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Volumn 6, Issue 5, 1996, Pages 643-649

Sometimes a great motion: The application of transient electric birefringence to the study of macromolecular structure

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMER; NUCLEIC ACID; PROTEIN;

EID: 0030272594     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80031-5     Document Type: Article
Times cited : (25)

References (56)
  • 3
    • 0023954970 scopus 로고
    • Electric linear dichroism and birefringence of biological polyelectrolytes
    • Charney E: Electric linear dichroism and birefringence of biological polyelectrolytes. O Rev Biophys 1988, 21:1-60.
    • (1988) O Rev Biophys , vol.21 , pp. 1-60
    • Charney, E.1
  • 4
    • 0000741446 scopus 로고
    • Time-dependent birefringence, linear dichroism, and optical rotation resulting from rigid-body rotational diffusion
    • Wegener WA, Dowben RM, Koester VJ: Time-dependent birefringence, linear dichroism, and optical rotation resulting from rigid-body rotational diffusion. J Chem Phys 1979, 70:622-632.
    • (1979) J Chem Phys , vol.70 , pp. 622-632
    • Wegener, W.A.1    Dowben, R.M.2    Koester, V.J.3
  • 9
    • 84985720098 scopus 로고
    • Monte Carlo approach to the analysis of the rotational diffusion of wormlike chains
    • Hagerman PJ, Zimm, BH: Monte Carlo approach to the analysis of the rotational diffusion of wormlike chains. Biopolymers 1981, 20:1481-1502.
    • (1981) Biopolymers , vol.20 , pp. 1481-1502
    • Hagerman, P.J.1    Zimm, B.H.2
  • 10
    • 0019588074 scopus 로고
    • Investigation of the flexibility of DNA using transient electric birefringence
    • Hagerman PJ: Investigation of the flexibility of DNA using transient electric birefringence. Biopolymers 1981, 20:1503-1535.
    • (1981) Biopolymers , vol.20 , pp. 1503-1535
    • Hagerman, P.J.1
  • 11
    • 84990485097 scopus 로고
    • Transport properties of rigid and flexible macromolecules by Brownian dynamics simulation
    • Allison SA, McCammon JA: Transport properties of rigid and flexible macromolecules by Brownian dynamics simulation. Biopolymers 1984, 23:167-187.
    • (1984) Biopolymers , vol.23 , pp. 167-187
    • Allison, S.A.1    McCammon, J.A.2
  • 12
    • 0000305475 scopus 로고
    • Brownian dynamics simulations of a three-subunit and a ten-subunit wormlike chain: Comparison of results with trumbell theory and with experimental results from DNA
    • Lewis RJ, Allison SA, Eden D, Pecora R: Brownian dynamics simulations of a three-subunit and a ten-subunit wormlike chain: comparison of results with trumbell theory and with experimental results from DNA. J Chem Phys 1988, 89:2490-2503.
    • (1988) J Chem Phys , vol.89 , pp. 2490-2503
    • Lewis, R.J.1    Allison, S.A.2    Eden, D.3    Pecora, R.4
  • 13
    • 0026736993 scopus 로고
    • Electric dichroism and birefringence decay of short DNA restriction fragments studied by Brownian dynamics simulation
    • Allison SA, Nambi P: Electric dichroism and birefringence decay of short DNA restriction fragments studied by Brownian dynamics simulation. Macromolecules 1992, 25:759-768.
    • (1992) Macromolecules , vol.25 , pp. 759-768
    • Allison, S.A.1    Nambi, P.2
  • 14
    • 0022473134 scopus 로고
    • Myosin subfragment 1 has tertiary structural domains
    • Highsmith S, Eden D: Myosin subfragment 1 has tertiary structural domains. Biochemistry 1986, 25:2237-2242.
    • (1986) Biochemistry , vol.25 , pp. 2237-2242
    • Highsmith, S.1    Eden, D.2
  • 15
    • 0025261971 scopus 로고
    • Ligand-induced myosin subfragment 1 global conformational change
    • Highsmith S, Eden D: Ligand-induced myosin subfragment 1 global conformational change. Biochemistry 1990, 29:4087-4093.
    • (1990) Biochemistry , vol.29 , pp. 4087-4093
    • Highsmith, S.1    Eden, D.2
  • 16
    • 0026346195 scopus 로고
    • On the flexibility of myosin in solution
    • Curry JF, Krause S: On the flexibility of myosin in solution. Biopolymers 1991, 31:1677-1687.
    • (1991) Biopolymers , vol.31 , pp. 1677-1687
    • Curry, J.F.1    Krause, S.2
  • 17
    • 0027418804 scopus 로고
    • A structural difference between filaments of phosphorylated and dephosphorylated Acanthamoeba myosin II revealed by electric birefringence
    • 7. Rau DC, Ganguly C, Koru ED: A structural difference between filaments of phosphorylated and dephosphorylated Acanthamoeba myosin II revealed by electric birefringence. J Biol Chem 1993, 268:4612-4621.
    • (1993) J Biol Chem , vol.268 , pp. 4612-4621
    • Rau, D.C.1    Ganguly, C.2    Koru, E.D.3
  • 18
    • 0027467450 scopus 로고
    • Myosin-ATP chemomechanics
    • Highsmith S, Eden D: Myosin-ATP chemomechanics. Biochemistry 1993, 32:2455-2458.
    • (1993) Biochemistry , vol.32 , pp. 2455-2458
    • Highsmith, S.1    Eden, D.2
  • 19
    • 0028958752 scopus 로고
    • Solution structure of two molecular motor domains: Nonclaret disjunctional and kinesin
    • Eden D, Luu BQ, Zapata DJ, Sablin EP, Kuli FJ: Solution structure of two molecular motor domains: nonclaret disjunctional and kinesin. Biophys J 1995, 68:59s-65s. A novel application of TEB to the study of two protein 'motor' domains. Although the two domains have very similar primary sequences, their hydrodynamic and electro-optical behaviors are found to be quite different. This investigation utilizes a birefringence instrument with a response time approaching 1 ns and a cell design that permits measurements to be made at physiological salt concentrations.
    • (1995) Biophys J , vol.68
    • Eden, D.1    Luu, B.Q.2    Zapata, D.J.3    Sablin, E.P.4    Kuli, F.J.5
  • 20
    • 0022385727 scopus 로고
    • Identification of a novel forcegenerating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS, Sheetz MP: Identification of a novel forcegenerating protein, kinesin, involved in microtubule-based motility. Cell 1985, 42:39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 21
    • 0025309662 scopus 로고
    • One motor, many tails: An expanding repertoire of force-generating enzymes
    • Vale RD, Goldstein LSB: One motor, many tails: an expanding repertoire of force-generating enzymes. Cell 1990, 60:883-885.
    • (1990) Cell , vol.60 , pp. 883-885
    • Vale, R.D.1    Goldstein, L.S.B.2
  • 22
    • 0025364774 scopus 로고
    • Identification and characterization of a gene encoding a kinesin-like protein in Drosophila
    • McDonald HB, Goldstein LSB: Identification and characterization of a gene encoding a kinesin-like protein in Drosophila. Cell 1990, 61:991-1000.
    • (1990) Cell , vol.61 , pp. 991-1000
    • McDonald, H.B.1    Goldstein, L.S.B.2
  • 23
    • 0027463255 scopus 로고
    • Structural and functional domains of the Drosophila ncd microtubule motor protein
    • Chandra R, Salmon ED, Erickson HP, Lockhart A, Endow SA: Structural and functional domains of the Drosophila ncd microtubule motor protein. J Biol Chem 1993, 268:9005-9013.
    • (1993) J Biol Chem , vol.268 , pp. 9005-9013
    • Chandra, R.1    Salmon, E.D.2    Erickson, H.P.3    Lockhart, A.4    Endow, S.A.5
  • 24
    • 0028348071 scopus 로고
    • Characterization of multiple oligomeric vimentin intermediate filament units by transient electric birefringence measurements
    • Kooijman M, Bloemendal M, Van Amerongen H, Traub P, Van Grondelle R: Characterization of multiple oligomeric vimentin intermediate filament units by transient electric birefringence measurements. J Mol Biol 1994, 236:1241-1249.
    • (1994) J Mol Biol , vol.236 , pp. 1241-1249
    • Kooijman, M.1    Bloemendal, M.2    Van Amerongen, H.3    Traub, P.4    Van Grondelle, R.5
  • 25
    • 0028859162 scopus 로고
    • The assembly state of the intermediate filament proteins desmin and glial fibrillary acidic protein at low ionic strength
    • Kooijman M, Van Amerongen H, Traub P, Van Grondelle R, Bloemendal M: The assembly state of the intermediate filament proteins desmin and glial fibrillary acidic protein at low ionic strength. FEBS Lett 1995, 358:185-188.
    • (1995) FEBS Lett , vol.358 , pp. 185-188
    • Kooijman, M.1    Van Amerongen, H.2    Traub, P.3    Van Grondelle, R.4    Bloemendal, M.5
  • 26
    • 0028850871 scopus 로고
    • Hydrodynamic and electrical characterization of T-vimentin dinners and tetramers by transient electric birefringence measurements
    • Kooijman M, Bloemendal M, Traub P, Van Grondelle R, Van Amerongen H: Hydrodynamic and electrical characterization of T-vimentin dinners and tetramers by transient electric birefringence measurements. J Biol Chem 1995, 270:2931-2937. This interesting study exploits the ability of birefringence measurements to distinguish between permanent and induced-dipole orientation mechanisms. It is shown that dimers of the intermediate filament protein T-vimentin (possessing a permanent dipole moment) are oriented in a staggered, antiparallel arrangement in the tetramer, as the latter lacked a detectable permanent moment.
    • (1995) J Biol Chem , vol.270 , pp. 2931-2937
    • Kooijman, M.1    Bloemendal, M.2    Traub, P.3    Van Grondelle, R.4    Van Amerongen, H.5
  • 27
    • 0000145810 scopus 로고
    • Transient electric birefringence study of the persistence length and electric polarizability of restriction fragments in DNA
    • Elias JG, Eden D: Transient electric birefringence study of the persistence length and electric polarizability of restriction fragments in DNA. Macromo/ecules 1981, 14:410-419.
    • (1981) Macromo/ecules , vol.14 , pp. 410-419
    • Elias, J.G.1    Eden, D.2
  • 28
    • 0019543558 scopus 로고
    • Electric birefringence of restriction enzyme fragments of DNA: Optical factor and electric polarizability as a function of molecular weight
    • Stellwagen NC: Electric birefringence of restriction enzyme fragments of DNA: Optical factor and electric polarizability as a function of molecular weight Biopolymers 1981, 20:399-434.
    • (1981) Biopolymers , vol.20 , pp. 399-434
    • Stellwagen, N.C.1
  • 29
    • 0027087437 scopus 로고
    • Zinc induces a bend within the transcription factor IIIA-binding region of the 5S RNA gene
    • Nickol J, Rau DC: Zinc induces a bend within the transcription factor IIIA-binding region of the 5S RNA gene. J Mol Biol 1992, 228:1115-1123.
    • (1992) J Mol Biol , vol.228 , pp. 1115-1123
    • Nickol, J.1    Rau, D.C.2
  • 30
    • 0030581180 scopus 로고    scopus 로고
    • Helix rigidity of DNA: The meroduplex as an experimental paradigm
    • Hagerman KR, Hagerman PJ: Helix rigidity of DNA: the meroduplex as an experimental paradigm. J Mol Biol 1996, 260:207-223. This investigation provides a demonstration of the extreme sensitivity of new birefringence instrumentation, providing well defined birefringence decay profiles for the single-stranded DNA polymer, (dTn), which has a signal strength that is less than 1% of the corresponding value for the duplex, dAn-dTn. The study also demonstrates that the principal determinant of helix rigidity is the base-stacking interaction.
    • (1996) J Mol Biol , vol.260 , pp. 207-223
    • Hagerman, K.R.1    Hagerman, P.J.2
  • 31
    • 0000231785 scopus 로고
    • Geometry of a branched DNA structure in solution
    • Cooper JP, Hagerman PJ: Geometry of a branched DNA structure in solution. Proc Natl Acad Sei USA 1989, 86:7336-7340.
    • (1989) Proc Natl Acad Sei USA , vol.86 , pp. 7336-7340
    • Cooper, J.P.1    Hagerman, P.J.2
  • 33
    • 0027982008 scopus 로고
    • Conformation of the central, threehelix junction of the 5 S ribosomal RNA of Su/folobus acidocaldarius
    • Shen Z, Hagerman PJ: Conformation of the central, threehelix junction of the 5 S ribosomal RNA of Su/folobus acidocaldarius. J Mol Biol 1994, 241:415-430.
    • (1994) J Mol Biol , vol.241 , pp. 415-430
    • Shen, Z.1    Hagerman, P.J.2
  • 34
    • 0028004021 scopus 로고
    • Global conformation of a self-cleaving hammerhead RNA
    • Amiri KMA, Hagerman PJ: Global conformation of a self-cleaving hammerhead RNA. Biochemistry 1994, 33:13172-13177.
    • (1994) Biochemistry , vol.33 , pp. 13172-13177
    • Amiri, K.M.A.1    Hagerman, P.J.2
  • 35
    • 0028969693 scopus 로고
    • Bulge-induced bends in RNA: Quantification by transient electric birefringence
    • Zacharias M, Hagerman PJ: Bulge-induced bends in RNA: quantification by transient electric birefringence. J Mol Biol 1995, 247:486-500. A systematic analysis of the magnitudes of bulge-induced distortions in RNA using TEB. This investigation provides a useful set of standards for analyzing the influence of nonhelix elements on RNA structure, and provides an evaluation of several of the assumptions that are implicit in the analysis of the decay profiles.
    • (1995) J Mol Biol , vol.247 , pp. 486-500
    • Zacharias, M.1    Hagerman, P.J.2
  • 37
    • 0029065694 scopus 로고
    • Determination of the angle between the anticodon and aminoacyl acceptor stems of yeast phenylalanyl tRNA in solution
    • Friederich MW, Gast F-U, Vacano E, Hagerman PJ: Determination of the angle between the anticodon and aminoacyl acceptor stems of yeast phenylalanyl tRNA in solution. Proc Natl Acad Sei USA 1995, 92:4803-4807.
    • (1995) Proc Natl Acad Sei USA , vol.92 , pp. 4803-4807
    • Friederich, M.W.1    Gast, F.-U.2    Vacano, E.3    Hagerman, P.J.4
  • 38
    • 0029032837 scopus 로고
    • The bend in RNA created by the trans-activation response element bulge of human immunodeficiency virus is straightened by arginine and by Tatderived peptide
    • Zacharias M, Hagerman PJ: The bend in RNA created by the trans-activation response element bulge of human immunodeficiency virus is straightened by arginine and by Tatderived peptide. Proc Natl Acad Sei USA 1995, 92:6052-6056. An application of TEB to the study of the interaction between a peptide and a nonhelix element (bulge) in RNA. Using the HIV Tat-TAR system, it is demonstrated that the initial -50' bend created by the bulge itself is essentially eliminated upon binding of either a Tat basic peptide or arginine.
    • (1995) Proc Natl Acad Sei USA , vol.92 , pp. 6052-6056
    • Zacharias, M.1    Hagerman, P.J.2
  • 40
    • 0029913806 scopus 로고    scopus 로고
    • The influence of symmetric internal loops on the flexibility of RNA
    • Zacharias M, Hagerman PJ: The influence of symmetric internal loops on the flexibility of RNA. J Mol Biol 1996, 257:276-289.
    • (1996) J Mol Biol , vol.257 , pp. 276-289
    • Zacharias, M.1    Hagerman, P.J.2
  • 42
    • 0030590218 scopus 로고    scopus 로고
    • The global conformation of an active hammerhead RNA during the process of self-cleavage
    • Amiri KMA, Hagerman PJ: The global conformation of an active hammerhead RNA during the process of self-cleavage. J Mol 8/0/1996, 261:125-134. All previous structural studies of the self-cleaving hammerhead RNA have been essentially static (equilibrium) measurements. This set of experiments has taken the birefringence approach into the time-resolved domain by measuring the decay profiles over the course of the self-cleaving reaction. It is demonstrated that no significant populations of intermediates that possess significantly altered global geometry are formed during the reaction. This experiment demonstrates the potential for TEB to study the evolution of global structure during the course of a reaction.
    • (1996) J Mol 8/0 , vol.261 , pp. 125-134
    • Amiri, K.M.A.1    Hagerman, P.J.2
  • 43
    • 0020161682 scopus 로고
    • Orientation relaxation of DNA restriction fragments and the internal mobility of the double helix
    • Diekmann S, Hillen W, Morgeneyer B, Wells RD, Porschke D: Orientation relaxation of DNA restriction fragments and the internal mobility of the double helix. Biophys Chem 1982, 15:263-270.
    • (1982) Biophys Chem , vol.15 , pp. 263-270
    • Diekmann, S.1    Hillen, W.2    Morgeneyer, B.3    Wells, R.D.4    Porschke, D.5
  • 44
    • 0023953148 scopus 로고
    • Turn of promoter DNA by cAMP receptor protein characterized by bead model simulation of rotational diffusion
    • Antosiewicz J, Porschke D: Turn of promoter DNA by cAMP receptor protein characterized by bead model simulation of rotational diffusion. J Biomol Struct Dyn 1988, 5:819-837.
    • (1988) J Biomol Struct Dyn , vol.5 , pp. 819-837
    • Antosiewicz, J.1    Porschke, D.2
  • 45
    • 0028351709 scopus 로고
    • The structure of the RNA polymerase-promoter complex DNA-bending-angle by quantitative electrooptics
    • Meyer-Almes F-J, Heumann H, Porschke D: The structure of the RNA polymerase-promoter complex DNA-bending-angle by quantitative electrooptics. J Mol Biol 1994, 236:1-6.
    • (1994) J Mol Biol , vol.236 , pp. 1-6
    • Meyer-Almes, F.-J.1    Heumann, H.2    Porschke, D.3
  • 47
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan JF, Groebe DR, Witherell GW, Uhlenbeck OC: Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res 1987, 15:8783-8798.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 50
    • 0026203710 scopus 로고
    • Electric birefringence imaging of electrokinetic agarose orientation
    • Lanan M, Shick R, Morris MD: Electric birefringence imaging of electrokinetic agarose orientation. Biopolymers 1991, 31:1095-1104.
    • (1991) Biopolymers , vol.31 , pp. 1095-1104
    • Lanan, M.1    Shick, R.2    Morris, M.D.3
  • 51
    • 0024977952 scopus 로고
    • Orientation of the agarose gel matrix in pulsed electric fields
    • Stellwagen J, Stellwagen NC: Orientation of the agarose gel matrix in pulsed electric fields. Nucleic Acids Res 1989, 17:1537-1548.
    • (1989) Nucleic Acids Res , vol.17 , pp. 1537-1548
    • Stellwagen, J.1    Stellwagen, N.C.2
  • 52
    • 0025838091 scopus 로고
    • Microscopic behaviour of DNA during electrophoresis: Electrophoretic orientation
    • Norden B, Elvingson C, Jonsson M, Akerman B: Microscopic behaviour of DNA during electrophoresis: electrophoretic orientation. Q Rev Biophys 1991, 24:103-164.
    • (1991) Q Rev Biophys , vol.24 , pp. 103-164
    • Norden, B.1    Elvingson, C.2    Jonsson, M.3    Akerman, B.4
  • 53
    • 0028156393 scopus 로고
    • Transient electric birefringence of agarose gels. I. Unidirectional electric fields
    • Stellwagen J, Stellwagen NC: Transient electric birefringence of agarose gels. I. Unidirectional electric fields. Biopolymers 1994, 34:187-201.
    • (1994) Biopolymers , vol.34 , pp. 187-201
    • Stellwagen, J.1    Stellwagen, N.C.2
  • 54
    • 0028501297 scopus 로고
    • Transient electric birefringence of agarose gels. II. Reversing electric fields and comparison with other polymer gels
    • Stellwagen J, Stellwagen NC: Transient electric birefringence of agarose gels. II. Reversing electric fields and comparison with other polymer gels. Biopolymers 1994, 34:1259-1273.
    • (1994) Biopolymers , vol.34 , pp. 1259-1273
    • Stellwagen, J.1    Stellwagen, N.C.2
  • 55
    • 0028130487 scopus 로고
    • The role of the adsorption complex in the termination of filamentous phage assembly
    • Gailus V, Ramsperger U, Johner C, Kramer H, Rasched I: The role of the adsorption complex in the termination of filamentous phage assembly. Res Microbiol 1994, 145:699-709.
    • (1994) Res Microbiol , vol.145 , pp. 699-709
    • Gailus, V.1    Ramsperger, U.2    Johner, C.3    Kramer, H.4    Rasched, I.5
  • 56
    • 0027165178 scopus 로고
    • Structural analysis of Trypanosoma brucei brucei chromatin by limited proteolysis
    • Michalon P, Couturier R, Bender K, Hecker H, Marion C: Structural analysis of Trypanosoma brucei brucei chromatin by limited proteolysis. Eur J Biochem 1993, 216:387-394.
    • (1993) Eur J Biochem , vol.216 , pp. 387-394
    • Michalon, P.1    Couturier, R.2    Bender, K.3    Hecker, H.4    Marion, C.5


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