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Volumn 70, Issue 4, 1996, Pages 1603-1608

Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; SNAKE VENOM;

EID: 0029863182     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79759-X     Document Type: Article
Times cited : (46)

References (25)
  • 1
    • 0028878141 scopus 로고
    • Acetylcholinesterase: Diffusional encounter rate constant for dumbbell model of ligands
    • Antosiewicz, J., M. K. Gilson, I. H, Lee, and J. A. McCammon. 1995. Acetylcholinesterase: diffusional encounter rate constant for dumbbell model of ligands. Biophys. J. 68:62-68.
    • (1995) Biophys. J. , vol.68 , pp. 62-68
    • Antosiewicz, J.1    Gilson, M.K.2    Lee, I.H.3    McCammon, J.A.4
  • 2
    • 85005688711 scopus 로고
    • Acetylcholinesterase: Effects of ionic strength and dimerization on the rate constants
    • Antosiewicz. J., M. K. Gilson. and J. A. McCammon. 1994. Acetylcholinesterase: effects of ionic strength and dimerization on the rate constants, Isr. J. Chem. 34:151-158.
    • (1994) Isr. J. Chem. , vol.34 , pp. 151-158
    • Antosiewicz, J.1    Gilson, M.K.2    McCammon, J.A.3
  • 3
    • 0024241856 scopus 로고
    • An unusual electrooptical effect observed for DNA fragments and its apparent relation to a permanent electric moment associated with bent DNA
    • Antosiewicz, J., and D. Porschke. 1989a. An unusual electrooptical effect observed for DNA fragments and its apparent relation to a permanent electric moment associated with bent DNA. Biaphys. Chem. 33:19-30.
    • (1989) Biaphys. Chem. , vol.33 , pp. 19-30
    • Antosiewicz, J.1    Porschke, D.2
  • 4
    • 0024788820 scopus 로고
    • The nature of protein dipole moments: Experimental and calculated permanent dipole of a-chymotrypsin
    • Antosiewicz, J., and D. Porschke. 1989b. The nature of protein dipole moments: experimental and calculated permanent dipole of a-chymotrypsin. Biochemistry. 28:10072-10078.
    • (1989) Biochemistry , vol.28 , pp. 10072-10078
    • Antosiewicz, J.1    Porschke, D.2
  • 5
    • 0002630825 scopus 로고
    • Enzymatic destruction of acetylcholine
    • J. I. Hubbard, editor. Plenum, New York
    • Barnard, E. A. 1974. Enzymatic destruction of acetylcholine. In The Peripheral Nervous System J. I. Hubbard, editor. Plenum, New York. 201-224.
    • (1974) The Peripheral Nervous System , pp. 201-224
    • Barnard, E.A.1
  • 6
    • 0000463977 scopus 로고
    • Contribution a l'étude de l'effect kerr présenté par les solutions diluées de macromolécules rigides
    • Benoit, H. 1951. Contribution a l'étude de l'effect kerr présenté par les solutions diluées de macromolécules rigides. Ann. Phys. 6:561-609.
    • (1951) Ann. Phys. , vol.6 , pp. 561-609
    • Benoit, H.1
  • 8
    • 0020130381 scopus 로고
    • Electric properties and structure of DNA restriction fragments from measurements of the electric dichroism
    • Diekmann. S., W. Hillen, M Jung, R. D. Wells, and D. Porschke. 1982. Electric properties and structure of DNA restriction fragments from measurements of the electric dichroism. Biophys. Chem. 15:157-167.
    • (1982) Biophys. Chem. , vol.15 , pp. 157-167
    • Diekmann, S.1    Hillen, W.2    Jung, M.3    Wells, R.D.4    Porschke, D.5
  • 9
    • 0016180134 scopus 로고
    • Acetylcholinesterase
    • Dudai, Y., and I. Silman. 1974. Acetylcholinesterase. Methods Enzymol. 34:571-580.
    • (1974) Methods Enzymol. , vol.34 , pp. 571-580
    • Dudai, Y.1    Silman, I.2
  • 13
    • 0017089228 scopus 로고
    • Affinity chromatography of acetylcholinesterases: The importance of hydrophobic interactions
    • Massoulié, J., and S. Bon. 1976. Affinity chromatography of acetylcholinesterases: the importance of hydrophobic interactions. Eur. J. Biochem. 68:531-539.
    • (1976) Eur. J. Biochem. , vol.68 , pp. 531-539
    • Massoulié, J.1    Bon, S.2
  • 14
    • 0343387160 scopus 로고
    • Electric polarizability of polar ions
    • Mysels, K. J. 1953. Electric polarizability of polar ions. J. Chem. Phys. 21:201-205.
    • (1953) J. Chem. Phys. , vol.21 , pp. 201-205
    • Mysels, K.J.1
  • 15
    • 0019317512 scopus 로고
    • Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands
    • Nolte, H J , T. L. Rosenberry, and E. Neumann. 1980. Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry. 19:3705-3711.
    • (1980) Biochemistry , vol.19 , pp. 3705-3711
    • Nolte, H.J.1    Rosenberry, T.L.2    Neumann, E.3
  • 16
    • 33947480381 scopus 로고
    • Electric properties of macromolecules. IV. Determination of electric and optical parameters from saturation of electric birefringence in solutions
    • O'Konski, C. T., K. Yoshioka, and W. H. Ottung. 1959. Electric properties of macromolecules. IV. Determination of electric and optical parameters from saturation of electric birefringence in solutions. J. Phys. Chem. 63:1558-1565.
    • (1959) J. Phys. Chem. , vol.63 , pp. 1558-1565
    • O'Konski, C.T.1    Yoshioka, K.2    Ottung, W.H.3
  • 17
    • 0019322239 scopus 로고
    • Structure and dynamics of a tryptophanepeptide-polynucieotide complex
    • Porschke, D. 1980. Structure and dynamics of a tryptophanepeptide-polynucieotide complex. Nucleic Acids Res. 8:1591-1612.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 1591-1612
    • Porschke, D.1
  • 18
    • 0021926711 scopus 로고
    • The mechanism of ion polarisation along DNA double helices
    • Porschke, D. 1985. The mechanism of ion polarisation along DNA double helices. Biophys. Chem. 22:237-247.
    • (1985) Biophys. Chem. , vol.22 , pp. 237-247
    • Porschke, D.1
  • 19
    • 0023442745 scopus 로고
    • Electric, optical and hydrodynamic parameters of lac repressor from measurements of the electric dichroism - High permanent dipole moment associated with the protein
    • Porsehke, D. 1987. Electric, optical and hydrodynamic parameters of lac repressor from measurements of the electric dichroism - high permanent dipole moment associated with the protein. Biophys. Chem. 28:137-147.
    • (1987) Biophys. Chem. , vol.28 , pp. 137-147
    • Porsehke, D.1
  • 20
    • 0021870990 scopus 로고
    • The conformation of single stranded oligonucieotides and of oligonucleotide-oligopeptide complexes from their rotation relaxation in the nanosecond time range
    • Porschke, D., and M. Jung. 1985. The conformation of single stranded oligonucieotides and of oligonucleotide-oligopeptide complexes from their rotation relaxation in the nanosecond time range. J. Biomol. Struct. Dyn. 2:1173-1184.
    • (1985) J. Biomol. Struct. Dyn. , vol.2 , pp. 1173-1184
    • Porschke, D.1    Jung, M.2
  • 21
    • 33845282579 scopus 로고
    • Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states
    • Quinn, D. M. 1987. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem. Rev. 87:955-979.
    • (1987) Chem. Rev. , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 22
    • 0027265211 scopus 로고
    • An electrostatic guidance mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
    • Ripoll, D. R., C. H. Faerman, P. H. Axelsen, I. Silman, and J. L. Sussman. 1993. An electrostatic guidance mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proc. Natl. Acad. Sci. USA. 90:5128-5132.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5128-5132
    • Ripoll, D.R.1    Faerman, C.H.2    Axelsen, P.H.3    Silman, I.4    Sussman, J.L.5
  • 23
    • 0027934296 scopus 로고
    • Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase
    • Shafferman, A., A. Ordentlich, D. Barak, C. Kronman, R. Ber, T. Bino, N. Ariel, R. Osman, and B. Velan. 1994. Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase. EMBO J. 13:3448-3455.
    • (1994) EMBO J. , vol.13 , pp. 3448-3455
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Kronman, C.4    Ber, R.5    Bino, T.6    Ariel, N.7    Osman, R.8    Velan, B.9
  • 24
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J. L., M. Harel, F. Frolow, C. Oefner, A. Goldman, L. Toker, and I. Silman. 1991. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 253: 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 25
    • 0027386759 scopus 로고
    • Acetylcholinesterase: Electrostatic steering increases the rate of ligand binding
    • Tan, R. C., T. N. Troung, J. A. McCammon, and J. L. Sussman. 1993. Acetylcholinesterase: electrostatic steering increases the rate of ligand binding. Biochemistry. 32:401-403.
    • (1993) Biochemistry , vol.32 , pp. 401-403
    • Tan, R.C.1    Troung, T.N.2    McCammon, J.A.3    Sussman, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.