Y. Kim, K. Valentine, S. J. Opella, S. L. Schendel, and W. A. Cramer, Solid-state NMR-studies of the membrane-bound closed state of the Colicin E1 channel domain in lipid bilayers, Protein Sci. 7, 342-348 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 342-348
    • Kim, Y.1    Valentine, K.2    Opella, S.J.3    Schendel, S.L.4    Cramer, W.A.5
  • 11
    • 0025101067 scopus 로고
    • Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D
    • F. D. Moll and T. A. Cross, Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D, Biophys. J. 57, 351-362 (1990).
    • (1990) Biophys. J. , vol.57 , pp. 351-362
    • Moll, F.D.1    Cross, T.A.2
  • 12
    • 0001147747 scopus 로고    scopus 로고
    • Preparation of oriented lipid bilayer on ultrathin polymers for solid-state NMR analyses of peptide-membrane interactions
    • S. Auge, H. Mazarguil, M. Tropis, and A. Milon, Preparation of oriented lipid bilayer on ultrathin polymers for solid-state NMR analyses of peptide-membrane interactions, J. Magn. Reson. 124, 455-458 (1997).
    • (1997) J. Magn. Reson. , vol.124 , pp. 455-458
    • Auge, S.1    Mazarguil, H.2    Tropis, M.3    Milon, A.4
  • 13
    • 0001641659 scopus 로고
    • Improving sensitivity in mechanically oriented phospholipid bilayers using ultrathin plates - A deuterium solid-state NMR study
    • R. S. Prosser, S. A. Hunt, and R. R. Void, Improving sensitivity in mechanically oriented phospholipid bilayers using ultrathin plates - A deuterium solid-state NMR study, J. Magn. Reson. B 109, 109-111 (1995).
    • (1995) J. Magn. Reson. B , vol.109 , pp. 109-111
    • Prosser, R.S.1    Hunt, S.A.2    Void, R.R.3
  • 14
    • 0025182649 scopus 로고
    • Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO
    • I. Sander and J. H. Prestegard, Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO, Biophys. J. 58, 447-460 (1990).
    • (1990) Biophys. J. , vol.58 , pp. 447-460
    • Sander, I.1    Prestegard, J.H.2
  • 16
    • 36149023808 scopus 로고
    • Nuclear-magnetic-resonance line narrowing by a rotating rf field
    • M. Lee and W. I. Goldburg, Nuclear-magnetic-resonance line narrowing by a rotating rf field, Phys. Rev. A 140, 1261-1271 (1965).
    • (1965) Phys. Rev. A , vol.140 , pp. 1261-1271
    • Lee, M.1    Goldburg, W.I.2
  • 17
    • 0002377859 scopus 로고
    • Frequency-switched pulse sequences: Homonuclear decoupling and dilute spin NMR in solids
    • A. Bielecki, A. C. Kolbert, and M. H. Levitt, Frequency-switched pulse sequences: Homonuclear decoupling and dilute spin NMR in solids, Chem. Phys. Lett. 155, 341-346 (1989).
    • (1989) Chem. Phys. Lett. , vol.155 , pp. 341-346
    • Bielecki, A.1    Kolbert, A.C.2    Levitt, M.H.3
  • 19
    • 0016958780 scopus 로고
    • Uncoupling of local field spectra in nuclear magnetic resonance: Determination of atomic positions in solids
    • J. S. Waugh, Uncoupling of local field spectra in nuclear magnetic resonance: Determination of atomic positions in solids, Proc. Natl. Acad. Sci. USA 73, 1394-1397 (1976).
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1394-1397
    • Waugh, J.S.1
  • 20
    • 0021288949 scopus 로고
    • Gramicidin channels
    • O. S. Andersen, Gramicidin channels, Ann. Rev. Physiol. 46, 531-548 (1984).
    • (1984) Ann. Rev. Physiol. , vol.46 , pp. 531-548
    • Andersen, O.S.1
  • 21
    • 0027533833 scopus 로고
    • The use of physical methods in determining gramicidin channel structure and function
    • D. D. Busath, The use of physical methods in determining gramicidin channel structure and function, Annu. Rev. Physiol. 55, 473-501 (1993).
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 473-501
    • Busath, D.D.1
  • 22
    • 0027329868 scopus 로고
    • 2 H NMR determination of the global correlation time of the gramicidin channel in a lipid bilayer
    • 2 H NMR determination of the global correlation time of the gramicidin channel in a lipid bilayer, Biophys. J. 65, 1162-1167 (1993).
    • (1993) Biophys. J. , vol.65 , pp. 1162-1167
    • Lee, K.C.1    Hu, W.2    Cross, T.A.3
  • 23
    • 0029024518 scopus 로고
    • Correlations between function and dynamics: Time scale coincidence for ion translocation and molecular dynamics in the gramicidin channel backbone
    • C. L. North and T. A. Cross, Correlations between function and dynamics: Time scale coincidence for ion translocation and molecular dynamics in the gramicidin channel backbone, Biochemistry 34, 5883-5895 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5883-5895
    • North, C.L.1    Cross, T.A.2
  • 24
    • 0027503130 scopus 로고
    • Orientational constraints as three-dimensional structural constraints from chemical shift anisotropy: The polypeptide backbone of gramicidin A in a lipid bilayer
    • W. Mai, W. Hu, C. Wang, and T. A. Cross, Orientational constraints as three-dimensional structural constraints from chemical shift anisotropy: The polypeptide backbone of gramicidin A in a lipid bilayer, Protein Sci. 2, 532-542 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 532-542
    • Mai, W.1    Hu, W.2    Wang, C.3    Cross, T.A.4
  • 26
    • 0001326066 scopus 로고
    • Deformation electron density of α-glycylglycine at 82K. 1. The neutron diffraction study
    • A. Kvick, A. R. Al-Karaghouli, and T. F. Koetzle, Deformation electron density of α-glycylglycine at 82K. 1. The neutron diffraction study, Acta Crystallogr. B 33, 3796-3801 (1977).
    • (1977) Acta Crystallogr. B , vol.33 , pp. 3796-3801
    • Kvick, A.1    Al-Karaghouli, A.R.2    Koetzle, T.F.3
  • 27
    • 0001977233 scopus 로고
    • Orientation-dependent deuteron spin-lattice relaxation times in bilayer membranes: Characterization of the overall lipid motion
    • C. Mayer, G. Gröbner, K. Müller, K. Weisz, and G. Kothe, Orientation-dependent deuteron spin-lattice relaxation times in bilayer membranes: Characterization of the overall lipid motion, Chem. Phys. Lett. 165, 155-161 (1990).
    • (1990) Chem. Phys. Lett. , vol.165 , pp. 155-161
    • Mayer, C.1    Gröbner, G.2    Müller, K.3    Weisz, K.4    Kothe, G.5
  • 29
    • 33646291925 scopus 로고
    • Transient oscillations in NMR cross-polarization experiments in solids
    • L. Müller, A. Kumar, T. Baumann, and R. R. Ernst, Transient oscillations in NMR cross-polarization experiments in solids, Phys. Rev. Lett. 32, 1402-1406 (1974).
    • (1974) Phys. Rev. Lett. , vol.32 , pp. 1402-1406
    • Müller, L.1    Kumar, A.2    Baumann, T.3    Ernst, R.R.4
  • 30
    • 0000269597 scopus 로고
    • Resolved dipolar coupling spectra of dilute nuclear spins in solids
    • R. K. Hester, J. L. Ackerman, V. R. Cross, and J. S. Waugh, Resolved dipolar coupling spectra of dilute nuclear spins in solids, Phys. Rev. Lett. 34, 993-995 (1975).
    • (1975) Phys. Rev. Lett. , vol.34 , pp. 993-995
    • Hester, R.K.1    Ackerman, J.L.2    Cross, V.R.3    Waugh, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.