메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages

Optically induced thermal gradients for protein characterization in nanolitre-scale samples in microfluidic devices

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 84881467435     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02130     Document Type: Article
Times cited : (13)

References (31)
  • 2
    • 15944380354 scopus 로고    scopus 로고
    • High-throughput measurement of protein stability in microtiter plates
    • DOI 10.1002/bit.20397
    • Aucamp, J. P., Cosme, A. M., Lye, G. J. & Dalby, P. A. High-throughput measurement of protein stability in microtiter plates. Biotechnol. Bioeng. 89, 599-607 (2005). (Pubitemid 40444814)
    • (2005) Biotechnology and Bioengineering , vol.89 , Issue.5 , pp. 599-607
    • Aucamp, J.P.1    Cosme, A.M.2    Lye, G.J.3    Dalby, P.A.4
  • 3
    • 79959451524 scopus 로고    scopus 로고
    • Leveraging the contribution of thermodynamics in drug discovery with the help of fluorescence-based thermal shift assays
    • Hau, J. C. et al. Leveraging the contribution of thermodynamics in drug discovery with the help of fluorescence-based thermal shift assays. J. Biomol. Screen. 16, 552-556 (2011).
    • (2011) J. Biomol. Screen. , vol.16 , pp. 552-556
    • Hau, J.C.1
  • 4
    • 78650485354 scopus 로고    scopus 로고
    • Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes
    • Layton, C. J. & Hellinga, H. W. Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes. Biochemistry 49, 10831-10841 (2010).
    • (2010) Biochemistry , vol.49 , pp. 10831-10841
    • Layton, C.J.1    Hellinga, H.W.2
  • 6
    • 79951674715 scopus 로고    scopus 로고
    • High-throughput process development for biopharmaceutical drug substances
    • Bhambure, R., Kumar, K. & Rathore, A.S. High-throughput process development for biopharmaceutical drug substances. Trends Biotechnol. 29, 127-135 (2011).
    • (2011) Trends Biotechnol. , vol.29 , pp. 127-135
    • Bhambure, R.1    Kumar, K.2    Rathore, A.S.3
  • 7
    • 79957998371 scopus 로고    scopus 로고
    • Protein stability by number: High-throughput and statistical approaches to one of protein science's most difficult problems
    • Magliery, T. J., Lavinder, J. J. & Sullivan, B. J. Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems. Curr. Opin. Chem. Biol. 15, 443-451 (2011).
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 443-451
    • Magliery, T.J.1    Lavinder, J.J.2    Sullivan, B.J.3
  • 8
    • 77955120354 scopus 로고    scopus 로고
    • Protein denaturation and protein:Drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale
    • Gaudet, M., Remtulla, N., Jackson, S. E., Main, E. R. G., Bracewell, D. G., Aeppli, G. & Dalby, P. A. Protein denaturation and protein:drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale. Protein Sci. 19, 1544-1554 (2010).
    • (2010) Protein Sci. , vol.19 , pp. 1544-1554
    • Gaudet, M.1    Remtulla, N.2    Jackson, S.E.3    Main, E.R.G.4    Bracewell, D.G.5    Aeppli, G.6    Dalby, P.A.7
  • 9
    • 67849129183 scopus 로고    scopus 로고
    • High-throughput thermal scanning: A general, rapid dye-binding thermal shift screen for protein engineering
    • Lavinder, J. J., Hari, S. B., Sullivan, B. J. & Magliery, T. J. High-throughput thermal scanning: A general, rapid dye-binding thermal shift screen for protein engineering. J. Am. Chem. Soc. 131, 3794-3795 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3794-3795
    • Lavinder, J.J.1    Hari, S.B.2    Sullivan, B.J.3    Magliery, T.J.4
  • 10
    • 79960692993 scopus 로고    scopus 로고
    • Quantitation of protein-protein interactions by thermal stability shift analysis
    • Layton, C. J. & Hellinga, H. W. Quantitation of protein-protein interactions by thermal stability shift analysis. Protein Sci. 20, 1439-1450 (2011).
    • (2011) Protein Sci. , vol.20 , pp. 1439-1450
    • Layton, C.J.1    Hellinga, H.W.2
  • 11
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M. M. & Bolen, D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068 (1988).
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 12
    • 0030967237 scopus 로고    scopus 로고
    • Thermal denaturation of iso-l-cytochrome c variants: Comparison with solvent denaturation
    • Herrmann, L. M. & Bowler, B. E. Thermal denaturation of iso-1-cytochrome c variants: Comparison with solvent denaturation. Protein Sci. 6, 657-665 (1997). (Pubitemid 27120062)
    • (1997) Protein Science , vol.6 , Issue.3 , pp. 657-665
    • Herrmann, L.M.1    Bowler, B.E.2
  • 13
    • 79951577757 scopus 로고    scopus 로고
    • A high-throughput fluorescence chemical denaturation assay as a general screen for protein-ligand binding
    • Mahendrarajah, K., Dalby, P. A., Wilkinson, B., Jackson, S. E. & Main, E. R. G. A high-throughput fluorescence chemical denaturation assay as a general screen for protein-ligand binding. Anal. Biochem. 411, 155-157 (2011).
    • (2011) Anal. Biochem. , vol.411 , pp. 155-157
    • Mahendrarajah, K.1    Dalby, P.A.2    Wilkinson, B.3    Jackson, S.E.4    Main, E.R.G.5
  • 14
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using thermofluor
    • DOI 10.1021/bi048135v
    • Matulis, D., Kranz, J. K., Raymond Salemme, F. & Todd, M. J. Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry 44, 5258-5266 (2005). (Pubitemid 40471238)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 15
    • 0025234587 scopus 로고
    • PH-Induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson, D. E., Becktel, W. J. & Dahlquist, F. W. pH-Induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29, 2403-2408 (1990). (Pubitemid 20095485)
    • (1990) Biochemistry , vol.29 , Issue.9 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 17
    • 8344290520 scopus 로고    scopus 로고
    • Acid denaturation and refolding of green fluorescent protein
    • DOI 10.1021/bi048733+
    • Enoki, S., Saeki, K., Maki, K. & Kuwajima, K. Acid denaturation and refolding of green fluorescent protein. Biochemistry 43, 14238-14248 (2004). (Pubitemid 39482773)
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14238-14248
    • Enoki, S.1    Saeki, K.2    Maki, K.3    Kuwajima, K.4
  • 18
    • 77952027734 scopus 로고    scopus 로고
    • Thermal trap for DNA replication
    • Mast, C. B. & Braun, D. Thermal trap for DNA replication. Phys. Rev. Lett. 104, 188102-188106 (2010).
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 188102-188106
    • Mast, C.B.1    Braun, D.2
  • 19
    • 0642285283 scopus 로고    scopus 로고
    • Exponential DNA replication by laminar convection
    • Braun, D., Goddard, N. L. & Libchaber, A. Exponential DNA replication by laminar convection. Phys. Rev. Lett. 91, 158103-158106 (2003).
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 158103-158106
    • Braun, D.1    Goddard, N.L.2    Libchaber, A.3
  • 20
    • 34848914313 scopus 로고    scopus 로고
    • Melting curve analysis in a shapshot
    • Baaske, P., Duhr, S. & Braun, D. Melting curve analysis in a shapshot. Appl. Phys. Lett. 91, 133901-133903 (2007).
    • (2007) Appl. Phys. Lett. , vol.91 , pp. 133901-133903
    • Baaske, P.1    Duhr, S.2    Braun, D.3
  • 21
    • 8344290520 scopus 로고    scopus 로고
    • Acid denaturation and refolding of green fluorescent protein
    • DOI 10.1021/bi048733+
    • Enoki, S., Saeki, K., Maki, K. & Kuwajima, K. Acid denaturation and refolding of green fluorescent protein. Biochemistry 43, 14238-14248 (2004) (Pubitemid 39482773)
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14238-14248
    • Enoki, S.1    Saeki, K.2    Maki, K.3    Kuwajima, K.4
  • 22
    • 0036489443 scopus 로고    scopus 로고
    • Green Fluorescent Protein (GFP): Applications, structure, and related photophysical behavior
    • Zimmer, M. Green Fluorescent Protein (GFP): Applications, structure, and related photophysical behavior. Chem. Rev. 102, 759-782 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 759-782
    • Zimmer, M.1
  • 23
    • 0019892005 scopus 로고
    • Renaturation of aequorea green-fluorescent protein
    • Bokman, S. H. & Ward, W. W. Renaturation of aequorea green-fluorescent protein. Biochem. Biophys. Res. Comm. 101, 1372-1380 (1981).
    • (1981) Biochem. Biophys. Res. Comm. , vol.101 , pp. 1372-1380
    • Bokman, S.H.1    Ward, W.W.2
  • 24
    • 1242264025 scopus 로고    scopus 로고
    • Thermal characteristics of recombinant green fluorescent protein (GFPuv) extracted from Escherichia coli
    • DOI 10.1111/j.1472-765X.2003.01460.x
    • Vessoni Penna, T. C., Ishii, M., Cholewa, O. & Souza, L. C. Thermal characteristics of recombinant green fluorescent protein (GFPuv) extracted from Escherichia coli. Letts. Appl. Microbiol. 38, 135-139 (2004). (Pubitemid 38232703)
    • (2004) Letters in Applied Microbiology , vol.38 , Issue.2 , pp. 135-139
    • Vessoni Penna, T.C.1    Ishii, M.2    Cholewa, O.3    De Souza, L.C.4
  • 25
    • 24044492592 scopus 로고    scopus 로고
    • Effect of pH on thermal- and chemical-induced denaturation of GFP
    • DOI 10.1385/ABAB:126:2:149
    • Alkaabi, K. M., Yafea, A. & Ashraf, S. S. Effect of pH on thermal-and chemical-induced denaturation of GFP. Appl. Biochem. Biotechnol. 126, 149-156 (2005). (Pubitemid 41213294)
    • (2005) Applied Biochemistry and Biotechnology , vol.126 , Issue.2 , pp. 149-156
    • Alkaabi, K.M.1    Yafea, A.2    Ashraf, S.S.3
  • 27
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. J. & Schellman, J. A. Protein stability curves. Biopolymers 26, 1859-1877 (1987).
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 28
    • 0030029469 scopus 로고    scopus 로고
    • Interactions of the CelS binding ligand with various receptor domains of the Clostridium thermocellum cellulosomal scaffolding protein, CipA
    • Lytle, B., Myers, C., Kruus, K. & Wu, J. H. Interactions of the CelS binding ligand with various receptor domains of the Clostridium thermocellum cellulosomal scaffolding protein, CipA. J. Bacteriol. 178, 1200-1203 (1996). (Pubitemid 26048041)
    • (1996) Journal of Bacteriology , vol.178 , Issue.4 , pp. 1200-1203
    • Lytle, B.1    Myers, C.2    Kruus, K.3    Wu, J.H.D.4
  • 29
    • 34848914313 scopus 로고    scopus 로고
    • Melting curve analysis in a snapshot
    • Baaske, P., Duhr, S. & Braun, D. Melting curve analysis in a snapshot. Appl. Phys. Lett. 91, 133901 (2007).
    • (2007) Appl. Phys. Lett. , vol.91 , pp. 133901
    • Baaske, P.1    Duhr, S.2    Braun, D.3
  • 30
    • 10844287980 scopus 로고    scopus 로고
    • Thermophoresis of DNA determined by microfluidic fluorescence
    • DOI 10.1140/epje/i2004-10073-5
    • Duhr, S., Arduini, S. & Braun, D. Thermophoresis and DNA determined by microfluidic fluorescence. Eur. Phys. J. E. 15, 277-286 (2004). (Pubitemid 40003073)
    • (2004) European Physical Journal E , vol.15 , Issue.3 , pp. 277-286
    • Duhr, S.1    Arduini, S.2    Braun, D.3
  • 31
    • 0033542301 scopus 로고    scopus 로고
    • Incompressible limit for solutions of the isentropic Navier-Stokes equations with Dirichlet boundary conditions
    • Desjardins, B., Grenier, E., Lions, P. L. & Masmoudi, N. Incompressible limit for solutions of the isentropic Navier-Stokes equations with Dirichlet boundary conditions. J. Math. Pur. Appl. 78, 461-471 (1998).
    • (1998) J. Math. Pur. Appl. , vol.78 , pp. 461-471
    • Desjardins, B.1    Grenier, E.2    Lions, P.L.3    Masmoudi, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.