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Volumn 5, Issue 12, 1998, Pages 689-697

Strategies for protein-based nanofabrication: Ni2+-NTA as a chemical mask to control biologically imposed symmetry

Author keywords

Atomic force microscopy; Histidine tag proteins; Molecular self assembly; Protein engineering; Proteins on surfaces

Indexed keywords

NANOFABRICATION; PROTEIN ENGINEERING;

EID: 13144302850     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(98)90662-7     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0028971503 scopus 로고
    • Nanotechnology: R & D challenges and opportunities for application in biotechnology
    • Laval, J.M., Chopineau, J. & Thomas, D. (1995). Nanotechnology: R & D challenges and opportunities for application in biotechnology. Trends Biotechnol. 13, 474-481.
    • (1995) Trends Biotechnol. , vol.13 , pp. 474-481
    • Laval, J.M.1    Chopineau, J.2    Thomas, D.3
  • 2
    • 0031127671 scopus 로고    scopus 로고
    • Photo-switchable biomaterials as ground for optobioelectronic devices
    • Wilner, I. & Wilner, B. (1997). Photo-switchable biomaterials as ground for optobioelectronic devices. Bioelec. Bioenerg. 42, 43-57.
    • (1997) Bioelec. Bioenerg. , vol.42 , pp. 43-57
    • Wilner, I.1    Wilner, B.2
  • 3
    • 0002859612 scopus 로고    scopus 로고
    • The development of peptide nanostructures
    • Voyer, R. (1997). The development of peptide nanostructures. Bioorg. Chem. 184, 1-37.
    • (1997) Bioorg. Chem. , vol.184 , pp. 1-37
    • Voyer, R.1
  • 4
    • 0029185755 scopus 로고
    • Biospecific adsorption of carbonic anhydrase to self-assembled monolayers of alkanethiolates that present benzenesulfonamide groups on gold
    • Mrksich, M., Grunwell, J.R., & Whitesides, G.M. (1995). Biospecific adsorption of carbonic anhydrase to self-assembled monolayers of alkanethiolates that present benzenesulfonamide groups on gold. J. Am. Chem. Soc. 117, 12009-12010.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12009-12010
    • Mrksich, M.1    Grunwell, J.R.2    Whitesides, G.M.3
  • 7
    • 0030739097 scopus 로고    scopus 로고
    • Formation of stable polypeptide monolayers at interfaces: Controlling molecular conformation and orientation
    • Boncheva, M. & Vogel, H. (1997). Formation of stable polypeptide monolayers at interfaces: controlling molecular conformation and orientation. Biophys. J. 73, 1056-1072.
    • (1997) Biophys. J. , vol.73 , pp. 1056-1072
    • Boncheva, M.1    Vogel, H.2
  • 8
    • 0342710343 scopus 로고    scopus 로고
    • Self-assembling of glutathione S-transferase/calmodulin fusion protein on chemically modified gold surface
    • Damrongchai, N., Yun, K., Kobatake, E. & Aizawa, M. (1997). Self-assembling of glutathione S-transferase/calmodulin fusion protein on chemically modified gold surface. J. Biotechnol. 55, 125-133.
    • (1997) J. Biotechnol. , vol.55 , pp. 125-133
    • Damrongchai, N.1    Yun, K.2    Kobatake, E.3    Aizawa, M.4
  • 9
    • 0031259833 scopus 로고    scopus 로고
    • Affinity fusion strategies for detection, purification and immobilization of recombinant proteins
    • Stahl, S., Lundeberg, J., Uhlen, M. & Nygren, P.A. (1997). Affinity fusion strategies for detection, purification and immobilization of recombinant proteins. Prot. Express. Purif. 11, 1-16.
    • (1997) Prot. Express. Purif. , vol.11 , pp. 1-16
    • Stahl, S.1    Lundeberg, J.2    Uhlen, M.3    Nygren, P.A.4
  • 10
    • 0001620620 scopus 로고
    • Genetic engineering of surface attachment sites yields oriented protein monolayers
    • Stayton, P.S., Olinger, J.M., Jiang, M., Bohn, P.W. & Sligar, S.G. (1992). Genetic engineering of surface attachment sites yields oriented protein monolayers. J. Am. Chem. Soc. 114, 9298-9299.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9298-9299
    • Stayton, P.S.1    Olinger, J.M.2    Jiang, M.3    Bohn, P.W.4    Sligar, S.G.5
  • 11
    • 0029025914 scopus 로고
    • Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids
    • Dietrich, C., Schmitt, L. & Tampe, R. (1995). Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids. Proc. Natl Acad. Sci. USA 92, 9014-9018.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9014-9018
    • Dietrich, C.1    Schmitt, L.2    Tampe, R.3
  • 12
    • 0029995882 scopus 로고    scopus 로고
    • Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines
    • Frey, W., et. al., & Arnold, F.H. (1996). Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines. Proc. Natl Acad. Sci. USA 93, 4937-4941.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4937-4941
    • Frey, W.1    Arnold, F.H.2
  • 13
    • 0025925381 scopus 로고
    • 3-His sites in α-helices of synthetic metal-binding bovine somatotropin
    • 3-His sites in α-helices of synthetic metal-binding bovine somatotropin. Prot. Eng. 4, 301-305.
    • (1991) Prot. Eng. , vol.4 , pp. 301-305
    • Suh, S.-S.1    Haymore, B.L.2    Arnold, F.H.3
  • 14
    • 0030949053 scopus 로고    scopus 로고
    • Reversible oriented surface immobilization of functional proteins on oxide surfaces
    • Schmid, E.L., Keller, T.A., Dienes, Z. & Vogel, H. (1997). Reversible oriented surface immobilization of functional proteins on oxide surfaces. Anal. Chem. 69, 1979-1985.
    • (1997) Anal. Chem. , vol.69 , pp. 1979-1985
    • Schmid, E.L.1    Keller, T.A.2    Dienes, Z.3    Vogel, H.4
  • 15
    • 0031570909 scopus 로고    scopus 로고
    • Generation of biotin/avidin/enzyme nanostructures with maskless photolithography
    • Dontha, N., Nowall, W.B. & Kuhr, W.G. (1997). Generation of biotin/avidin/enzyme nanostructures with maskless photolithography. Anal. Chem. 69, 2619-2625.
    • (1997) Anal. Chem. , vol.69 , pp. 2619-2625
    • Dontha, N.1    Nowall, W.B.2    Kuhr, W.G.3
  • 16
    • 0028820735 scopus 로고
    • Engineered chimeric streptavidin tetramers as novel tools for bioseparations and drug delivery
    • Chilkoti, A., Schwartz, B.L., Smith, R.D., Long, C.J. & Stayton, P.S. (1995). Engineered chimeric streptavidin tetramers as novel tools for bioseparations and drug delivery. Biotechnology 13, 1198-1204.
    • (1995) Biotechnology , vol.13 , pp. 1198-1204
    • Chilkoti, A.1    Schwartz, B.L.2    Smith, R.D.3    Long, C.J.4    Stayton, P.S.5
  • 17
    • 0022776515 scopus 로고
    • Novel subunit interactions in the structure of glutamine synthetase
    • Almassy, R.J., Janson, C.A., Hamlin, R., Xuong, N.H. & Eisenberg, D. (1986). Novel subunit interactions in the structure of glutamine synthetase. Nature. 323, 304-309.
    • (1986) Nature , vol.323 , pp. 304-309
    • Almassy, R.J.1    Janson, C.A.2    Hamlin, R.3    Xuong, N.H.4    Eisenberg, D.5
  • 18
    • 0008387356 scopus 로고
    • Glutamine synthetase forms three- and seven-stranded cables
    • Frey, T.G., Eisenberg, D. & Eiserling, F.A. (1975). Glutamine synthetase forms three- and seven-stranded cables. Proc. Natl Acad. Sci. USA 72, 3402-3406.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 3402-3406
    • Frey, T.G.1    Eisenberg, D.2    Eiserling, F.A.3
  • 19
    • 0028618538 scopus 로고
    • Supramolecular self-assembly of glutamine synthetase: Mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking
    • Dabrowski, M.J., Yanchunas, J. Jr., Villafranca, B.C., Dietze, E.C., Schurke, P.J. & Atkins, W.M. (1994). Supramolecular self-assembly of glutamine synthetase: mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking. Biochemistry 33, 14957-14964.
    • (1994) Biochemistry , vol.33 , pp. 14957-14964
    • Dabrowski, M.J.1    Yanchunas Jr., J.2    Villafranca, B.C.3    Dietze, E.C.4    Schurke, P.J.5    Atkins, W.M.6
  • 20
    • 0028618788 scopus 로고
    • Supramolecular self-assembly of E. coli glutamine synthetase: Characterization of dodecamer stacking and high-order association
    • Yanchunas, J., Dabrowski, M.J., Schurke, P.J. & Atkins, W.M. (1994). Supramolecular self-assembly of E. coli glutamine synthetase: characterization of dodecamer stacking and high-order association. Biochemistry 33, 14949-14956.
    • (1994) Biochemistry , vol.33 , pp. 14949-14956
    • Yanchunas, J.1    Dabrowski, M.J.2    Schurke, P.J.3    Atkins, W.M.4
  • 21
    • 0028639233 scopus 로고
    • Supramolecular self-assembly of E. coli glutamine synthetase: Effects of pressure and adenylylation state on dodecamer stacking
    • Atkins, W.M. (1994). Supramolecular self-assembly of E. coli glutamine synthetase: effects of pressure and adenylylation state on dodecamer stacking. Biochemistry 33, 14965-14973.
    • (1994) Biochemistry , vol.33 , pp. 14965-14973
    • Atkins, W.M.1
  • 22
    • 0031425151 scopus 로고    scopus 로고
    • Synthesis and characterization of supramolecular protein aggregates: Self-assembled, molecularly-ordered, protein tubes from electrostatic complementation of glutamine synthetase dodecamers
    • Dabrowski, M.J., Chen, J.P. & Atkins, W.M. (1997). Synthesis and characterization of supramolecular protein aggregates: self-assembled, molecularly-ordered, protein tubes from electrostatic complementation of glutamine synthetase dodecamers. Protein Eng. 10, 1289-1294.
    • (1997) Protein Eng. , vol.10 , pp. 1289-1294
    • Dabrowski, M.J.1    Chen, J.P.2    Atkins, W.M.3
  • 23
    • 0029519283 scopus 로고
    • Engineering macromolecular self-assembly: Molecular tubes vs. protein sheets via single amino acid substitutions in E. coli glutamine synthetase
    • Dabrowski, M.D. & Atkins, W.M. (1995). Engineering macromolecular self-assembly: molecular tubes vs. protein sheets via single amino acid substitutions in E. coli glutamine synthetase. Adv. Mater. 7, 1015-1017.
    • (1995) Adv. Mater. , vol.7 , pp. 1015-1017
    • Dabrowski, M.D.1    Atkins, W.M.2
  • 24
    • 0013568403 scopus 로고
    • Application of dynamic light scattering to biological systems
    • (Brown, W., ed.), University Press, New York
    • Janmey, P.A. (1993). Application of dynamic light scattering to biological systems. In Dynamic Light Scattering: The Method and Some Applications (Brown, W., ed.), University Press, New York. 5, 611-651.
    • (1993) Dynamic Light Scattering: The Method and Some Applications , vol.5 , pp. 611-651
    • Janmey, P.A.1
  • 25
    • 0028364295 scopus 로고
    • Biomolecular imaging with the atomic force microscope
    • Hansma, H.G. & Hoh, J. (1994). Biomolecular imaging with the atomic force microscope. Ann. Rev. Biophys. Biomol. Struct. 23, 115-139.
    • (1994) Ann. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 115-139
    • Hansma, H.G.1    Hoh, J.2
  • 26
    • 0029807108 scopus 로고    scopus 로고
    • Bifunctional fusion proteins of calmodulin and protein A as affinity ligands in protein purification and in the study of protein-protein interactions
    • Hentz, N.G. & Daunert, S. (1996). Bifunctional fusion proteins of calmodulin and protein A as affinity ligands in protein purification and in the study of protein-protein interactions. Anal. Chem. 68, 3937-3944.
    • (1996) Anal. Chem. , vol.68 , pp. 3937-3944
    • Hentz, N.G.1    Daunert, S.2
  • 27
    • 0024375747 scopus 로고
    • Partial unfolding of dodecameric glutamine synthetase from Escherichia coli: Temperature-induced reversible transitions of two domains
    • Shrake, A., Fisher, M.T., McFarland, P.J. & Ginsburg, A. (1989) Partial unfolding of dodecameric glutamine synthetase from Escherichia coli: temperature-induced reversible transitions of two domains. Biochemistry 28, 6281-6294.
    • (1989) Biochemistry , vol.28 , pp. 6281-6294
    • Shrake, A.1    Fisher, M.T.2    McFarland, P.J.3    Ginsburg, A.4
  • 28
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethyl pyrocarbonate
    • Miles, E.W. (1977). Modification of histidyl residues in proteins by diethyl pyrocarbonate. Methods Enzymol. 47, 431-442.
    • (1977) Methods Enzymol. , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 29
    • 0020176542 scopus 로고
    • Constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher, S.W.A. (1982). Constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput. Phys. Commun. 27, 213-227.
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.A.1


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