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Volumn 25, Issue 1-3, 2004, Pages 5-14

Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CENTRIFUGATION; CHROMOPHORES; CONFORMATIONS; CRYSTAL STRUCTURE; INTERFACES (MATERIALS); MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYPEPTIDES; RELAXATION PROCESSES; STEREOCHEMISTRY; SYNTHESIS (CHEMICAL); X RAY DIFFRACTION ANALYSIS;

EID: 0346343096     PISSN: 09262040     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ssnmr.2003.06.001     Document Type: Article
Times cited : (11)

References (35)
  • 3
    • 0032986388 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure
    • Fu R., Cross T.A. Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure. Annu. Rev. Biophys. Biomol. Struct. 28:1999;235-268.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 235-268
    • Fu, R.1    Cross, T.A.2
  • 5
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula P.E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, P.E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 6
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke H., Richter H.T., Lanyi J.K. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science. 280:1998;1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 7
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L.O., Siegert R., Lehmann W.D., Oesterhelt D. Lipid patches in membrane protein oligomers. crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. USA. 95:1998;11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 9
    • 77956853496 scopus 로고
    • High-resolution solid-state NMR studies of synthetic and biological macromolecules
    • Saitô H., Ando I. High-resolution solid-state NMR studies of synthetic and biological macromolecules. Annu. Rep. NMR Spectrosc. 21:1989;209-290.
    • (1989) Annu. Rep. NMR Spectrosc. , vol.21 , pp. 209-290
    • Saitô, H.1    Ando, I.2
  • 10
    • 77956739241 scopus 로고    scopus 로고
    • Empirical versus nonempirical evaluation of secondary structure of fibrous and membrane proteins by solid-state NMR: A practical approach
    • Saitô H., Tuzi S., Naito A. Empirical versus nonempirical evaluation of secondary structure of fibrous and membrane proteins by solid-state NMR. a practical approach Annu. Rep. NMR Spectrosc. 36:1998;79-121.
    • (1998) Annu. Rep. NMR Spectrosc. , vol.36 , pp. 79-121
    • Saitô, H.1    Tuzi, S.2    Naito, A.3
  • 15
    • 36749105542 scopus 로고
    • Transverse relaxation of dipolar coupled spin system under rf irradiation: Detecting motions in solid
    • Rothwell W.T., Waugh J.S. Transverse relaxation of dipolar coupled spin system under rf irradiation. detecting motions in solid J. Chem. Phys. 75:1981;2721-2732.
    • (1981) J. Chem. Phys. , vol.75 , pp. 2721-2732
    • Rothwell, W.T.1    Waugh, J.S.2
  • 16
    • 0000570050 scopus 로고
    • Slow molecular motion detected in the NMR spectra of rotating solids
    • Suwelack D., Rothwell W.P., Waugh J.S. Slow molecular motion detected in the NMR spectra of rotating solids. J. Chem. Phys. 73:1980;2559-2569.
    • (1980) J. Chem. Phys. , vol.73 , pp. 2559-2569
    • Suwelack, D.1    Rothwell, W.P.2    Waugh, J.S.3
  • 17
    • 0000900292 scopus 로고
    • A synthetic medium for extremely halophilic bacteria
    • Onishi H., McCance E.M., Gibbons N.E. A synthetic medium for extremely halophilic bacteria. Can. J. Microbiol. 11:1965;365-373.
    • (1965) Can. J. Microbiol. , vol.11 , pp. 365-373
    • Onishi, H.1    Mccance, E.M.2    Gibbons, N.E.3
  • 18
    • 0025924636 scopus 로고
    • Properties of Asp212 - Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base
    • Needleman R., Chang M., Ni B., Varo G., Fornes J., White S.H., Lanyi J.K. Properties of Asp212 - Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base. J. Biol. Chem. 266:1991;11478-11484.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11478-11484
    • Needleman, R.1    Chang, M.2    Ni, B.3    Varo, G.4    Fornes, J.5    White, S.H.6    Lanyi, J.K.7
  • 19
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D., Stoeckenius W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:1974;667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 27
    • 36849117843 scopus 로고
    • Proton relaxation times in paramagnetic solutions
    • Bloembergen N. Proton relaxation times in paramagnetic solutions. J. Chem. Phys. 27:1957;572-573.
    • (1957) J. Chem. Phys. , vol.27 , pp. 572-573
    • Bloembergen, N.1
  • 28
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon I. Relaxation processes in a system of two spins. Phys. Rev. 99:1955;559-565.
    • (1955) Phys. Rev. , vol.99 , pp. 559-565
    • Solomon, I.1
  • 31
    • 0029181728 scopus 로고
    • 15N Random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N Random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR. 5:1995;67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Biga, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 32
    • 0035148603 scopus 로고    scopus 로고
    • 13C]Val-labeled transmembrane peptides of bacteriorhodopsin in lipid bilayers: Insertion, rigid-body motions, and local conformational fluctuations at ambient temperature
    • 13C] Val-labeled transmembrane peptides of bacteriorhodopsin in lipid bilayers. insertion, rigid-body motions, and local conformational fluctuations at ambient temperature Biopolymers. 58:2001;78-88.
    • (2001) Biopolymers , vol.58 , pp. 78-88
    • Kimura, S.1    Naito, A.2    Tuzi, S.3    Saitô, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.