메뉴 건너뛰기




Volumn 73, Issue 3, 1997, Pages 1579-1592

Effects of fluorine substitution on the structure and dynamics of complexes of dihydrofolate reductase (Escherichia coli)

Author keywords

[No Author keywords available]

Indexed keywords

6 FLUOROTRYPTOPHAN; DIHYDROFOLATE REDUCTASE; TRYPTOPHAN;

EID: 0030744035     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78190-6     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 0029198395 scopus 로고
    • Eukaryotic dihydrofolate reductase
    • Blakley, R. L. 1995. Eukaryotic dihydrofolate reductase. Adv. Enzymol. 70:23-102.
    • (1995) Adv. Enzymol. , vol.70 , pp. 23-102
    • Blakley, R.L.1
  • 2
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate
    • Bolin, J. T., D. J. Filman, D. A. Matthews, R. C. Hamlin, and J. Kraut. 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257:13650-13662.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 4
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff, C., and J. Kraut. 1991. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry. 30:2227-2239.
    • (1991) Biochemistry. , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 5
    • 0025270551 scopus 로고
    • + ternary complex. Substrate binding and a model for the transition state
    • + ternary complex. Substrate binding and a model for the transition state. Biochemistry. 29:3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 7
    • 0008796956 scopus 로고
    • Molecular dynamics/free energy perturbation study on the relative affinities of the binding of reduced and oxidized NADP to dihydrofolate reductase
    • Cummins, P. L., K. Ramnarayan, U. C. Singh, and J. E. Gready. 1991. Molecular dynamics/free energy perturbation study on the relative affinities of the binding of reduced and oxidized NADP to dihydrofolate reductase. J. Am. Chem. Soc. 113:8247-8256.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8247-8256
    • Cummins, P.L.1    Ramnarayan, K.2    Singh, U.C.3    Gready, J.E.4
  • 9
    • 0029102089 scopus 로고
    • Dynamics of the dihydrofolate reductase-folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features
    • Epstein, D. M., S. J. Benkovic, and P. E. Wright. 1995. Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. Biochemistry. 34:11037-11048.
    • (1995) Biochemistry , vol.34 , pp. 11037-11048
    • Epstein, D.M.1    Benkovic, S.J.2    Wright, P.E.3
  • 10
    • 0026326486 scopus 로고
    • Analysis of hydride transfer and cofactor fluorescence decay in mutants of dihydrofolate reductase: Possible evidence for participation of enzyme molecular motions in catalysis
    • Farnum, M. F., D. Magde, E. E. Howell, J. T. Hirai, M. S. Warren, J. K. Grimsley, and J. Kraut. 1991. Analysis of hydride transfer and cofactor fluorescence decay in mutants of dihydrofolate reductase: possible evidence for participation of enzyme molecular motions in catalysis. Biochemistry. 30:11567-11579.
    • (1991) Biochemistry , vol.30 , pp. 11567-11579
    • Farnum, M.F.1    Magde, D.2    Howell, E.E.3    Hirai, J.T.4    Warren, M.S.5    Grimsley, J.K.6    Kraut, J.7
  • 11
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C. A., K. A. Johnson, and S. J. Benkovic. 1987. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry. 26:4085-4094.
    • (1987) Biochemistry , vol.26 , pp. 4085-4094
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 12
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges
    • Gasteiger, J., and M. Marsili. 1980. Iterative partial equalization of orbital electronegativity - a rapid access to atomic charges. Tetrahedron. 36: 3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 13
    • 0020799931 scopus 로고
    • The calculation of molar volumes and the use of volume analysis in the investigation of structured media and of solid state organic reactivity
    • Gavezzotti, A. 1983. The calculation of molar volumes and the use of volume analysis in the investigation of structured media and of solid state organic reactivity. J. Am. Chem. Soc. 105:5220-5225.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5220-5225
    • Gavezzotti, A.1
  • 14
    • 0027998347 scopus 로고
    • Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function
    • Gekko, K., Y. Kunori, H. Takeuchi, S. Ichihara, and M. Kodama. 1994. Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function. J. Biochem. 116:34-41.
    • (1994) J. Biochem. , vol.116 , pp. 34-41
    • Gekko, K.1    Kunori, Y.2    Takeuchi, H.3    Ichihara, S.4    Kodama, M.5
  • 15
    • 0000648758 scopus 로고
    • Fluorine NMR of proteins
    • Gerig, J. T. 1994. Fluorine NMR of proteins. Prog. NMR Spectrosc. 26:293-370.
    • (1994) Prog. NMR Spectrosc. , vol.26 , pp. 293-370
    • Gerig, J.T.1
  • 16
    • 0026652129 scopus 로고
    • NMR detection of bound water molecules in the active site of L. casei dihydrofolate reductase in aqueous solution
    • Gerothanassis, I. P., B. Birdsall, C. J. Bauer, T. A. Frenkiel, and J. Feeney. 1992. NMR detection of bound water molecules in the active site of L. casei dihydrofolate reductase in aqueous solution. J. Mol. Biol. 226: 549-554.
    • (1992) J. Mol. Biol. , vol.226 , pp. 549-554
    • Gerothanassis, I.P.1    Birdsall, B.2    Bauer, C.J.3    Frenkiel, T.A.4    Feeney, J.5
  • 17
    • 84988074826 scopus 로고
    • Force field parameterization for the 4-fluorophenyl group
    • Gregory, D. H., and J. T. Gerig. 1989. Force field parameterization for the 4-fluorophenyl group. J. Comput. Chem. 10:711-717.
    • (1989) J. Comput. Chem. , vol.10 , pp. 711-717
    • Gregory, D.H.1    Gerig, J.T.2
  • 18
    • 0026172002 scopus 로고
    • Prediction of fluorine chemical shifts in proteins
    • Gregory, D. H., and J. T. Gerig. 1991. Prediction of fluorine chemical shifts in proteins. Biopolymers. 31:845-858.
    • (1991) Biopolymers. , vol.31 , pp. 845-858
    • Gregory, D.H.1    Gerig, J.T.2
  • 19
    • 0028175779 scopus 로고
    • 19F NMR spectroscopy of [6-F]tryptophan-labeled Escherichia coli dihydrofolate reductase: Equilibrium folding and ligand binding studies
    • 19F NMR spectroscopy of [6-F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies. Biochemistry. 33:5502-5509.
    • (1994) Biochemistry , vol.33 , pp. 5502-5509
    • Hoeltzli, S.D.1    Frieden, C.2
  • 20
    • 0020992720 scopus 로고
    • Applications of amino acid analogs for studying co- and posttranslational modifications of proteins
    • Hortin, G., and I. Boime. 1983. Applications of amino acid analogs for studying co-and posttranslational modifications of proteins. Methods Enzymol. 96:777-784.
    • (1983) Methods Enzymol. , vol.96 , pp. 777-784
    • Hortin, G.1    Boime, I.2
  • 21
    • 0022794053 scopus 로고
    • Structure and internal mobility of proteins: A molecular dynamics study of hen egg white lysozyme
    • Ichiye, T., B. D. Olafson, S. Swaminathan, and M. Karplus. 1986. Structure and internal mobility of proteins: a molecular dynamics study of hen egg white lysozyme. Biopolymers. 25:1909-1937.
    • (1986) Biopolymers. , vol.25 , pp. 1909-1937
    • Ichiye, T.1    Olafson, B.D.2    Swaminathan, S.3    Karplus, M.4
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. 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.1
  • 24
    • 0029867804 scopus 로고    scopus 로고
    • Solvent effects on the fluorine shielding of fluorobenzene
    • Lau, E. Y., and J. T. Gerig. 1996. Solvent effects on the fluorine shielding of fluorobenzene. J. Am. Chem. Soc. 118:1194-1200.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1194-1200
    • Lau, E.Y.1    Gerig, J.T.2
  • 25
    • 8644243613 scopus 로고
    • Partition coefficients and their uses
    • Leo, A., C. Hantsch, and D. Elkins. 1971. Partition coefficients and their uses. Chem. Rev. 71:525-616.
    • (1971) Chem. Rev. , vol.71 , pp. 525-616
    • Leo, A.1    Hantsch, C.2    Elkins, D.3
  • 26
    • 0026757079 scopus 로고
    • Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization
    • Li, L., C. J. Falzone, P. E. Wright, and S. J. Benkovic. 1992. Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization. Biochemistry. 31:7826-7833.
    • (1992) Biochemistry , vol.31 , pp. 7826-7833
    • Li, L.1    Falzone, C.J.2    Wright, P.E.3    Benkovic, S.J.4
  • 27
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 29
    • 0026532312 scopus 로고
    • A theoretical approach to drug design. 3. Relative thermodynamics of inhibitor binding by E. coli dihydrofolate reductase to ethyl derivatives of trimethoprim substituted at the 3′-position, 4′-position, and 5′-position
    • McDonald, J. J., and C. L. Brooks. 1992. A theoretical approach to drug design. 3. Relative thermodynamics of inhibitor binding by E. coli dihydrofolate reductase to ethyl derivatives of trimethoprim substituted at the 3′-position, 4′-position, and 5′-position. J. Am. Chem. Soc. 114: 2062-2072.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2062-2072
    • McDonald, J.J.1    Brooks, C.L.2
  • 30
    • 0028924642 scopus 로고
    • Contributions of tryptophan 24 and glutamate 30 to binding long-lived water molecules in the ternary complex of human dihydrofolate reductase with methotrexate and NADPH studied by site-directed mutagenesis and nuclear magnetic resonance spectroscopy
    • Meiering, E. M., H. Li, T. J. Delcamp, J. H. Freisheim, and G. Wagner. 1995. Contributions of tryptophan 24 and glutamate 30 to binding long-lived water molecules in the ternary complex of human dihydrofolate reductase with methotrexate and NADPH studied by site-directed mutagenesis and nuclear magnetic resonance spectroscopy. J. Mol. Biol. 247:309-325.
    • (1995) J. Mol. Biol. , vol.247 , pp. 309-325
    • Meiering, E.M.1    Li, H.2    Delcamp, T.J.3    Freisheim, J.H.4    Wagner, G.5
  • 31
    • 0028921374 scopus 로고
    • Detection of long-lived bound water molecules in complexes of human dihydrofolate reductase with methotrexate and NADPH
    • Meiering, E. M., and G. Wagner. 1995. Detection of long-lived bound water molecules in complexes of human dihydrofolate reductase with methotrexate and NADPH. J. Mol. Biol. 247:294-308.
    • (1995) J. Mol. Biol. , vol.247 , pp. 294-308
    • Meiering, E.M.1    Wagner, G.2
  • 32
    • 84986505827 scopus 로고
    • Validation of the general purpose QUANTA 3.2/CHARMm force field
    • Momany, F. A., and R. Rone. 1992. Validation of the general purpose QUANTA 3.2/CHARMm force field. J. Comput. Chem. 13:888-900.
    • (1992) J. Comput. Chem. , vol.13 , pp. 888-900
    • Momany, F.A.1    Rone, R.2
  • 33
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, G. J., S. J. Anthony-Cahill, M. C. Griffiths, and P. G. Shultz. 1989. A general method for site-specific incorporation of unnatural amino acids into proteins. Science. 244:182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, G.J.1    Anthony-Cahill, S.J.2    Griffiths, M.C.3    Shultz, P.G.4
  • 34
    • 84977307362 scopus 로고
    • A revision of van der Waals atomic radii for molecular crystals: N, O, F, Se, Br, and I bonded to carbon
    • Nyberg, S. C., and C. H. Faerman. 1985. A revision of van der Waals atomic radii for molecular crystals: N, O, F, Se, Br, and I bonded to carbon. Acta Crystaltogr. B41:264-278.
    • (1985) Acta Crystaltogr. B , vol.41 , pp. 264-278
    • Nyberg, S.C.1    Faerman, C.H.2
  • 35
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner, C., A. D'Arcy, and F. K. Winkler. 1988. Crystal structure of human dihydrofolate reductase complexed with folate. Eur. J. Biochem. 174:377-384.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 377-384
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3
  • 36
    • 0029939820 scopus 로고    scopus 로고
    • Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function
    • Ohmae, E., K. Iriyama, S. Ichihara, and K. Gekko. 1996. Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. 119:703-710.
    • (1996) J. Biochem. , vol.119 , pp. 703-710
    • Ohmae, E.1    Iriyama, K.2    Ichihara, S.3    Gekko, K.4
  • 37
    • 2442460927 scopus 로고
    • Molecular dynamics analysis of NMR relaxation in a zinc-finger peptide
    • Palmer, A. G., and D. A. Case. 1992. Molecular dynamics analysis of NMR relaxation in a zinc-finger peptide. J. Am. Chem. Soc. 114: 9059-9067.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9059-9067
    • Palmer, A.G.1    Case, D.A.2
  • 38
    • 0001465616 scopus 로고
    • Chemical shifts in proteins: A shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein using a multipole shielding polarizability-local reaction field-molecular dynamics approach
    • Pearson, J. G., E. Oldfield, F. S. Lee, and A. Warshel. 1993. Chemical shifts in proteins: a shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein using a multipole shielding polarizability-local reaction field-molecular dynamics approach. J. Am. Chem. Soc. 115:6851-6862.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6851-6862
    • Pearson, J.G.1    Oldfield, E.2    Lee, F.S.3    Warshel, A.4
  • 39
    • 0023665334 scopus 로고
    • Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase
    • Penner, M. H., and C. Frieden. 1987. Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase. J. Biol. Chem. 262: 15908-15914.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15908-15914
    • Penner, M.H.1    Frieden, C.2
  • 40
    • 0021191208 scopus 로고
    • Fluctuations in protein structure from X-ray diffraction
    • Petsko, G. A., and D. Ringe. 1984. Fluctuations in protein structure from X-ray diffraction. Annu. Rev. Biophys. Bioeng. 13:331-371.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 331-371
    • Petsko, G.A.1    Ringe, D.2
  • 41
    • 0029562951 scopus 로고
    • 1 in solution: Correlation with NMR and X-ray data and insights into biological function
    • 1 in solution: correlation with NMR and X-ray data and insights into biological function. J. Mol. Biol. 254:771-792.
    • (1995) J. Mol. Biol. , vol.254 , pp. 771-792
    • Philippopoulos, M.1    Lim, C.2
  • 43
    • 0028985318 scopus 로고
    • Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: Mechanistic implications
    • Reyes, V. M., M. R. Sawaya, K. A. Brown, and I. Kraut. 1995. Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications. Biochemistry. 34:2710-2723.
    • (1995) Biochemistry , vol.34 , pp. 2710-2723
    • Reyes, V.M.1    Sawaya, M.R.2    Brown, K.A.3    Kraut, I.4
  • 44
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23: 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 45
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M. R., and J. Kraut. 1997. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 36:586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 47
    • 0024026370 scopus 로고
    • Probing the salt bridge in the dihydrofolate reductase-methotrexate complex by using the coordinate-coupled free-energy perturbation method
    • Singh, U. C. 1988. Probing the salt bridge in the dihydrofolate reductase-methotrexate complex by using the coordinate-coupled free-energy perturbation method. Proc. Natl. Acad. Sci. USA. 85:4280-4282.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4280-4282
    • Singh, U.C.1
  • 48
    • 0024239036 scopus 로고
    • A free energy perturbation study of the binding of methotrexate to mutants of dihydrofolate reductase
    • Singh, U. C., and S. J. Benkovic. 1988. A free energy perturbation study of the binding of methotrexate to mutants of dihydrofolate reductase. Proc. Natl. Acad. Sci. USA. 85:9519-9523.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9519-9523
    • Singh, U.C.1    Benkovic, S.J.2
  • 50
    • 0028986918 scopus 로고
    • Internal mobility of the basic pancreatic trypsin inhibitor in solution: A comparison of NMR spin relaxation measurements and molecular dynamics simulations
    • Smith, P. E., R. C. van Schaik, T. Szyperski, K. Wuthrich, and van W. R. Gunsteren. 1995. Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations. J. Mol. Biol. 246:356-365.
    • (1995) J. Mol. Biol. , vol.246 , pp. 356-365
    • Smith, P.E.1    Van Schaik, R.C.2    Szyperski, T.3    Wuthrich, K.4    Van Gunsteren, W.R.5
  • 51
    • 0040092474 scopus 로고
    • The dipole moment of the methyl and ethyl halides
    • Smyth, C. P., and K. B. McAlpine. 1934. The dipole moment of the methyl and ethyl halides. J. Chem. Phys. 2:499-502.
    • (1934) J. Chem. Phys. , vol.2 , pp. 499-502
    • Smyth, C.P.1    McAlpine, K.B.2
  • 52
    • 0343761107 scopus 로고
    • Observations concerning the treatment of long-range interactions in molecular dynamics simulations
    • Tasaki, K., S. McDonald, and J. W. Brady. 1993. Observations concerning the treatment of long-range interactions in molecular dynamics simulations. J. Comput. Chem. 15:667-683.
    • (1993) J. Comput. Chem. , vol.15 , pp. 667-683
    • Tasaki, K.1    McDonald, S.2    Brady, J.W.3
  • 53
    • 22944467757 scopus 로고
    • Computer experiments on classical fluids. I
    • Verlet, L. 1967. Computer experiments on classical fluids. I. Phys. Rev. 159:98-113.
    • (1967) Phys. Rev. , vol.159 , pp. 98-113
    • Verlet, L.1
  • 54
    • 0031557394 scopus 로고    scopus 로고
    • Domain motions in dihydrofolate reductase: A molecular dynamics study
    • Verma, C. S., L. S. D. Caves, R. E. Hubbard, and G. C. K. Roberts. 1997. Domain motions in dihydrofolate reductase: a molecular dynamics study. J. Mol. Biol. 266:776-796.
    • (1997) J. Mol. Biol. , vol.266 , pp. 776-796
    • Verma, C.S.1    Caves, L.S.D.2    Hubbard, R.E.3    Roberts, G.C.K.4
  • 56
    • 0342455819 scopus 로고
    • Semisynthetic analogues of cytochrome c: Modifications to fragment (66-104)
    • R. E. Offord and C. Di Bello, editors. Academic, New York
    • Wallace, C. J. A. 1978. Semisynthetic analogues of cytochrome c: modifications to fragment (66-104). In Semisynthetic Peptides and Proteins. R. E. Offord and C. Di Bello, editors. Academic, New York. 101-114.
    • (1978) Semisynthetic Peptides and Proteins , pp. 101-114
    • Wallace, C.J.A.1
  • 57
    • 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
  • 58
    • 0029031765 scopus 로고
    • 15N-NMR relaxation analysis and molecular dynamics simulation: Examination of dynamics model
    • 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamics model. Biochemistry. 34: 6587-6601.
    • (1995) Biochemistry , vol.34 , pp. 6587-6601
    • Yamasaki, K.1    Saito, M.2    Oobatake, M.3    Kanaya, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.