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Volumn 26, Issue 13, 2010, Pages 10433-10436

Application of Halotag protein to covalent immobilization of recombinant proteins for single molecule force spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPES; CONTOUR LENGTHS; COVALENT IMMOBILIZATION; FORCE-EXTENSION; MECHANICAL UNFOLDING; MICA SUBSTRATES; MICA SURFACES; POLYPROTEINS; RECOMBINANT PROTEIN; SINGLE MOLECULE FORCE SPECTROSCOPY; SITE-SPECIFIC; STANDARD METHOD;

EID: 77954268327     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la101658a     Document Type: Article
Times cited : (36)

References (28)
  • 2
    • 37749030526 scopus 로고    scopus 로고
    • Probing the mechanical stability of proteins using the atomic force microscope
    • Brockwell, D. J. Probing the mechanical stability of proteins using the atomic force microscope. Biochem. Soc. Trans. 2007, 35 (Pt 6), 1564 - 1568.
    • (2007) Biochem. Soc. Trans. , vol.35 , Issue.PART 6 , pp. 1564-1568
    • Brockwell, D.J.1
  • 8
    • 38349101056 scopus 로고    scopus 로고
    • The NTA-His6 bond is strong enough for AFM single-molecular recognition studies
    • Verbelen, C., Gruber, H. J., and Dufrene, Y. F. The NTA-His6 bond is strong enough for AFM single-molecular recognition studies. J. Mol. Recognit. 2007, 20 (6), 490 - 494.
    • (2007) J. Mol. Recognit. , vol.20 , Issue.6 , pp. 490-494
    • Verbelen, C.1    Gruber, H.J.2    Dufrene, Y.F.3
  • 9
    • 33745388031 scopus 로고    scopus 로고
    • Development of glutathione-coupled cantilever for the single-molecule force measurement by scanning force microscopy
    • Yoshimura, S. H., Takahashi, H., Otsuka, S., and Takeyasu, K. Development of glutathione-coupled cantilever for the single-molecule force measurement by scanning force microscopy. FEBS Lett. 2006, 580 (16), 3961 - 3965.
    • (2006) FEBS Lett. , vol.580 , Issue.16 , pp. 3961-3965
    • Yoshimura, S.H.1    Takahashi, H.2    Otsuka, S.3    Takeyasu, K.4
  • 10
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E. L., Moy, V. T., and Gaub, H. E. Adhesion forces between individual ligand-receptor pairs. Science 1994, 264 (5157), 415 - 417.
    • (1994) Science , vol.264 , Issue.5157 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 11
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy, V. T., Florin, E. L., and Gaub, H. E. Intermolecular forces and energies between ligands and receptors. Science 1994, 266 (5183), 257 - 259.
    • (1994) Science , vol.266 , Issue.5183 , pp. 257-259
    • Moy, V.T.1    Florin, E.L.2    Gaub, H.E.3
  • 12
    • 27944496013 scopus 로고    scopus 로고
    • Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy
    • Kufer, S. K., Dietz, H., Albrecht, C., Blank, K., Kardinal, A., Rief, M., and Gaub, H. E. Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy. Eur. Biophys. J. 2005, 35 (1), 72 - 78.
    • (2005) Eur. Biophys. J. , vol.35 , Issue.1 , pp. 72-78
    • Kufer, S.K.1    Dietz, H.2    Albrecht, C.3    Blank, K.4    Kardinal, A.5    Rief, M.6    Gaub, H.E.7
  • 15
    • 34447272975 scopus 로고    scopus 로고
    • The HaloTag: A novel technology for cell imaging and protein analysis
    • Los, G. V. and Wood, K. The HaloTag: a novel technology for cell imaging and protein analysis. Methods Mol. Biol. 2007, 356, 195 - 208.
    • (2007) Methods Mol. Biol. , vol.356 , pp. 195-208
    • Los, G.V.1    Wood, K.2
  • 16
    • 68349127373 scopus 로고    scopus 로고
    • HaloTag7: A genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification
    • Ohana, R. F., Encell, L. P., Zhao, K., Simpson, D., Slater, M. R., Urh, M., and Wood, K. V. HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification. Protein Expression Purif. 2009, 68 (1), 110 - 120.
    • (2009) Protein Expression Purif. , vol.68 , Issue.1 , pp. 110-120
    • Ohana, R.F.1    Encell, L.P.2    Zhao, K.3    Simpson, D.4    Slater, M.R.5    Urh, M.6    Wood, K.V.7
  • 17
    • 0036891724 scopus 로고    scopus 로고
    • Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold
    • Zinober, R. C., Brockwell, D. J., Beddard, G. S., Blake, A. W., Olmsted, P. D., Radford, S. E., and Smith, D. A. Mechanically unfolding proteins: the effect of unfolding history and the supramolecular scaffold. Protein Sci. 2002, 11 (12), 2759 - 2765.
    • (2002) Protein Sci. , vol.11 , Issue.12 , pp. 2759-2765
    • Zinober, R.C.1    Brockwell, D.J.2    Beddard, G.S.3    Blake, A.W.4    Olmsted, P.D.5    Radford, S.E.6    Smith, D.A.7
  • 18
    • 0036931098 scopus 로고    scopus 로고
    • Glutaraldehyde modified mica: A new surface for atomic force microscopy of chromatin
    • Wang, H., Bash, R., Yodh, J. G., Hager, G. L., Lohr, D., and Lindsay, S. M. Glutaraldehyde modified mica: a new surface for atomic force microscopy of chromatin. Biophys. J. 2002, 83 (6), 3619 - 3625.
    • (2002) Biophys. J. , vol.83 , Issue.6 , pp. 3619-3625
    • Wang, H.1    Bash, R.2    Yodh, J.G.3    Hager, G.L.4    Lohr, D.5    Lindsay, S.M.6
  • 19
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt, H. J. and Jaschke, M. Calculation of thermal noise in atomic force microscopy. Nanotechnology 1995, 6, 1 - 7.
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2
  • 22
    • 58149356274 scopus 로고    scopus 로고
    • The effect of temperature on mechanical resistance of the native and intermediate States of I27
    • Taniguchi, Y., Brockwell, D. J., and Kawakami, M. The effect of temperature on mechanical resistance of the native and intermediate States of I27. Biophys. J. 2008, 95, 5296 - 5305.
    • (2008) Biophys. J. , vol.95 , pp. 5296-5305
    • Taniguchi, Y.1    Brockwell, D.J.2    Kawakami, M.3
  • 24
    • 41249102384 scopus 로고    scopus 로고
    • Mechanical unfoldons as building blocks of maltose-binding protein
    • Bertz, M. and Rief, M. Mechanical unfoldons as building blocks of maltose-binding protein. J. Mol. Biol. 2008, 378 (2), 447 - 458.
    • (2008) J. Mol. Biol. , vol.378 , Issue.2 , pp. 447-458
    • Bertz, M.1    Rief, M.2
  • 25
    • 41149180083 scopus 로고    scopus 로고
    • Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: Evidence for a kinetic partitioning mechanism
    • Peng, Q. and Li, H. Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: evidence for a kinetic partitioning mechanism. Proc. Natl. Acad. Sci. U.S.A. 2008, 105 (6), 1885 - 1890.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.6 , pp. 1885-1890
    • Peng, Q.1    Li, H.2
  • 26
    • 1842479420 scopus 로고    scopus 로고
    • Evolving haloalkane dehalogenases
    • Janssen, D. B. Evolving haloalkane dehalogenases. Curr. Opin. Chem. Biol. 2004, 8 (2), 150 - 159.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , Issue.2 , pp. 150-159
    • Janssen, D.B.1
  • 28
    • 0034809309 scopus 로고    scopus 로고
    • Force measurement and inhibitor binding assay of monomer and engineered dimer of bovine carbonic anhydrase B
    • Wang, T., Arakawa, H., and Ikai, A. Force measurement and inhibitor binding assay of monomer and engineered dimer of bovine carbonic anhydrase B. Biochem. Biophys. Res. Commun. 2001, 285 (1), 9 - 14.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , Issue.1 , pp. 9-14
    • Wang, T.1    Arakawa, H.2    Ikai, A.3


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