메뉴 건너뛰기




Volumn 75, Issue 6, 1998, Pages 2794-2800

Weak substrate binding to transport proteins studied by NMR

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBON 13; CARRIER PROTEIN; FUCOSE; GALACTOSE; LEVO FUCOSE; PROTON; SUGAR; UNCLASSIFIED DRUG;

EID: 0031768107     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77722-7     Document Type: Article
Times cited : (23)

References (25)
  • 4
    • 0344522336 scopus 로고
    • A line shape analysis of the effects introduced by motions in the nuclear magnetic resonance spectra of decoupled systems
    • Frydman, L., and B. Frydman. 1990. A line shape analysis of the effects introduced by motions in the nuclear magnetic resonance spectra of decoupled systems. J. Chem. Phys. 92:1620-1626.
    • (1990) J. Chem. Phys. , vol.92 , pp. 1620-1626
    • Frydman, L.1    Frydman, B.2
  • 5
    • 85011817347 scopus 로고
    • Detection of weak heteronuclear dipolar couplings by rotational-echo double resonance nuclear magnetic resonance
    • edited by Warren, W. S. Academic Press, New York
    • Gullian, T., and J. Schaefer. 1989. Detection of weak heteronuclear dipolar couplings by rotational-echo double resonance nuclear magnetic resonance. In Advances In Magnetic Resonance, edited by Warren, W. S. Academic Press, New York. 57-83.
    • (1989) Advances in Magnetic Resonance , pp. 57-83
    • Gullian, T.1    Schaefer, J.2
  • 6
    • 0028240991 scopus 로고
    • + symport protein, FucP, for transport of L-fucose into Escherichia coli
    • + symport protein, FucP, for transport of L-fucose into Escherichia coli. Mol. Microbiol. 12:799-809.
    • (1994) Mol. Microbiol. , vol.12 , pp. 799-809
    • Gunn, P.J.1    Tate, C.G.2    Henderson, P.J.F.3
  • 8
    • 0001369427 scopus 로고
    • Spin-lattice relaxation in periodically perturbed systems
    • Haeberlen, U., and J. S. Waugh. 1969. Spin-lattice relaxation in periodically perturbed systems. Phys. Rev. 185:420-429.
    • (1969) Phys. Rev. , vol.185 , pp. 420-429
    • Haeberlen, U.1    Waugh, J.S.2
  • 9
    • 0027640474 scopus 로고
    • The 12-transmembrane helix transporters
    • Henderson, P. J. F. 1993. The 12-transmembrane helix transporters. Curr. Opin. Cell Biol. 5:708-721.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 708-721
    • Henderson, P.J.F.1
  • 10
    • 0022558561 scopus 로고
    • Assays, genetics, and reconstitution of proton-linked galactose, arabinose, and xylose transport systems of Escherichia coli
    • Henderson, P. J. F., and A. J. S. Macpherson. 1985. Assays, genetics, and reconstitution of proton-linked galactose, arabinose, and xylose transport systems of Escherichia coli. Methods Enzymol. 125:387-429.
    • (1985) Methods Enzymol. , vol.125 , pp. 387-429
    • Henderson, P.J.F.1    Macpherson, A.J.S.2
  • 11
    • 36549091040 scopus 로고
    • Theory and simulations of homonuclear spin pair systems in rotating solids
    • Levitt, M. H., D. P. Raleigh, F. Creuzet, and R. G. Griffin. 1990. Theory and simulations of homonuclear spin pair systems in rotating solids. J. Chem. Phys.92:6347-6364.
    • (1990) J. Chem. Phys. , vol.92 , pp. 6347-6364
    • Levitt, M.H.1    Raleigh, D.P.2    Creuzet, F.3    Griffin, R.G.4
  • 13
    • 0028673158 scopus 로고
    • Protein-ligand interactions: Exchange processes and determination of ligand conformation and protein-ligand contacts
    • Lian, L. Y., I. L. Barsukov, M. J. Sutcliffe, K. H. Sze, and G. C. K. Roberts. 1994. Protein-ligand interactions: exchange processes and determination of ligand conformation and protein-ligand contacts. Methods Enzymol. 239:657-700.
    • (1994) Methods Enzymol. , vol.239 , pp. 657-700
    • Lian, L.Y.1    Barsukov, I.L.2    Sutcliffe, M.J.3    Sze, K.H.4    Roberts, G.C.K.5
  • 16
    • 0000539530 scopus 로고
    • NMR of rotating solids
    • Maricq, M. M., and J. S. Waugh. 1979. NMR of rotating solids. J. Chem. Phys. 70:3300-3316.
    • (1979) J. Chem. Phys. , vol.70 , pp. 3300-3316
    • Maricq, M.M.1    Waugh, J.S.2
  • 17
    • 0025370553 scopus 로고
    • Osmochemistry of solute translocation
    • Mitchell, P. 1990. Osmochemistry of solute translocation. Res. Microbiol. 141:286-289.
    • (1990) Res. Microbiol. , vol.141 , pp. 286-289
    • Mitchell, P.1
  • 18
    • 0027529417 scopus 로고
    • Proton-linked L-rhamnose transport, and it comparison with L-fucose transport in Enterobacteriaceae
    • Muiry, J. A. R., T. C. Gunn, T. P. McDonald, S. A. Bradley, C. G. Tate, and P. J. F. Henderson. 1993. Proton-linked L-rhamnose transport, and it comparison with L-fucose transport in Enterobacteriaceae. Biochem. J. 290:833-842.
    • (1993) Biochem. J. , vol.290 , pp. 833-842
    • Muiry, J.A.R.1    Gunn, T.C.2    McDonald, T.P.3    Bradley, S.A.4    Tate, C.G.5    Henderson, P.J.F.6
  • 20
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W., and C. Weissmann. 1973. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:502-517.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-517
    • Schaffner, W.1    Weissmann, C.2
  • 21
    • 0027164927 scopus 로고
    • Dynamics in a protein-lipid complex: Nuclear magnetic resonance measurements on the headgroup of cardiolipin when bound to cytochrome c
    • Spooner, P. J. R., A. A. Duralski, S. E. Rankin, T. J. T. Pinheiro, and A. Watts. 1993. Dynamics in a protein-lipid complex: nuclear magnetic resonance measurements on the headgroup of cardiolipin when bound to cytochrome c. Biophys J. 65:106-112.
    • (1993) Biophys J. , vol.65 , pp. 106-112
    • Spooner, P.J.R.1    Duralski, A.A.2    Rankin, S.E.3    Pinheiro, T.J.T.4    Watts, A.5
  • 23
    • 33845553163 scopus 로고
    • Spin dynamics in the carbon-13 nuclear magnetic resonance spectrometric analysis of coal by cross polarization magic-angle spinning
    • Sullivan, M. J., and G. E. Maciel. 1982. Spin dynamics in the carbon-13 nuclear magnetic resonance spectrometric analysis of coal by cross polarization magic-angle spinning. Anal. Chem. 54:1615-1623.
    • (1982) Anal. Chem. , vol.54 , pp. 1615-1623
    • Sullivan, M.J.1    Maciel, G.E.2
  • 25
    • 0029332135 scopus 로고
    • Membrane protein structure: The contribution and potential of novel solid state NMR approaches
    • Watts, A., A. S. Ulrich, and D. A. Middleton. 1995. Membrane protein structure: the contribution and potential of novel solid state NMR approaches (review). Mol. Membrane Biol. 12:233-246.
    • (1995) Mol. Membrane Biol. , vol.12 , pp. 233-246
    • Watts, A.1    Ulrich, A.S.2    Middleton, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.