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Volumn 239, Issue 3, 1996, Pages 710-719

Conformational analysis of blood group A trisaccharide in solution and in the binding site of Dolichos biflorus lectin using transient and transferred nuclear Overhauser enhancement (NOE) and rotating-frame NOE experiments

Author keywords

Blood group A trisaccharide; Dolichos biflorus lectin; Molecular modeling; Protein carbohydrate interaction; Transferred nuclear Overhauser enhancement

Indexed keywords

BLOOD GROUP ANTIGEN; TRISACCHARIDE;

EID: 0029948364     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0710u.x     Document Type: Article
Times cited : (35)

References (57)
  • 1
    • 0000526534 scopus 로고
    • A molecular mechanics force field (MM3) for alcohols and ethers
    • Allinger, N. L., Rahman, M. & Lii, J.-H. (1990) A molecular mechanics force field (MM3) for alcohols and ethers, J. Am. Chem. Soe. 112, 8293-8307.
    • (1990) J. Am. Chem. Soe. , vol.112 , pp. 8293-8307
    • Allinger, N.L.1    Rahman, M.2    Lii, J.-H.3
  • 2
    • 0024821263 scopus 로고
    • Molecular mechanics. The MM3 force field for hydrocarbons. 1
    • Allinger, N. L., Yuh, Y.-H. & Lii, J.-H. (1989) Molecular mechanics. The MM3 force field for hydrocarbons. 1, J. Am. Chem. Soc. 111, 8551-8566.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8551-8566
    • Allinger, N.L.1    Yuh, Y.-H.2    Lii, J.-H.3
  • 3
    • 0029243119 scopus 로고
    • Identification of protein-mediated indirect NOE effects in a disaccharide-Fab′ complex by transferred ROESY
    • Arepalli, S. R., Glaudemans, C. P. J., Daves, G. D., Kovac, P. & Bax, A. (1995) Identification of protein-mediated indirect NOE effects in a disaccharide-Fab′ complex by transferred ROESY. J. Magn. Reson. B106, 195-198.
    • (1995) J. Magn. Reson. , vol.B106 , pp. 195-198
    • Arepalli, S.R.1    Glaudemans, C.P.J.2    Daves, G.D.3    Kovac, P.4    Bax, A.5
  • 4
    • 5144233105 scopus 로고
    • MLEV-17-Base two-dimensional homonuclear magneti/ation transfer spectroscopy
    • Bax, A. & Davies, D. G. (1985) MLEV-17-Base two-dimensional homonuclear magneti/ation transfer spectroscopy, J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davies, D.G.2
  • 5
    • 45449124114 scopus 로고
    • Correction of cross-peak intensities in 2D spin-locked NOE spectroscopy for offset and Hartmann-Hahn effects
    • Bax, A. (1988) Correction of cross-peak intensities in 2D spin-locked NOE spectroscopy for offset and Hartmann-Hahn effects, J. Magn. Reson. 77, 134-147.
    • (1988) J. Magn. Reson. , vol.77 , pp. 134-147
    • Bax, A.1
  • 6
    • 0026787507 scopus 로고
    • Conformation of β-melhylmelihiose hound to the ricin B-chain as determined from transferred nuclear Overhauser effects
    • Bevilacqua, V. L., Kim, Y. & Prestegard, J. H. (1992) Conformation of β-melhylmelihiose hound to the ricin B-chain as determined from transferred nuclear Overhauser effects. Biochemistry 31, 9339-9349.
    • (1992) Biochemistry , vol.31 , pp. 9339-9349
    • Bevilacqua, V.L.1    Kim, Y.2    Prestegard, J.H.3
  • 7
    • 0025316943 scopus 로고
    • Conformation of methyl β-lactoside bound to the ricin B-chain: Interpretation of transferred nuclear Overhauser effects facilitated by spin simulation and selective deuteration
    • Bevilacqua, V. L., Thomson, D. S. & Prestegard, J. U. (1990) Conformation of methyl β-lactoside bound to the ricin B-chain: interpretation of transferred nuclear Overhauser effects facilitated by spin simulation and selective deuteration, Biochemistry 29, 5529-5537.
    • (1990) Biochemistry , vol.29 , pp. 5529-5537
    • Bevilacqua, V.L.1    Thomson, D.S.2    Prestegard, J.U.3
  • 8
    • 0026500777 scopus 로고
    • X-ray structure of a biantennary octasaccharide-lectin complex at 2.3 angstroms resolution
    • Bourne, Y., Rougé, P. & Cambillau, C. (1992) X-ray structure of a biantennary octasaccharide-lectin complex at 2.3 angstroms resolution, J. Biol Chem. 267, 197-203.
    • (1992) J. Biol Chem. , vol.267 , pp. 197-203
    • Bourne, Y.1    Rougé, P.2    Cambillau, C.3
  • 9
    • 0028773158 scopus 로고
    • Structure of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: Role of the fucose moiety
    • Bourne, Y., Mazurier, J., Legrand, D., Rougé, P., Montreuil, J., Spik, G. & Cambillau, C. (1995) Structure of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety, Structure 2, 209-219.
    • (1995) Structure , vol.2 , pp. 209-219
    • Bourne, Y.1    Mazurier, J.2    Legrand, D.3    Rougé, P.4    Montreuil, J.5    Spik, G.6    Cambillau, C.7
  • 10
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Applications to proton correlation spectroscopy
    • Braunschwciler, L. & Ernsl, R. R. (1983) Coherence transfer by isotropic mixing: applications to proton correlation spectroscopy, J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschwciler, L.1    Ernsl, R.R.2
  • 11
    • 0028300617 scopus 로고
    • Solution structure of a trisaccharide-antibody complex: Comparison of NMR measurements with a crystal structure
    • Bundle, O. R., Baumann, H., Brisson, J. R., Gagné, S. M., Zdanov, A. & Cygler, M. (1994) Solution structure of a trisaccharide-antibody complex: comparison of NMR measurements with a crystal structure, Biochemistry 33, 5183-5192.
    • (1994) Biochemistry , vol.33 , pp. 5183-5192
    • Bundle, O.R.1    Baumann, H.2    Brisson, J.R.3    Gagné, S.M.4    Zdanov, A.5    Cygler, M.6
  • 12
    • 0000297709 scopus 로고
    • Conformational energy calculations and proton nuclear Overhauser enhancements reveal a unique conformation for blood group A oligosaccharides
    • Bush, A. C., Yan, Z.-Y. & Rao, N. B. N. (1986) Conformational energy calculations and proton nuclear Overhauser enhancements reveal a unique conformation for blood group A oligosaccharides, J. Am. Chem. Soc. 108, 6168-6173.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6168-6173
    • Bush, A.C.1    Yan, Z.-Y.2    Rao, N.B.N.3
  • 15
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore, G. M. & Gronenborn, A. M. (1982) Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins, J. Magn. Res. 48, 402-417.
    • (1982) J. Magn. Res. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 16
    • 0001342923 scopus 로고
    • Theory of the time dependent transferred nuclear Overhauser effect: Applications to structural analysis of ligand-protein complexes in solution
    • Clore, G. M. & Gronenborn, A. M. (1983) Theory of the time dependent transferred nuclear Overhauser effect: applications to structural analysis of ligand-protein complexes in solution. J. Magn. Res. 53, 423-442.
    • (1983) J. Magn. Res. , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.M.2
  • 18
    • 0023661070 scopus 로고
    • Virtual and solution conformations of oligosaccharides
    • Cuming, D. A. & Carver, J. P. (1987) Virtual and solution conformations of oligosaccharides. Biochemistry 26, 6664-6676.
    • (1987) Biochemistry , vol.26 , pp. 6664-6676
    • Cuming, D.A.1    Carver, J.P.2
  • 19
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectros-copy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectros-copy, J. Am. Chem. Soc. 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davies, D.G.1    Bax, A.2
  • 20
    • 0027196879 scopus 로고
    • The 2.0 Å structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human hlood group determinant
    • Delbaere, L. T. J., Vandonselaar, M., Prasad, L., Quail, J. W., Wilson, K. S. & Dauter, Z. (1993) The 2.0 Å structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human hlood group determinant, J. Mol. Biol. 230, 950-966.
    • (1993) J. Mol. Biol. , vol.230 , pp. 950-966
    • Delbaere, L.T.J.1    Vandonselaar, M.2    Prasad, L.3    Quail, J.W.4    Wilson, K.S.5    Dauter, Z.6
  • 21
    • 0026752484 scopus 로고
    • Conformational analysis of the anomeric forms of kojibiose, nigerose, and maltose using MM3
    • Dowd, M. K., Zeng, J., French, A. D. & Reilly, P. J. (1992) Conformational analysis of the anomeric forms of kojibiose, nigerose, and maltose using MM3, Carbohydr. Res. 230, 223-244.
    • (1992) Carbohydr. Res. , vol.230 , pp. 223-244
    • Dowd, M.K.1    Zeng, J.2    French, A.D.3    Reilly, P.J.4
  • 22
    • 0014952515 scopus 로고
    • Purification and caracterization of a lectin (plant hemagglutinin) with hlood group A specificity from Dolichos biflorus
    • Etzler, M. E. & Kabat, E. A. (1970) Purification and caracterization of a lectin (plant hemagglutinin) with hlood group A specificity from Dolichos biflorus, Biochemistry 9, 869-877.
    • (1970) Biochemistry , vol.9 , pp. 869-877
    • Etzler, M.E.1    Kabat, E.A.2
  • 23
    • 0025668523 scopus 로고
    • Significant conformational changes in an antigenic carbohydrate epitope upon binding to monoclonal antibody
    • Glaudemans, C. P. J., Lerner, L., Daves, G. D., Kovac, P., Venable, R. & Bax, A. (1990) Significant conformational changes in an antigenic carbohydrate epitope upon binding to monoclonal antibody, Biochemistry 29, 10 906-10 911.
    • (1990) Biochemistry , vol.29 , pp. 10906-10911
    • Glaudemans, C.P.J.1    Lerner, L.2    Daves, G.D.3    Kovac, P.4    Venable, R.5    Bax, A.6
  • 24
    • 0026341012 scopus 로고
    • Molecular modeling of protein/carbohydrate interactions. Docking of monosaccharides in the binding site of concanavalin A
    • Imberty, A., Hardman, K. D., Carver, J. P. & Pèrez, S. (1991) Molecular modeling of protein/carbohydrate interactions. Docking of monosaccharides in the binding site of concanavalin A, Glycobiology 1, 631-642.
    • (1991) Glycobiology , vol.1 , pp. 631-642
    • Imberty, A.1    Hardman, K.D.2    Carver, J.P.3    Pèrez, S.4
  • 26
    • 0027985523 scopus 로고
    • Molecular modelling of the Dolichos hiflorus seed lectin and its specific interactions with carbohydrates: α-D-N-acetyl-galactosamine, Forssman disaccharide and blood group A trisaccharide
    • Imberty, A., Casset, F., Gegg, C. V., Etzler, M. E. & Pérez, S. (1994) Molecular modelling of the Dolichos hiflorus seed lectin and its specific interactions with carbohydrates: α-D-N-acetyl-galactosamine, Forssman disaccharide and blood group A trisaccharide, Glycoconj. J. 11, 400-413.
    • (1994) Glycoconj. J. , vol.11 , pp. 400-413
    • Imberty, A.1    Casset, F.2    Gegg, C.V.3    Etzler, M.E.4    Pérez, S.5
  • 27
    • 0029014988 scopus 로고
    • Computer simulation of histo-blood group oligosaccharides: Energy maps of all constituting disaccharides and potential energy surfaces of 14 ABH and Lewis carbohydrate antigens
    • Imberty, A., Mikros, E., Koca, J., Mollicone, R., Oriol, R. & Pérez, S. (1995) Computer simulation of histo-blood group oligosaccharides: energy maps of all constituting disaccharides and potential energy surfaces of 14 ABH and Lewis carbohydrate antigens, Glycoconj. J. 12, 331-349.
    • (1995) Glycoconj. J. , vol.12 , pp. 331-349
    • Imberty, A.1    Mikros, E.2    Koca, J.3    Mollicone, R.4    Oriol, R.5    Pérez, S.6
  • 28
    • 0039719399 scopus 로고
    • Abbreviations and symbols for the description of the conformation of polypeptide chain
    • IUPAC-IUB Commission on Biochemical Nomenclature (1971) Abbreviations and symbols for the description of the conformation of polypeptide chain, Arch. Biochem. Biophys. 145, 405-479.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 405-479
  • 30
    • 0002533005 scopus 로고
    • Computer program CICADA - Travelling along conformational potential energy hypersurface
    • Koca, J. (1994) Computer program CICADA - Travelling along conformational potential energy hypersurface. J. Mol. Struct. (Theochem) 308, 13-24.
    • (1994) J. Mol. Struct. (Theochem) , vol.308 , pp. 13-24
    • Koca, J.1
  • 31
    • 84986468699 scopus 로고
    • Conformational analysis and flexibility of carbohydrates using the CICADA approach with MM3
    • Koca, J., Pérez, S. & Imberty, A. (1995) Conformational analysis and flexibility of carbohydrates using the CICADA approach with MM3, J. Comp. Chem. 16, 296-310.
    • (1995) J. Comp. Chem. , vol.16 , pp. 296-310
    • Koca, J.1    Pérez, S.2    Imberty, A.3
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0000843125 scopus 로고
    • Zur Kenntnis der antifermenlativen lyrischen und agglutinierenden Wirkungen des Blutserums und der Lymphe
    • Landsteiner, K. (1900) Zur Kenntnis der antifermenlativen lyrischen und agglutinierenden Wirkungen des Blutserums und der Lymphe, Zentralbl. Bakteriol. 27, 357-362.
    • (1900) Zentralbl. Bakteriol. , vol.27 , pp. 357-362
    • Landsteiner, K.1
  • 34
    • 0001347671 scopus 로고
    • The conformations of oligosaccharides related to the ABH and Lewis human blood group determinants
    • Lemieux, R. U., Bock, K., Delbaere, L. T. J., Koto, S. & Rao, V. S. (1980) The conformations of oligosaccharides related to the ABH and Lewis human blood group determinants, Can. J. Chem. 58, 631-653.
    • (1980) Can. J. Chem. , vol.58 , pp. 631-653
    • Lemieux, R.U.1    Bock, K.2    Delbaere, L.T.J.3    Koto, S.4    Rao, V.S.5
  • 35
    • 0029339153 scopus 로고
    • Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis
    • Lommerse, J. P. M., Kroon-Batenburg, L. M. J., Kroon, J., Kamerling, J. & Vliegenthart, J. F. G. (1995) Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis, J. Biol. NMR 5, 79-94.
    • (1995) J. Biol. NMR , vol.5 , pp. 79-94
    • Lommerse, J.P.M.1    Kroon-Batenburg, L.M.J.2    Kroon, J.3    Kamerling, J.4    Vliegenthart, J.F.G.5
  • 36
    • 0028206798 scopus 로고
    • Thermodynamics of lectin-carbohydrate interactions. Titration microcalorimetry measurements of the binding of N-linked carbohydrates and ovalbumin to concanavalin
    • Mandal, D. K., Kishore, N. & Brewer, F. C. (1994) Thermodynamics of lectin-carbohydrate interactions. Titration microcalorimetry measurements of the binding of N-linked carbohydrates and ovalbumin to concanavalin, Biochemistry 33, 1149-1156.
    • (1994) Biochemistry , vol.33 , pp. 1149-1156
    • Mandal, D.K.1    Kishore, N.2    Brewer, F.C.3
  • 37
    • 0021114895 scopus 로고
    • Application of phase sensitive twodimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • Marion, D. & Wüthrich, K. (1983) Application of phase sensitive twodimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113, 967-974.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 38
    • 0000546538 scopus 로고
    • Complete relaxation matrix analysis of transferred nuclear Overhauser effects
    • Ni, F. (1992) Complete relaxation matrix analysis of transferred nuclear Overhauser effects, J. Magn. Reson. 96, 651-656.
    • (1992) J. Magn. Reson. , vol.96 , pp. 651-656
    • Ni, F.1
  • 39
    • 0028381004 scopus 로고
    • Accounting for ligand-protein interactions in the relaxation matrix analysis of transferred nuclear Overhauser effects
    • Ni, F. & Zhu, Y. (1994) Accounting for ligand-protein interactions in the relaxation matrix analysis of transferred nuclear Overhauser effects. J. Magn. Reson. B102, 180-184.
    • (1994) J. Magn. Reson. , vol.B102 , pp. 180-184
    • Ni, F.1    Zhu, Y.2
  • 40
    • 46149141123 scopus 로고
    • Accounting tor spin diffusion in the analysis of 2D NOE data
    • Olejniczak, E. T., Gampe, R. T. & Fezik, S. W. (1986) Accounting tor spin diffusion in the analysis of 2D NOE data, J. Magn. Reson. 67, 28-41.
    • (1986) J. Magn. Reson. , vol.67 , pp. 28-41
    • Olejniczak, E.T.1    Gampe, R.T.2    Fezik, S.W.3
  • 41
    • 0002350188 scopus 로고
    • (Cartron. J. P. & Rouger, P., eds) Plenum Press, New York
    • Oriol, R. (1995) Blood cell biochemistry (Cartron. J. P. & Rouger, P., eds) vol. 6, pp. 37-73, Plenum Press, New York.
    • (1995) Blood Cell Biochemistry , vol.6 , pp. 37-73
    • Oriol, R.1
  • 42
    • 0003014623 scopus 로고
    • Practical tools for molecular modeling of complex carbohydrates and their interactions with proteins
    • (Pullman, A., Jartsen, J. & Pullman, B., eds) Kluwer Academic Publishers, Dordrecht
    • Pérez, S., Meyer, C. & Imberty, A. (1995) Practical tools for molecular modeling of complex carbohydrates and their interactions with proteins, in Modelling of biomolecular structures and mechanisms (Pullman, A., Jartsen, J. & Pullman, B., eds) pp. 425-454. Kluwer Academic Publishers, Dordrecht.
    • (1995) Modelling of Biomolecular Structures and Mechanisms , pp. 425-454
    • Pérez, S.1    Meyer, C.2    Imberty, A.3
  • 44
    • 0016843221 scopus 로고
    • 1H nuclear magnetic resonance determination of the conformations of the polyene chain portions of 9-cis-and 13-cis-retinal in solution
    • 1H nuclear magnetic resonance determination of the conformations of the polyene chain portions of 9-cis-and 13-cis-retinal in solution, J. Am. Chem. Soc. 97, 1023-1027.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 1023-1027
    • Rowan III, R.1    Sykes, B.D.2
  • 46
    • 0027336415 scopus 로고
    • T1Q-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens
    • Scherf, T. & Anglister, J. A. (1993) T1Q-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens, Biophys. J. 64, 754-761.
    • (1993) Biophys. J. , vol.64 , pp. 754-761
    • Scherf, T.1    Anglister, J.A.2
  • 47
    • 0027538064 scopus 로고
    • Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin. and lentil (Lens culinaris) lectin
    • Schwarz, F. P., Puri, K. D., Bhat, R. G. & Surolia, A. (1993) Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin. and lentil (Lens culinaris) lectin, J. Biol. Chem. 268, 7668-7677.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7668-7677
    • Schwarz, F.P.1    Puri, K.D.2    Bhat, R.G.3    Surolia, A.4
  • 48
    • 0027534507 scopus 로고
    • Defining the precision with which a protein structure is determined by NMR. Application to motilin
    • Shriver, J. & Edmondson, S. (1993) Defining the precision with which a protein structure is determined by NMR. Application to motilin. Biochemistry 32, 1610-1617.
    • (1993) Biochemistry , vol.32 , pp. 1610-1617
    • Shriver, J.1    Edmondson, S.2
  • 49
    • 36749110658 scopus 로고
    • Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: The effect of fluctuating internuclear distances
    • Tropp, J. (1980) Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: The effect of fluctuating internuclear distances, J. Chem. Phys. 72, 6035-6043.
    • (1980) J. Chem. Phys. , vol.72 , pp. 6035-6043
    • Tropp, J.1
  • 50
    • 0024241438 scopus 로고
    • Regulation of expression of carbohydrate blood group antigens
    • Watkins, W. M., Greenwell, P., Yates, A. D. & Johnson, P. H. (1988) Regulation of expression of carbohydrate blood group antigens, Biochimie (Paris) 70, 1597-1611.
    • (1988) Biochimie (Paris) , vol.70 , pp. 1597-1611
    • Watkins, W.M.1    Greenwell, P.2    Yates, A.D.3    Johnson, P.H.4
  • 51
    • 0027631384 scopus 로고
    • Conformational analysis of α-D-Fuc-( 1→4)-β-D-GlcNAc-OMe. One-dimensional transient NOE experiments and Metropolis Monte Carlo simulations
    • Weimar, T., Meyer, B. & Peters, T. (1993) Conformational analysis of α-D-Fuc-( 1→4)-β-D-GlcNAc-OMe. One-dimensional transient NOE experiments and Metropolis Monte Carlo simulations. J. Biomol. NMR 3, 399-414.
    • (1993) J. Biomol. NMR , vol.3 , pp. 399-414
    • Weimar, T.1    Meyer, B.2    Peters, T.3
  • 52
    • 8944223060 scopus 로고    scopus 로고
    • Combined NMR, grid search/MM3 and Metropolis Monte Carlo/GEGOP studies of two L-fucose containing disaccharides: α-L-Fuc-(1,4)-β-D-GlcNAc-OMe and α-L-Fuc-(1,6)-β-D-GlcNAc-OMe
    • in the press
    • Weimar, T., Peters, T., Pérez, S. & Imberty, A. (1996) Combined NMR, grid search/MM3 and Metropolis Monte Carlo/GEGOP studies of two L-fucose containing disaccharides: α-L-Fuc-(1,4)-β-D-GlcNAc-OMe and α-L-Fuc-(1,6)-β-D-GlcNAc-OMe, J. Mol. Struct. (Theochem in the press.
    • (1996) J. Mol. Struct. Theochem
    • Weimar, T.1    Peters, T.2    Pérez, S.3    Imberty, A.4
  • 53
    • 9244239322 scopus 로고
    • The molecular conformation of cyclodi-β-alanyl
    • White, D. N. J. & Guy, M. H. P. (1975) The molecular conformation of cyclodi-β-alanyl, J. Chem. Soc. Perkin Trans. 2, 43-46.
    • (1975) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 43-46
    • White, D.N.J.1    Guy, M.H.P.2
  • 54
    • 36849135534 scopus 로고
    • Spin relaxation processes in a two-proton system undergoing anisotropic reorientation
    • Woessner, D. E. (1962) Spin relaxation processes in a two-proton system undergoing anisotropic reorientation, J. Chem. Phys. 36, 1-4.
    • (1962) J. Chem. Phys. , vol.36 , pp. 1-4
    • Woessner, D.E.1
  • 55
    • 36849125639 scopus 로고
    • Nuclear magnetic dipole-dipole relaxation in molecules with internal motion
    • Woessner, D. E. (1965) Nuclear magnetic dipole-dipole relaxation in molecules with internal motion, J. Chem. Phys. 42, 1855-1859.
    • (1965) J. Chem. Phys. , vol.42 , pp. 1855-1859
    • Woessner, D.E.1
  • 56
    • 0025319809 scopus 로고
    • Molecular dynamics simulations and the conformational mobility of blood group oligosaccharides
    • Yan, Z. Y. & Bush, A. C. (1990) Molecular dynamics simulations and the conformational mobility of blood group oligosaccharides, Biopolymers 29, 799-811.
    • (1990) Biopolymers , vol.29 , pp. 799-811
    • Yan, Z.Y.1    Bush, A.C.2
  • 57
    • 0023472240 scopus 로고
    • Influence of nonaqueous solvents on the conformation of blood group oligosaccharides
    • Yan, Z. Y., Rao, N. B. N. & Bush, A. C. (1992) Influence of nonaqueous solvents on the conformation of blood group oligosaccharides. J. Am. Chem. Soc. 109, 7663-7669.
    • (1992) J. Am. Chem. Soc. , vol.109 , pp. 7663-7669
    • Yan, Z.Y.1    Rao, N.B.N.2    Bush, A.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.