메뉴 건너뛰기




Volumn 1430, Issue 2, 1999, Pages 323-340

Electric birefringence of recombinant spectrin segments 14, 14-15, 14-16, and 14-17 from Drosophila α-spectrin

Author keywords

Birefringence; Dipole moment; Flexibility; Spectrin

Indexed keywords

SPECTRIN;

EID: 0033017979     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00014-X     Document Type: Article
Times cited : (5)

References (47)
  • 1
    • 0025848106 scopus 로고
    • The spectrin super-family
    • Dhermy D. The spectrin super-family. Biol. Cell. 71:1991;249-254.
    • (1991) Biol. Cell , vol.71 , pp. 249-254
    • Dhermy, D.1
  • 2
    • 0022168490 scopus 로고
    • Stabilizing infrastructure of cell membranes
    • Marchesi V.T. Stabilizing infrastructure of cell membranes. Annu. Rev. Cell Biol. 1:1985;531-561.
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 531-561
    • Marchesi, V.T.1
  • 3
    • 0022646311 scopus 로고
    • Spectrin, human erythrocyte shapes and mechanochemical properties
    • Stokke B.T., Mikkelsen A., Elgsaeter A. Spectrin, human erythrocyte shapes and mechanochemical properties. Biophys. J. 49:1986;319-328.
    • (1986) Biophys. J. , vol.49 , pp. 319-328
    • Stokke, B.T.1    Mikkelsen, A.2    Elgsaeter, A.3
  • 4
    • 0345379917 scopus 로고
    • Physical chemistry of the red cell cytoskeleton: The spectrin network
    • Mikkelsen A., Stokke B.T., Elgsaeter A. Physical chemistry of the red cell cytoskeleton: the spectrin network. Biorheology. 23:1986;213.
    • (1986) Biorheology , vol.23 , pp. 213
    • Mikkelsen, A.1    Stokke, B.T.2    Elgsaeter, A.3
  • 6
    • 0025042504 scopus 로고
    • Spectrin: A structural mediator between diverse plasma membrane proteins and the cytoplasm
    • Bennett V. Spectrin: a structural mediator between diverse plasma membrane proteins and the cytoplasm. Curr. Opin. Cell Biol. 2:1990;51-56.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 51-56
    • Bennett, V.1
  • 7
    • 0025937014 scopus 로고
    • Shapes and shape changes in vitro in normal red cells
    • Elgsaeter A., Mikkelsen A. Shapes and shape changes in vitro in normal red cells. Biochim. Biophys. Acta. 1071:1991;273-290.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 273-290
    • Elgsaeter, A.1    Mikkelsen, A.2
  • 8
    • 0029825450 scopus 로고    scopus 로고
    • Peptides with more than one 106-amino acid sequence motif are needed to mimic the structural stability of spectrin
    • Menhart N., Mitchell T., Lusitani D., Topouzian N., Fung L.W.-M. Peptides with more than one 106-amino acid sequence motif are needed to mimic the structural stability of spectrin. J. Biol. Chem. 271:1996;30410-30416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30410-30416
    • Menhart, N.1    Mitchell, T.2    Lusitani, D.3    Topouzian, N.4    Fung, L.W.-M.5
  • 9
    • 0030042322 scopus 로고    scopus 로고
    • Spectrin: On the path from structure to function
    • Viel A., Branton D. Spectrin: on the path from structure to function. Curr. Opin. Cell Biol. 8:1996;49-55.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 49-55
    • Viel, A.1    Branton, D.2
  • 11
    • 0029913841 scopus 로고    scopus 로고
    • Mapping the human erythrocyte beta-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the alpha-actinin dimer site
    • Ursitti J.A., Kotula L., DeSilva T.M., Curtis P.J., Speicher D.W. Mapping the human erythrocyte beta-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the alpha-actinin dimer site. J. Biol. Chem. 271:1996;6636-6644.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6636-6644
    • Ursitti, J.A.1    Kotula, L.2    Desilva, T.M.3    Curtis, P.J.4    Speicher, D.W.5
  • 12
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual J., Pfuhl M., Rivas G., Pastore A., Saraste M. The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett. 383:1996;201-207.
    • (1996) FEBS Lett. , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 13
    • 0027749280 scopus 로고
    • Crystal structure of the repetitive segments of spectrin
    • Yan Y., Winograd E., Viel A., Cronin T., Harrison S.C. Crystal structure of the repetitive segments of spectrin. Science. 262:1993;2027-2030.
    • (1993) Science , vol.262 , pp. 2027-2030
    • Yan, Y.1    Winograd, E.2    Viel, A.3    Cronin, T.4    Harrison, S.C.5
  • 14
    • 0027977886 scopus 로고
    • A proton nuclear magnetic resonance study of the mobile regions of human erythroid spectrin
    • Begg G.E., Ralston G.B., Morris M.B. A proton nuclear magnetic resonance study of the mobile regions of human erythroid spectrin. Biophys. Chem. 52:1994;63-73.
    • (1994) Biophys. Chem. , vol.52 , pp. 63-73
    • Begg, G.E.1    Ralston, G.B.2    Morris, M.B.3
  • 15
    • 0030009643 scopus 로고    scopus 로고
    • Self-association of spectrin's repeating segments
    • Ralston G.B., Cronin T.J., Branton D. Self-association of spectrin's repeating segments. Biochemistry. 35:1996;5257-5263.
    • (1996) Biochemistry , vol.35 , pp. 5257-5263
    • Ralston, G.B.1    Cronin, T.J.2    Branton, D.3
  • 17
    • 0030066743 scopus 로고    scopus 로고
    • Erythrocyte spectrin maintains its segmental motions on oxidation: A spin-label EPR study
    • Fung L.W.-M., Kalaw B.O., Hatfield R.M., Dias M.N. Erythrocyte spectrin maintains its segmental motions on oxidation: a spin-label EPR study. Biophys. J. 70:1996;841-851.
    • (1996) Biophys. J. , vol.70 , pp. 841-851
    • Fung, L.W.-M.1    Kalaw, B.O.2    Hatfield, R.M.3    Dias, M.N.4
  • 18
    • 0020214922 scopus 로고
    • Differences in the electric birefringence of spectrin dimers and tetramers as shown by the fast reversing electric pulse method
    • Roux B., Cassoly R. Differences in the electric birefringence of spectrin dimers and tetramers as shown by the fast reversing electric pulse method. Biophys. Chem. 16:1982;193-198.
    • (1982) Biophys. Chem. , vol.16 , pp. 193-198
    • Roux, B.1    Cassoly, R.2
  • 19
    • 0026755595 scopus 로고
    • Dynamic light scattering investigations of human erythrocyte spectrin
    • Budzynski D.M., Benight A.S., LaBrake C.C., Fung L.W.-M. Dynamic light scattering investigations of human erythrocyte spectrin. Biochemistry. 31:1992;3653-3660.
    • (1992) Biochemistry , vol.31 , pp. 3653-3660
    • Budzynski, D.M.1    Benight, A.S.2    Labrake, C.C.3    Fung, L.W.-M.4
  • 20
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin: Biophysical and electron microscopic studies
    • Shotton D.M., Burke B., Branton D. The molecular structure of human erythrocyte spectrin: biophysical and electron microscopic studies. J. Mol. Biol. 131:1979;303-329.
    • (1979) J. Mol. Biol. , vol.131 , pp. 303-329
    • Shotton, D.M.1    Burke, B.2    Branton, D.3
  • 21
    • 0021840724 scopus 로고
    • Human erythrocyte spectrin dimer intrinsic viscosity: Temperature dependence and implications for the molecular basis of the erythrocyte membrane
    • Stokke B.T., Mikkelsen A., Elgsaeter A. Human erythrocyte spectrin dimer intrinsic viscosity: temperature dependence and implications for the molecular basis of the erythrocyte membrane. Biochim. Biophys. Acta. 816:1985;102-110.
    • (1985) Biochim. Biophys. Acta , vol.816 , pp. 102-110
    • Stokke, B.T.1    Mikkelsen, A.2    Elgsaeter, A.3
  • 23
    • 0032075297 scopus 로고    scopus 로고
    • Brownian dynamics simulation of needle-spring chains
    • Mikkelsen A., Knudsen K.D., Elgsaeter A. Brownian dynamics simulation of needle-spring chains. Physica A. 253:1998;66-76.
    • (1998) Physica a , vol.253 , pp. 66-76
    • Mikkelsen, A.1    Knudsen, K.D.2    Elgsaeter, A.3
  • 26
    • 0032499724 scopus 로고    scopus 로고
    • Electrooptic analysis of macromolecule dipole moments using asymmetric reversing electric pulses
    • Bjørkøy A., Elgsaeter A., Mikkelsen A. Electrooptic analysis of macromolecule dipole moments using asymmetric reversing electric pulses. Biophys. Chem. 72:1998;247-264.
    • (1998) Biophys. Chem. , vol.72 , pp. 247-264
    • Bjørkøy, A.1    Elgsaeter, A.2    Mikkelsen, A.3
  • 27
    • 4243642135 scopus 로고
    • Comparison of theories for the translational and rotational diffusion coefficients of rod-like macromolecules. Application to short DNA fragments
    • Tirado M.M. Comparison of theories for the translational and rotational diffusion coefficients of rod-like macromolecules. Application to short DNA fragments. J. Chem. Phys. 81:1984;2047-2052.
    • (1984) J. Chem. Phys. , vol.81 , pp. 2047-2052
    • Tirado, M.M.1
  • 28
    • 0000741446 scopus 로고
    • Time-dependent birefringence, linear dichroism, and optical rotation resulting from rigid-body rotational diffusion
    • Wegener W.A., Dowben R.M., Koester V.J. Time-dependent birefringence, linear dichroism, and optical rotation resulting from rigid-body rotational diffusion. J. Chem. Phys. 70:1979;622-632.
    • (1979) J. Chem. Phys. , vol.70 , pp. 622-632
    • Wegener, W.A.1    Dowben, R.M.2    Koester, V.J.3
  • 29
    • 0028605876 scopus 로고
    • Hydrodynamics of segmentally flexible macromolecules
    • Garcia de la Torre J. Hydrodynamics of segmentally flexible macromolecules. Eur. Biophys. J. 23:1994;307-322.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 307-322
    • Garcia De La Torre, J.1
  • 30
    • 84985720098 scopus 로고
    • Monte Carlo approach to the analysis of the rotational diffusion of wormlike chains
    • Hagerman P.J., Zimm B.H. Monte Carlo approach to the analysis of the rotational diffusion of wormlike chains. Biopolymers. 20:1981;1481-1502.
    • (1981) Biopolymers , vol.20 , pp. 1481-1502
    • Hagerman, P.J.1    Zimm, B.H.2
  • 32
    • 0015159414 scopus 로고
    • A nanosecond temperature-jump apparatus
    • Hoffman G.W. A nanosecond temperature-jump apparatus. Rev. Sci. Instrum. 42:1971;1643-1647.
    • (1971) Rev. Sci. Instrum. , vol.42 , pp. 1643-1647
    • Hoffman, G.W.1
  • 33
    • 0017020199 scopus 로고
    • Cable temperature jump apparatus with improved sensitivity and time resolution
    • Porschke D. Cable temperature jump apparatus with improved sensitivity and time resolution. Rev. Sci. Instrum. 47:1976;1363-1365.
    • (1976) Rev. Sci. Instrum. , vol.47 , pp. 1363-1365
    • Porschke, D.1
  • 34
    • 0001286652 scopus 로고
    • An electric field jump apparatus with ns time resolution for electro-optical measurements at physiological salt concentrations
    • Porschke D., Obst A. An electric field jump apparatus with ns time resolution for electro-optical measurements at physiological salt concentrations. Rev. Sci. Instrum. 62:1991;818-820.
    • (1991) Rev. Sci. Instrum. , vol.62 , pp. 818-820
    • Porschke, D.1    Obst, A.2
  • 36
    • 0033008239 scopus 로고    scopus 로고
    • Transient electric birefringence of human erythroid spectrin dimers and tetramers at ionic strengths 4 and 53 mM
    • submitted for publication
    • A. Bjørkøy, A. Mikkelsen, A. Elgsaeter, Transient electric birefringence of human erythroid spectrin dimers and tetramers at ionic strengths 4 and 53 mM, Eur. Biophys. J., submitted for publication.
    • Eur. Biophys. J.
    • Bjørkøy, A.1    Mikkelsen, A.2    Elgsaeter, A.3
  • 37
    • 0018083895 scopus 로고
    • Human spectrin. II. An electro-optic study
    • Mikkelsen A., Elgsaeter A. Human spectrin. II. An electro-optic study. Biochim. Biophys. Acta. 536:1978;245-251.
    • (1978) Biochim. Biophys. Acta , vol.536 , pp. 245-251
    • Mikkelsen, A.1    Elgsaeter, A.2
  • 38
    • 0019889485 scopus 로고
    • A comparative electro-optic study of heterotetramers and heterodimers
    • Mikkelsen A., Elgsaeter A., Human Spectrin V. A comparative electro-optic study of heterotetramers and heterodimers. Biochim. Biophys. Acta. 668:1981;74-80.
    • (1981) Biochim. Biophys. Acta , vol.668 , pp. 74-80
    • Mikkelsen, A.1    Elgsaeter, A.2    Human Spectrin, V.3
  • 39
    • 13044286837 scopus 로고    scopus 로고
    • Deconvolution can be used in electrooptic studies to correct for non-ideal electric excitation pulses only when the permanent dipole moment of the studied molecules is negligible
    • submitted for publication
    • A. Bjørkøy, A. Elgsaeter, A. Mikkelsen, Deconvolution can be used in electrooptic studies to correct for non-ideal electric excitation pulses only when the permanent dipole moment of the studied molecules is negligible, J. Biochem. Biophys. Methods, submitted for publication.
    • J. Biochem. Biophys. Methods
    • Bjørkøy, A.1    Elgsaeter, A.2    Mikkelsen, A.3
  • 40
    • 84981430529 scopus 로고
    • Numerical analysis of the rotational relaxation time of spectrin segments and spectrin heterodimer in dilute aqueous solution
    • Skjetne P., Knudsen K.D., Garcia de la Torre J., Elgsaeter A. Numerical analysis of the rotational relaxation time of spectrin segments and spectrin heterodimer in dilute aqueous solution. Macromol. Theory Simul. 4:1995;253-275.
    • (1995) Macromol. Theory Simul. , vol.4 , pp. 253-275
    • Skjetne, P.1    Knudsen, K.D.2    Garcia De La Torre, J.3    Elgsaeter, A.4
  • 41
    • 0006379005 scopus 로고
    • Brownian dynamics of the polarization of rodlike polyelectrolytes
    • Grycuk T., Antosiewicz J., Porschke D. Brownian dynamics of the polarization of rodlike polyelectrolytes. J. Phys. Chem. 98:1994;10881-10887.
    • (1994) J. Phys. Chem. , vol.98 , pp. 10881-10887
    • Grycuk, T.1    Antosiewicz, J.2    Porschke, D.3
  • 42
    • 0017256999 scopus 로고
    • Intramembrane particle aggregation in erythrocyte ghosts II. The influence of spectrin aggregation
    • Elgsaeter A., Shotton D., Branton D. Intramembrane particle aggregation in erythrocyte ghosts II. The influence of spectrin aggregation. Biochim. Biophys. Acta. 426:1976;101-122.
    • (1976) Biochim. Biophys. Acta , vol.426 , pp. 101-122
    • Elgsaeter, A.1    Shotton, D.2    Branton, D.3
  • 44
    • 33646937708 scopus 로고    scopus 로고
    • Analysis of chemical and physical relaxation processes of polyelectrolytes by electric field pulse methods: A comparison of critical comments with facts
    • Porschke D. Analysis of chemical and physical relaxation processes of polyelectrolytes by electric field pulse methods: a comparison of critical comments with facts. Ber. Bunsenges. Phys. Chem. 100:1996;715-720.
    • (1996) Ber. Bunsenges. Phys. Chem. , vol.100 , pp. 715-720
    • Porschke, D.1
  • 45
    • 0008217485 scopus 로고
    • Brownian dynamics simulations of electrooptic transients for complex macrodipoles
    • Antosiewicz J., Porschke D. Brownian dynamics simulations of electrooptic transients for complex macrodipoles. J. Phys. Chem. 97:1993;2767-2773.
    • (1993) J. Phys. Chem. , vol.97 , pp. 2767-2773
    • Antosiewicz, J.1    Porschke, D.2
  • 46
    • 0029100915 scopus 로고
    • Computation of the dipole moments of proteins
    • Antosiewicz J. Computation of the dipole moments of proteins. Biophys. J. 69:1995;1344-1354.
    • (1995) Biophys. J. , vol.69 , pp. 1344-1354
    • Antosiewicz, J.1
  • 47
    • 4243463817 scopus 로고
    • Electrostatics in biomolecular structure and dynamics
    • Davis M.E., McCammon J.A. Electrostatics in biomolecular structure and dynamics. Chem. Rev. 90:1990;509-521.
    • (1990) Chem. Rev. , vol.90 , pp. 509-521
    • Davis, M.E.1    McCammon, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.