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Volumn 19, Issue 11, 2010, Pages 2085-2095

Experimental optimization of protein refolding with a genetic algorithm

Author keywords

Genetic algorithms; High throughput optimization; Inclusion bodies; Multiobjective optimization; Protein refolding

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; GLUCOKINASE; GLUTATHIONE REDUCTASE; LYSOZYME; RECOMBINANT PROTEIN;

EID: 78349240664     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.488     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, Lilie H (1996) In vitro folding of inclusion body proteins. FASEB J 10:49-56.
    • (1996) FASEB J , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 2
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg AP (2002) Preparative protein refolding. Trends Biotechnol 20:437-443.
    • (2002) Trends Biotechnol , vol.20 , pp. 437-443
    • Middelberg, A.P.1
  • 3
    • 33846371209 scopus 로고    scopus 로고
    • Current status of technical protein refolding
    • DOI 10.1016/j.jbiotec.2006.12.004, PII S0168165606010273
    • Jungbauer A, Kaar W (2007) Current status of technical protein refolding. J Biotechnol 128:587-596. (Pubitemid 46135798)
    • (2007) Journal of Biotechnology , vol.128 , Issue.3 , pp. 587-596
    • Jungbauer, A.1    Kaar, W.2
  • 4
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • Clark E (2001) Protein refolding for industrial processes. Curr Opin Biotechnol 12:202-207.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 202-207
    • Clark, E.1
  • 5
    • 71549172508 scopus 로고    scopus 로고
    • Refolding solubilized inclusion body proteins
    • Burgess R (2009) Refolding solubilized inclusion body proteins. Methods Enzymol 463:259-282.
    • (2009) Methods Enzymol , vol.463 , pp. 259-282
    • Burgess, R.1
  • 6
    • 7044228084 scopus 로고    scopus 로고
    • Protein expression and refolding - A practical guide to getting the most out of inclusion bodies
    • Cabrita LD, Bottomley SP (2004) Protein expression and refolding - a practical guide to getting the most out of inclusion bodies. Biotechnol Annu Rev 10:31-50.
    • (2004) Biotechnol Annu Rev , vol.10 , pp. 31-50
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 7
    • 41549118541 scopus 로고    scopus 로고
    • A screening system for the identification of refolding conditions for a model protein kinase, p38alpha
    • Cowan RH, Davies RA, Pinheiro TT (2008) A screening system for the identification of refolding conditions for a model protein kinase, p38alpha. Anal Biochem 376:25-38.
    • (2008) Anal Biochem , vol.376 , pp. 25-38
    • Cowan, R.H.1    Davies, R.A.2    Pinheiro, T.T.3
  • 8
    • 33646580434 scopus 로고    scopus 로고
    • High-throughput identification of refolding conditions for LXRbeta without a functional assay
    • DOI 10.1016/j.pep.2005.11.010, PII S1046592805003967
    • Lin L, Seehra J, Stahl ML (2006) High-throughput identification of refolding conditions for LXRbeta without a functional assay. Protein Expr Purif 47:355-366. (Pubitemid 43729006)
    • (2006) Protein Expression and Purification , vol.47 , Issue.2 , pp. 355-366
    • Lin, L.1    Seehra, J.2    Stahl, M.L.3
  • 9
    • 22244468386 scopus 로고    scopus 로고
    • Investigation of protein refolding using a fractional factorial screen: A study of reagent effects and interactions
    • DOI 10.1110/ps.051433205
    • Willis MS, Hogan JK, Prabhakar P, Liu X, Tsai K, Wei Y, Fox T (2005) Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions. Protein Sci 14:1818-1826. (Pubitemid 40994152)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1818-1826
    • Willis, M.S.1    Hogan, J.K.2    Prabhakar, P.3    Liu, X.4    Tsai, K.5    Wei, Y.6    Fox, T.7
  • 11
    • 1642493929 scopus 로고    scopus 로고
    • An automated in vitro protein folding screen applied to a human dynactin subunit
    • DOI 10.1110/ps.03304604
    • Scheich C, Niesen FH, Seckler R, Büssow K (2004) An automated in vitro protein folding screen applied to a human dynactin subunit. Protein Sci 13:370-380. (Pubitemid 38124958)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 370-380
    • Scheich, C.1    Niesen, F.H.2    Seckler, R.3    Bussow, K.4
  • 14
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase
    • Armstrong N, de Lencastre A, Gouaux E (1999) A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase. Protein Sci 8:1475-1483. (Pubitemid 29328228)
    • (1999) Protein Science , vol.8 , Issue.7 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 18
    • 36049035020 scopus 로고    scopus 로고
    • Multi-objective optimization in combinatorial chemistry applied to the selective catalytic reduction of NO with C3H6
    • Gobin OC, Joaristi AM, Schüth F (2007) Multi-objective optimization in combinatorial chemistry applied to the selective catalytic reduction of NO with C3H6. J Catal 252:205-214.
    • (2007) J Catal , vol.252 , pp. 205-214
    • Gobin, O.C.1    Joaristi, A.M.2    Schüth, F.3
  • 19
    • 57549088017 scopus 로고    scopus 로고
    • On the suitability of different representations of solid catalysts for combinatorial library design by genetic algorithms
    • Gobin OC, Schüth F (2008) On the suitability of different representations of solid catalysts for combinatorial library design by genetic algorithms. J Comb Chem 10:835-846.
    • (2008) J Comb Chem , vol.10 , pp. 835-846
    • Gobin, O.C.1    Schüth, F.2
  • 20
    • 0034319166 scopus 로고    scopus 로고
    • Experimental design for fermentation media development: Statistical design or global random search?
    • Weuster-Botz D (2000) Experimental design for fermentation media development: statistical design or global random search? J Biosci Bioeng 90:473-483.
    • (2000) J Biosci Bioeng , vol.90 , pp. 473-483
    • Weuster-Botz, D.1
  • 21
    • 33748519287 scopus 로고    scopus 로고
    • Comparison of genetic algorithms for experimental multi-objective optimization on the example of medium design for cyanobacteria
    • Havel J, Link H, Hofinger M, Franco-Lara E, Weuster-Botz D (2006) Comparison of genetic algorithms for experimental multi-objective optimization on the example of medium design for cyanobacteria. Biotechnol J 1:549-555.
    • (2006) Biotechnol J , vol.1 , pp. 549-555
    • Havel, J.1    Link, H.2    Hofinger, M.3    Franco-Lara, E.4    Weuster-Botz, D.5
  • 22
    • 33751265229 scopus 로고    scopus 로고
    • Genetic algorithm for multi-objective experimental optimization
    • DOI 10.1007/s00449-006-0087-7
    • Link H, Weuster-Botz D (2006) Genetic algorithm for multi-objective experimental optimization. Bioprocess Biosyst Eng 29:385-390. (Pubitemid 44800774)
    • (2006) Bioprocess and Biosystems Engineering , vol.29 , Issue.5-6 , pp. 385-390
    • Link, H.1    Weuster-Botz, D.2
  • 25
    • 34548456411 scopus 로고    scopus 로고
    • Confronting high-throughput protein refolding using high pressure and solution screens
    • DOI 10.1016/j.pep.2007.05.014, PII S1046592807001416
    • Qoronfleh MW, Hesterberg LK, Seefeldt MB (2007) Confronting high-throughput protein refolding using high pressure and solution screens. Protein Expr Purif 55:209-224. (Pubitemid 47369657)
    • (2007) Protein Expression and Purification , vol.55 , Issue.2 , pp. 209-224
    • Qoronfleh, M.W.1    Hesterberg, L.K.2    Seefeldt, M.B.3
  • 28
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan DL, De Bernardez Clark E (1997) Oxidative renaturation of lysozyme at high concentrations. Biotechnol Bioeng 54:221-230.
    • (1997) Biotechnol Bioeng , vol.54 , pp. 221-230
    • Hevehan, D.L.1    De Bernardez Clark, E.2
  • 30
    • 2942547409 scopus 로고    scopus 로고
    • SPEA2: Improving the strength pareto evolutionary algorithm for multi-objective optimization
    • KC Giannakoglou, DT Tsahalis, J Periaux, KD Papaliliou, T Fogarty, Eds. Barcelona, Spain: CIMNE
    • Zitzler E, Laumanns M, Thiele L,SPEA2: improving the strength pareto evolutionary algorithm for multi-objective optimization. In: KC Giannakoglou, DT Tsahalis, J Periaux, KD Papaliliou, T Fogarty, Eds. (2002) Evolutionary methods for design, optimisation and control, Barcelona, Spain: CIMNE, pp 95-100.
    • (2002) Evolutionary Methods for Design, Optimisation and Control , pp. 95-100
    • Zitzler, E.1    Laumanns, M.2    Thiele, L.3
  • 31
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • Davies RC, Neuberger A, Wilson BM (1969) The dependence of lysozyme activity on pH and ionic strength. Biochim Biophys Acta 178:294-305.
    • (1969) Biochim Biophys Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 32
    • 0032788447 scopus 로고    scopus 로고
    • Circularly permuted variants of the green fluorescent protein
    • DOI 10.1016/S0014-5793(99)01044-3, PII S0014579399010443
    • Topell S, Hennecke J, Glockshuber R (1999) Circularly permuted variants of the green fluorescent protein. FEBS Lett 457:283-289. (Pubitemid 29401943)
    • (1999) FEBS Letters , vol.457 , Issue.2 , pp. 283-289
    • Topell, S.1    Hennecke, J.2    Glockshuber, R.3
  • 33
    • 0023809599 scopus 로고
    • Coupled assay of Na+,K+-ATPase activity
    • Nørby JG (1988) Coupled assay of Na+,K+-ATPase activity. Methods Enzymol 156:116-119.
    • (1988) Methods Enzymol , vol.156 , pp. 116-119
    • Nørby, J.G.1
  • 34
    • 0014429143 scopus 로고
    • Purification and subunit structure of glutathione reductase from bakers' yeast
    • Mavis D, Stellwagen E (1968) Purification and subunit structure of glutathione reductase from bakers' yeast. Biol Chem 4:809-814.
    • (1968) Biol Chem , vol.4 , pp. 809-814
    • Mavis, D.1    Stellwagen, E.2


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