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Volumn 141, Issue 2, 1999, Pages 301-311

Theoretical Analysis of the Inter-Ligand Overhauser Effect: A New Approach for Mapping Structural Relationships of Macromolecular Ligands

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; LIGAND;

EID: 0033257882     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1999.1897     Document Type: Article
Times cited : (44)

References (33)
  • 1
    • 0002832937 scopus 로고
    • Relaxation matrix analysis of the transferred nuclear Overhauser effect for finite exchange rates
    • R. E. London, M. E. Perlman, and D. G. Davis, Relaxation matrix analysis of the transferred nuclear Overhauser effect for finite exchange rates, J. Magn. Reson. 97, 79-98 (1992).
    • (1992) J. Magn. Reson. , vol.97 , pp. 79-98
    • London, R.E.1    Perlman, M.E.2    Davis, D.G.3
  • 2
    • 0032830041 scopus 로고    scopus 로고
    • The inter-ligand Overhauser effect: A powerful new NMR approach for mapping structural relationships of macromolecular ligands
    • D. Li, E. DeRose, and R. E. London, The inter-ligand Overhauser effect: A powerful new NMR approach for mapping structural relationships of macromolecular ligands, J. Biomol. NMR 15, 71-76 (1999).
    • (1999) J. Biomol. NMR , vol.15 , pp. 71-76
    • Li, D.1    DeRose, E.2    London, R.E.3
  • 3
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional N.M.R. spectroscopy
    • S. Macura and R. R. Ernst, Elucidation of cross relaxation in liquids by two-dimensional N.M.R. spectroscopy, Mol. Phys. 41, 95-117 (1980).
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 4
    • 0345763776 scopus 로고
    • Transient Fluorine-Proton Overhauser Effects in 4-(Trifluoromethyl)benzenesulfonyl-a-chymotrypsin
    • J. T. Gerig, Transient Fluorine-Proton Overhauser Effects in (4-(Trifluoromethyl)benzenesulfonyl-a-chymotrypsin, J. Am. Chem. Soc. 102, 7308-7312 (1980).
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7308-7312
    • Gerig, J.T.1
  • 5
    • 0001053688 scopus 로고
    • A theoretical study of the distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra
    • J. W. Keepers and T. L. James, A theoretical study of the distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra, J. Magn. Reson. 57, 404-426 (1984).
    • (1984) J. Magn. Reson. , vol.57 , pp. 404-426
    • Keepers, J.W.1    James, T.L.2
  • 6
    • 44949290542 scopus 로고
    • Calculation of the nulcear Overhauser effect and the determination of proton-proton distances in the presence of internal motions
    • T. M. G. Koning, R. Boelens, and R. Kaptein, Calculation of the nulcear Overhauser effect and the determination of proton-proton distances in the presence of internal motions, J. Magn. Reson. 90, 11-123 (1990).
    • (1990) J. Magn. Reson. , vol.90 , pp. 11-123
    • Koning, T.M.G.1    Boelens, R.2    Kaptein, R.3
  • 7
    • 0343972744 scopus 로고
    • General features of proton longitudinal relaxation in proteins in solution
    • Ishima, S. Shibata, and K. Akasaka, General features of proton longitudinal relaxation in proteins in solution, J. Magn. Reson. 91, 455-465 (1991).
    • (1991) J. Magn. Reson. , vol.91 , pp. 455-465
    • Ishima1    Shibata, S.2    Akasaka, K.3
  • 9
    • 0003518480 scopus 로고
    • Wiley, New York
    • I. H. Segel, "Enzyme Kinetics," pp. 506-523, Wiley, New York (1975).
    • (1975) Enzyme Kinetics , pp. 506-523
    • Segel, I.H.1
  • 10
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • J. Jeener, B. H. Meier, P. Bachmann, and R. R. Ernst, Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553 (1979).
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 11
    • 0020447132 scopus 로고
    • A. M. Gronenborn and G. M. Clore, Biochemistry 21, 4040 (1982); M. E. Davis, J. D. Madura, J. Sines, B. A. Luty, S. A. Allison, and J. A. McCammon, Diffusion-controlled enzymatic reactions, Methods Enzymol. 202, 473-497 (1991).
    • (1982) Biochemistry , vol.21 , pp. 4040
    • Gronenborn, A.M.1    Clore, G.M.2
  • 13
    • 0029919171 scopus 로고    scopus 로고
    • Phosphorus-31 nuclear magnetic resonance studies on coenzyme binding and specificity in glyceraldehyde-3-phosphate dehydrogenase
    • J. Eyschen, B. Vitoux, S. Rahuel-Clermont, M. Marraud, G. Branlant, and M. T. Cung, Phosphorus-31 nuclear magnetic resonance studies on coenzyme binding and specificity in glyceraldehyde-3-phosphate dehydrogenase, Biochemistry 35, 6064-6072 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6064-6072
    • Eyschen, J.1    Vitoux, B.2    Rahuel-Clermont, S.3    Marraud, M.4    Branlant, G.5    Cung, M.T.6
  • 15
    • 0002860359 scopus 로고
    • The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins
    • J. P. Albrand, B. Birdsall, J. Feeney, G. C. K. Roberts, and A. S. V. Burgen, The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins, Int. J. Biolog. Macromol. 1, 37-41 (1979).
    • (1979) Int. J. Biolog. Macromol. , vol.1 , pp. 37-41
    • Albrand, J.P.1    Birdsall, B.2    Feeney, J.3    Roberts, G.C.K.4    Burgen, A.S.V.5
  • 16
    • 0028728698 scopus 로고
    • Recent developments in transferred NOE methods
    • F. Ni, Recent developments in transferred NOE methods, Prog. NMR Spectrosc. 26, 517-606 (1994).
    • (1994) Prog. NMR Spectrosc. , vol.26 , pp. 517-606
    • Ni, F.1
  • 17
    • 0025338456 scopus 로고
    • Determination of ligand conformation in macromolecular complexes using the transferred nuclear Overhauser effect
    • A. M. Gronenborn and G. M. Clore, Determination of ligand conformation in macromolecular complexes using the transferred nuclear Overhauser effect, Biochem. Pharmacol. 40, 115-119 (1990).
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 115-119
    • Gronenborn, A.M.1    Clore, G.M.2
  • 18
    • 0029377157 scopus 로고
    • Complete relaxation and conformational exchnage matrix (CORCEMA) analysis of NOESY spectra of interacting systems-2-Dimensional transferred NOESY
    • H. N. B. Moseley, E. V. Curto, and N. R. Krishna, Complete relaxation and conformational exchnage matrix (CORCEMA) analysis of NOESY spectra of interacting systems-2-Dimensional transferred NOESY, J. Magn. Reson. B 108, 243-261 (1995).
    • (1995) J. Magn. Reson. B , vol.108 , pp. 243-261
    • Moseley, H.N.B.1    Curto, E.V.2    Krishna, N.R.3
  • 19
    • 0000071182 scopus 로고
    • Theory and experimental results of transfer-NOE experiments. 1. The influence of the off rate versus cross-relaxation rates
    • G. M. Lippens, C. Cerf, and K. Hallenga, Theory and experimental results of transfer-NOE experiments. 1. The influence of the off rate versus cross-relaxation rates, J. Magn. Reson. 99, 268-281 (1992).
    • (1992) J. Magn. Reson. , vol.99 , pp. 268-281
    • Lippens, G.M.1    Cerf, C.2    Hallenga, K.3
  • 20
    • 0002624406 scopus 로고
    • Theory and experimental results of transfer NOE experiments. II. The influence of residual mobility and relaxation centers inside the protein on the size of transfer NOEs
    • N. R. Nirmala, G. M. Lippens, and K. Hallenga, Theory and experimental results of transfer NOE experiments. II. The influence of residual mobility and relaxation centers inside the protein on the size of transfer NOEs, J. Magn. Reson. 100, 25-42 (1992).
    • (1992) J. Magn. Reson. , vol.100 , pp. 25-42
    • Nirmala, N.R.1    Lippens, G.M.2    Hallenga, K.3
  • 21
    • 0001780788 scopus 로고
    • Theoretical evaluation of the 2-dimensional transferred nuclear Overhauser effect
    • A. P. Campbell and B. D. Sykes, Theoretical evaluation of the 2-dimensional transferred nuclear Overhauser effect, J. Magn. Reson. 93, 77-92 (1991).
    • (1991) J. Magn. Reson. , vol.93 , pp. 77-92
    • Campbell, A.P.1    Sykes, B.D.2
  • 22
    • 0030917461 scopus 로고    scopus 로고
    • Screening mixtures for biological activity by NMR
    • B. Meyer, T. Weimar, and T. Peters, Screening mixtures for biological activity by NMR, Eur. J. Biochem. 246, 705-709 (1997).
    • (1997) Eur. J. Biochem. , vol.246 , pp. 705-709
    • Meyer, B.1    Weimar, T.2    Peters, T.3
  • 23
    • 0031576702 scopus 로고    scopus 로고
    • One-dimensional relaxation- and diffusion-edited NMR methods for screening compounds that bind to macromolecules
    • P. J. Hajduk, E. T. Olejniczak, and S. W. Fesik, One-dimensional relaxation- and diffusion-edited NMR methods for screening compounds that bind to macromolecules, J. Am. Chem. Soc. 119, 12,257-12,261 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12257-12261
    • Hajduk, P.J.1    Olejniczak, E.T.2    Fesik, S.W.3
  • 24
    • 0032456255 scopus 로고    scopus 로고
    • Simulations of transferred NOE in a ternary peptide-receptor-lipid complex
    • J. Czaplicki and A. Milon, Simulations of transferred NOE in a ternary peptide-receptor-lipid complex, J. Chim. Phys. 95, 196-207 (1998).
    • (1998) J. Chim. Phys. , vol.95 , pp. 196-207
    • Czaplicki, J.1    Milon, A.2
  • 25
    • 0023578842 scopus 로고
    • A transfer nuclear Overhauser effect study of coenzyme binding to distinct sites in binary and ternary complexes in glutamate dehydrogenase
    • A. Banerjee, H. R. Levy, G. C. Levy, C. LiMuti, B. M. Goldstein, and J. E. Bell, A transfer nuclear Overhauser effect study of coenzyme binding to distinct sites in binary and ternary complexes in glutamate dehydrogenase, Biochemistry 26, 8443-8450 (1987).
    • (1987) Biochemistry , vol.26 , pp. 8443-8450
    • Banerjee, A.1    Levy, H.R.2    Levy, G.C.3    LiMuti, C.4    Goldstein, B.M.5    Bell, J.E.6
  • 26
    • 0032209293 scopus 로고    scopus 로고
    • Protein mediated magnetic coupling between lactate and water protons
    • S. D. Swanson, Protein mediated magnetic coupling between lactate and water protons, J. Magn. Reson. 135, 248-255 (1998).
    • (1998) J. Magn. Reson. , vol.135 , pp. 248-255
    • Swanson, S.D.1
  • 27
    • 77956904836 scopus 로고    scopus 로고
    • Glutamate dehydrogenases
    • P. D. Boyer, Ed., Academic Press, New York
    • E. L. Smith, B. M. Austen, K. M. Blumenthal, and J. F. Nyc, Glutamate dehydrogenases, In "The Enzymes" (P. D. Boyer, Ed.), Vol. 11, pp. 293-367, Academic Press, New York.
    • The Enzymes , vol.11 , pp. 293-367
    • Smith, E.L.1    Austen, B.M.2    Blumenthal, K.M.3    Nyc, J.F.4
  • 28
    • 0033565447 scopus 로고    scopus 로고
    • The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery
    • P. E. Peterson and T. J. Smith, The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery, Structure 7, 769-782 (1999).
    • (1999) Structure , vol.7 , pp. 769-782
    • Peterson, P.E.1    Smith, T.J.2
  • 29
    • 0001308804 scopus 로고
    • Complete elimination of spin diffusion from selected resonances in two-dimensional cross-relaxation spectra of macromolecules by a novel pulse sequence
    • J. Fejzo, W. M. Westler, J. L. Markley, and S. Macura, Complete elimination of spin diffusion from selected resonances in two-dimensional cross-relaxation spectra of macromolecules by a novel pulse sequence, J. Am. Chem. Soc. 114, 1523-1524 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 1523-1524
    • Fejzo, J.1    Westler, W.M.2    Markley, J.L.3    Macura, S.4
  • 31
    • 0029048988 scopus 로고
    • Kinetic, binding, and NMR studies of perdeuterated yeast phosphoglycerate kinase and its interactions with substrates
    • C. G. Shibata, J. D. Gregory, B. S. Gerhardt, and E. H. Serpersu. Kinetic, binding, and NMR studies of perdeuterated yeast phosphoglycerate kinase and its interactions with substrates, Arch. Biochem. Biophys. 319, 204-210 (1995).
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 204-210
    • Shibata, C.G.1    Gregory, J.D.2    Gerhardt, B.S.3    Serpersu, E.H.4
  • 32
    • 0028343420 scopus 로고
    • Studies of inhibitor binding to Escherichia coli purine nucleoside phosphorylase using the transferred nuclear Overhauser effect and rotating-frame nuclear Overhauser enhancement
    • M. E. Perlman, D. G. Davis, G. W. Koszalka, J. V. Tuttle, and R. E. London, Studies of inhibitor binding to Escherichia coli purine nucleoside phosphorylase using the transferred nuclear Overhauser effect and rotating-frame nuclear Overhauser enhancement, Biochemistry 33, 7547-7559 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7547-7559
    • Perlman, M.E.1    Davis, D.G.2    Koszalka, G.W.3    Tuttle, J.V.4    London, R.E.5
  • 33
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high affinity ligands for proteins: SAR by NMR
    • S. B. Shuker, P. J. Hajduk, R. P. Meadows, and S. W. Fesik, Discovering high affinity ligands for proteins: SAR by NMR, Science 274, 1531-1534 (1996).
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4


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