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Volumn 2, Issue 2, 2013, Pages 83-92

Reducing codon redundancy and screening effort of combinatorial protein libraries created by saturation mutagenesis

Author keywords

codon redundancy; combinatorial mutagenesis; directed evolution; library quality; primer degeneracy; screening effort

Indexed keywords

CYCLOHEXANONE; UNSPECIFIC MONOOXYGENASE;

EID: 84874034041     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/sb300037w     Document Type: Article
Times cited : (232)

References (65)
  • 1
    • 0021826423 scopus 로고
    • Cassette mutagenesis - An efficient method for generation of multiple mutations at defined sites
    • Wells, J. A., Vasser, M., and Powers, D. B. (1985) Cassette mutagenesis-an efficient method for generation of multiple mutations at defined sites Gene 34, 315-323
    • (1985) Gene , vol.34 , pp. 315-323
    • Wells, J.A.1    Vasser, M.2    Powers, D.B.3
  • 2
    • 0022912910 scopus 로고
    • A simple and efficient procedure for saturation mutagenesis using mixed oligodeoxynucleotides
    • Derbyshire, K. M., Salvo, J. J., and Grindley, N. D. (1986) A simple and efficient procedure for saturation mutagenesis using mixed oligodeoxynucleotides Gene 46, 145-152
    • (1986) Gene , vol.46 , pp. 145-152
    • Derbyshire, K.M.1    Salvo, J.J.2    Grindley, N.D.3
  • 3
    • 0022479114 scopus 로고
    • Cloning of random-sequence oligodeoxynucleotides
    • Oliphant, A. R., Nussbaum, A. L., and Struhl, K. (1986) Cloning of random-sequence oligodeoxynucleotides Gene 44, 177-183
    • (1986) Gene , vol.44 , pp. 177-183
    • Oliphant, A.R.1    Nussbaum, A.L.2    Struhl, K.3
  • 4
    • 34250721751 scopus 로고    scopus 로고
    • Exploring and designing protein function with restricted diversity
    • Sidhu, S. S. and Kossiakoff, A. A. (2007) Exploring and designing protein function with restricted diversity Curr. Opin. Chem. Biol. 11, 347-354
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 347-354
    • Sidhu, S.S.1    Kossiakoff, A.A.2
  • 5
    • 79953318587 scopus 로고    scopus 로고
    • Status of protein engineering for biocatalysts: How to design an industrially useful biocatalyst
    • Bommarius, A. S., Blum, J. K., and Abrahamson, M. J. (2011) Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst Curr. Opin. Chem. Biol. 15, 194-200
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 194-200
    • Bommarius, A.S.1    Blum, J.K.2    Abrahamson, M.J.3
  • 6
    • 80052102623 scopus 로고    scopus 로고
    • Strategy and success for the directed evolution of enzymes
    • Dalby, P. A. (2011) Strategy and success for the directed evolution of enzymes Curr. Opin. Struct. Biol. 21, 473-480
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 473-480
    • Dalby, P.A.1
  • 7
    • 78149432825 scopus 로고    scopus 로고
    • Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions
    • Reetz, M. T. (2011) Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions Angew. Chem., Int. Ed. 50, 138-174
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 138-174
    • Reetz, M.T.1
  • 8
    • 68049111471 scopus 로고    scopus 로고
    • Finding better protein engineering strategies
    • Kazlauskas, R. J. and Bornscheuer, U. T. (2009) Finding better protein engineering strategies Nat. Chem. Biol. 5, 526-529
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 526-529
    • Kazlauskas, R.J.1    Bornscheuer, U.T.2
  • 9
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner, N. J. (2009) Directed evolution drives the next generation of biocatalysts Nat. Chem. Biol. 5, 567-573
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 567-573
    • Turner, N.J.1
  • 11
    • 79953310914 scopus 로고    scopus 로고
    • Optimizing non-natural protein function with directed evolution
    • Brustad, E. M. and Arnold, F. H. (2011) Optimizing non-natural protein function with directed evolution Curr. Opin. Chem. Biol. 15, 201-210
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 201-210
    • Brustad, E.M.1    Arnold, F.H.2
  • 12
    • 3543106035 scopus 로고    scopus 로고
    • Novel methods for directed evolution of enzymes: Quality, not quantity
    • Lutz, S. and Patrick, W. M. (2004) Novel methods for directed evolution of enzymes: quality, not quantity Curr. Opin. Biotechnol. 15, 291-297
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 291-297
    • Lutz, S.1    Patrick, W.M.2
  • 13
    • 2542563521 scopus 로고    scopus 로고
    • Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: Library construction methods for directed evolution
    • Neylon, C. (2004) Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution Nucleic Acids Res. 32, 1448-1459
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1448-1459
    • Neylon, C.1
  • 14
    • 84861228538 scopus 로고    scopus 로고
    • Site saturation mutagenesis: Methods and applications in protein engineering
    • Siloto, R. M. P. and Weselake, R. J. (2012) Site saturation mutagenesis: methods and applications in protein engineering Biocatal. Agric. Biotechnol. 181-189
    • (2012) Biocatal. Agric. Biotechnol. , pp. 181-189
    • Siloto, R.M.P.1    Weselake, R.J.2
  • 15
    • 8744220371 scopus 로고    scopus 로고
    • Inverse thinking about double mutants of enzymes
    • Mildvan, A. S. (2004) Inverse thinking about double mutants of enzymes Biochemistry 43, 14517-14520
    • (2004) Biochemistry , vol.43 , pp. 14517-14520
    • Mildvan, A.S.1
  • 16
    • 54349117265 scopus 로고    scopus 로고
    • Constructing and analyzing the fitness landscape of an experimental evolutionary process
    • Reetz, M. T. and Sanchis, J. (2008) Constructing and analyzing the fitness landscape of an experimental evolutionary process ChemBioChem 9, 2260-2267
    • (2008) ChemBioChem , vol.9 , pp. 2260-2267
    • Reetz, M.T.1    Sanchis, J.2
  • 17
    • 0014935646 scopus 로고
    • Natural selection and concept of a protein space
    • Smith, J. M. (1970) Natural selection and concept of a protein space Nature 225, 563-564
    • (1970) Nature , vol.225 , pp. 563-564
    • Smith, J.M.1
  • 18
    • 54349090614 scopus 로고    scopus 로고
    • Addressing the numbers problem in directed evolution
    • Reetz, M. T., Kahakeaw, D., and Lohmer, R. (2008) Addressing the numbers problem in directed evolution ChemBioChem 9, 1797-1804
    • (2008) ChemBioChem , vol.9 , pp. 1797-1804
    • Reetz, M.T.1    Kahakeaw, D.2    Lohmer, R.3
  • 19
    • 13844250741 scopus 로고    scopus 로고
    • High-throughput screens and selections of enzyme-encoding genes
    • Aharoni, A., Griffiths, A. D., and Tawfik, D. S. (2005) High-throughput screens and selections of enzyme-encoding genes Curr. Opin. Chem. Biol. 9, 210-216
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 210-216
    • Aharoni, A.1    Griffiths, A.D.2    Tawfik, D.S.3
  • 20
    • 79960984217 scopus 로고    scopus 로고
    • Protein engineering: Navigating between chance and reason
    • Baker, M. (2011) Protein engineering: navigating between chance and reason Nat. Methods 8, 623-626
    • (2011) Nat. Methods , vol.8 , pp. 623-626
    • Baker, M.1
  • 21
    • 58549110239 scopus 로고    scopus 로고
    • Shedding light on the efficacy of laboratory evolution based on iterative saturation mutagenesis
    • Reetz, M. T., Kahakeaw, D., and Sanchis, J. (2009) Shedding light on the efficacy of laboratory evolution based on iterative saturation mutagenesis Mol. BioSyst. 5, 115-122
    • (2009) Mol. BioSyst. , vol.5 , pp. 115-122
    • Reetz, M.T.1    Kahakeaw, D.2    Sanchis, J.3
  • 22
    • 0027761151 scopus 로고
    • Antibody Engineering by Parsimonious Mutagenesis
    • Balint, R. F. and Larrick, J. W. (1993) Antibody Engineering by Parsimonious Mutagenesis Gene 137, 109-118
    • (1993) Gene , vol.137 , pp. 109-118
    • Balint, R.F.1    Larrick, J.W.2
  • 23
    • 55849148481 scopus 로고    scopus 로고
    • Greatly reduced amino acid alphabets in directed evolution: Making the right choice for saturation mutagenesis at homologous enzyme positions
    • Reetz, M. T. and Wu, S. (2008) Greatly reduced amino acid alphabets in directed evolution: making the right choice for saturation mutagenesis at homologous enzyme positions Chem. Commun. (Cambridge) 5499-5501
    • (2008) Chem. Commun. (Cambridge) , pp. 5499-5501
    • Reetz, M.T.1    Wu, S.2
  • 24
    • 23444450226 scopus 로고    scopus 로고
    • Semi-rational approaches to engineering enzyme activity: Combining the benefits of directed evolution and rational design
    • Chica, R. A., Doucet, N., and Pelletier, J. N. (2005) Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design Curr. Opin. Biotechnol. 16, 378-384
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 378-384
    • Chica, R.A.1    Doucet, N.2    Pelletier, J.N.3
  • 25
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • Morley, K. L. and Kazlauskas, R. J. (2005) Improving enzyme properties: when are closer mutations better? Trends Biotechnol. 23, 231-237
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 26
    • 77954274719 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: Rigorous comparison with traditional methods
    • Reetz, M. T., Prasad, S., Carballeira, J. D., Gumulya, Y., and Bocola, M. (2010) Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: rigorous comparison with traditional methods J. Am. Chem. Soc. 132, 9144-9152
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9144-9152
    • Reetz, M.T.1    Prasad, S.2    Carballeira, J.D.3    Gumulya, Y.4    Bocola, M.5
  • 27
    • 84863337761 scopus 로고    scopus 로고
    • Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes
    • Chen, M. M., Snow, C. D., Vizcarra, C. L., Mayo, S. L., and Arnold, F. H. (2012) Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes Protein Eng. Des. Sel. 25, 171-178
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 171-178
    • Chen, M.M.1    Snow, C.D.2    Vizcarra, C.L.3    Mayo, S.L.4    Arnold, F.H.5
  • 28
    • 24044554219 scopus 로고    scopus 로고
    • Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase
    • Parikh, M. R. and Matsumura, I. (2005) Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase J. Mol. Biol. 352, 621-628
    • (2005) J. Mol. Biol. , vol.352 , pp. 621-628
    • Parikh, M.R.1    Matsumura, I.2
  • 30
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O'Maille, P. E., Bakhtina, M., and Tsai, M. D. (2002) Structure-based combinatorial protein engineering (SCOPE) J. Mol. Biol. 321, 677-691
    • (2002) J. Mol. Biol. , vol.321 , pp. 677-691
    • O'Maille, P.E.1    Bakhtina, M.2    Tsai, M.D.3
  • 31
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test
    • Reetz, M. T., Bocola, M., Carballeira, J. D., Zha, D. X., and Vogel, A. (2005) Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test Angew. Chem., Int. Ed. 44, 4192-4196
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 4192-4196
    • Reetz, M.T.1    Bocola, M.2    Carballeira, J.D.3    Zha, D.X.4    Vogel, A.5
  • 32
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz, M. T. and Carballeira, J. D. (2007) Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes Nat. Protoc. 2, 891-903
    • (2007) Nat. Protoc. , vol.2 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 34
    • 33846102955 scopus 로고    scopus 로고
    • Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function
    • Treynor, T. P., Vizcarra, C. L., Nedelcu, D., and Mayo, S. L. (2007) Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function Proc. Natl. Acad. Sci. U.S.A. 104, 48-53
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 48-53
    • Treynor, T.P.1    Vizcarra, C.L.2    Nedelcu, D.3    Mayo, S.L.4
  • 35
    • 65349142516 scopus 로고    scopus 로고
    • Computational tools for designing and engineering biocatalysts
    • Damborsky, J. and Brezovsky, J. (2009) Computational tools for designing and engineering biocatalysts Curr. Opin. Chem. Biol. 13, 26-34
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 26-34
    • Damborsky, J.1    Brezovsky, J.2
  • 38
    • 34250727621 scopus 로고    scopus 로고
    • Protein library design and screening: Working out the probabilities
    • Denault, M. and Pelletier, J. N. (2007) Protein library design and screening: working out the probabilities Methods Mol. Biol. 352, 127-154
    • (2007) Methods Mol. Biol. , vol.352 , pp. 127-154
    • Denault, M.1    Pelletier, J.N.2
  • 40
    • 0032030286 scopus 로고    scopus 로고
    • Codon-based mutagenesis using dimer-phosphoramidites
    • Neuner, P., Cortese, R., and Monaci, P. (1998) Codon-based mutagenesis using dimer-phosphoramidites Nucleic Acids Res. 26, 1223-1227
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1223-1227
    • Neuner, P.1    Cortese, R.2    Monaci, P.3
  • 41
    • 0028865576 scopus 로고
    • The synthesis of blocked triplet-phosphoramidites and their use in mutagenesis
    • Ono, A., Matsuda, A., Zhao, J., and Santi, D. V. (1995) The synthesis of blocked triplet-phosphoramidites and their use in mutagenesis Nucleic Acids Res. 23, 4677-4682
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4677-4682
    • Ono, A.1    Matsuda, A.2    Zhao, J.3    Santi, D.V.4
  • 42
    • 27944437517 scopus 로고    scopus 로고
    • Automated design of degenerate codon libraries
    • Mena, M. A. and Daugherty, P. S. (2005) Automated design of degenerate codon libraries Protein Eng., Des. Sel. 18, 559-561
    • (2005) Protein Eng., Des. Sel. , vol.18 , pp. 559-561
    • Mena, M.A.1    Daugherty, P.S.2
  • 43
    • 23944525846 scopus 로고    scopus 로고
    • Strategies and computational tools for improving randomized protein libraries
    • Patrick, W. M. and Firth, A. E. (2005) Strategies and computational tools for improving randomized protein libraries Biomol. Eng. 22, 105-112
    • (2005) Biomol. Eng. , vol.22 , pp. 105-112
    • Patrick, W.M.1    Firth, A.E.2
  • 44
    • 77956234144 scopus 로고    scopus 로고
    • Natural diversity to guide focused directed evolution
    • Jochens, H. and Bornscheuer, U. T. (2010) Natural diversity to guide focused directed evolution ChemBioChem 11, 1861-1866
    • (2010) ChemBioChem , vol.11 , pp. 1861-1866
    • Jochens, H.1    Bornscheuer, U.T.2
  • 45
    • 80052135332 scopus 로고    scopus 로고
    • Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution
    • Kille, S., Zilly, F. E., Acevedo, J. P., and Reetz, M. T. (2011) Regio- and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution Nat. Chem 3, 738-743
    • (2011) Nat. Chem , vol.3 , pp. 738-743
    • Kille, S.1    Zilly, F.E.2    Acevedo, J.P.3    Reetz, M.T.4
  • 46
    • 84855716024 scopus 로고    scopus 로고
    • When second best is good enough: Another probabilistic look at saturation mutagenesis
    • Nov, Y. (2012) When second best is good enough: another probabilistic look at saturation mutagenesis Appl. Environ. Microbiol. 78, 258-262
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 258-262
    • Nov, Y.1
  • 47
    • 0022422660 scopus 로고
    • Nomenclature for incompletely specified bases in nucleic-acid sequences - Recommendations 1984
    • Cornishbowden, A. (1985) Nomenclature for incompletely specified bases in nucleic-acid sequences-Recommendations 1984 Nucleic Acids Res. 13, 3021-3030
    • (1985) Nucleic Acids Res. , vol.13 , pp. 3021-3030
    • Cornishbowden, A.1
  • 48
    • 73349113954 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective enoate-reductase: Testing the utility of iterative saturation mutagenesis
    • Bougioukou, D. J., Kille, S., Taglieber, A., and Reetz, M. T. (2009) Directed evolution of an enantioselective enoate-reductase: Testing the utility of iterative saturation mutagenesis Adv. Synth. Catal. 351, 3287-3305
    • (2009) Adv. Synth. Catal. , vol.351 , pp. 3287-3305
    • Bougioukou, D.J.1    Kille, S.2    Taglieber, A.3    Reetz, M.T.4
  • 49
    • 0036841628 scopus 로고    scopus 로고
    • Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit
    • 1162, 1164-1165 - 1160
    • Hogrefe, H. H., Cline, J., Youngblood, G. L., and Allen, R. M. (2002) Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit BioTechniques 33, 1158-1160, 1162, 1164-1165
    • (2002) BioTechniques , vol.33 , pp. 1158
    • Hogrefe, H.H.1    Cline, J.2    Youngblood, G.L.3    Allen, R.M.4
  • 50
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G. and Sommer, S. S. (1990) The "megaprimer" method of site-directed mutagenesis BioTechniques 8, 404-407
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 51
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain-reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain-reaction Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 52
    • 84863280525 scopus 로고    scopus 로고
    • Construction of "small-intelligent" focused mutagenesis libraries using well-designed combinatorial degenerate primers
    • Tang, L., Gao, H., Zhu, X., Wang, X., Zhou, M., and Jiang, R. (2012) Construction of "small-intelligent" focused mutagenesis libraries using well-designed combinatorial degenerate primers BioTechniques 52, 149-158
    • (2012) BioTechniques , vol.52 , pp. 149-158
    • Tang, L.1    Gao, H.2    Zhu, X.3    Wang, X.4    Zhou, M.5    Jiang, R.6
  • 53
    • 18044397860 scopus 로고    scopus 로고
    • Mathematical expressions useful in the construction, description and evaluation of protein libraries
    • Bosley, A. D. and Ostermeier, M. (2005) Mathematical expressions useful in the construction, description and evaluation of protein libraries Biomol. Eng. 22, 57-61
    • (2005) Biomol. Eng. , vol.22 , pp. 57-61
    • Bosley, A.D.1    Ostermeier, M.2
  • 54
    • 0041765676 scopus 로고    scopus 로고
    • User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries
    • Patrick, W. M., Firth, A. E., and Blackburn, J. M. (2003) User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries Protein Eng. 16, 451-457
    • (2003) Protein Eng. , vol.16 , pp. 451-457
    • Patrick, W.M.1    Firth, A.E.2    Blackburn, J.M.3
  • 58
    • 42349087011 scopus 로고    scopus 로고
    • Systematic exploration of active site mutations on human deoxycytidine kinase substrate specificity
    • Iyidogan, P. and Lutz, S. (2008) Systematic exploration of active site mutations on human deoxycytidine kinase substrate specificity Biochemistry 47, 4711-4720
    • (2008) Biochemistry , vol.47 , pp. 4711-4720
    • Iyidogan, P.1    Lutz, S.2
  • 60
    • 0032518211 scopus 로고    scopus 로고
    • Modified base compositions at degenerate positions of a mutagenic oligonucleotide enhance randomness in site-saturation mutagenesis
    • Airaksinen, A. and Hovi, T. (1998) Modified base compositions at degenerate positions of a mutagenic oligonucleotide enhance randomness in site-saturation mutagenesis Nucleic Acids Res. 26, 576-581
    • (1998) Nucleic Acids Res. , vol.26 , pp. 576-581
    • Airaksinen, A.1    Hovi, T.2
  • 61
    • 0037225001 scopus 로고    scopus 로고
    • Evaluation of PCR amplification bias by terminal restriction fragment length polymorphism analysis of small-subunit rRNA and mcrA genes by using defined template mixtures of methanogenic pure cultures and soil DNA extracts
    • Lueders, T. and Friedrich, M. W. (2003) Evaluation of PCR amplification bias by terminal restriction fragment length polymorphism analysis of small-subunit rRNA and mcrA genes by using defined template mixtures of methanogenic pure cultures and soil DNA extracts Appl. Environ. Microbiol. 69, 320-326
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 320-326
    • Lueders, T.1    Friedrich, M.W.2
  • 63
    • 0034643921 scopus 로고    scopus 로고
    • A new randomization assay reveals unexpected elements of sequence bias in model 'randomized' gene libraries: Implications for biopanning
    • Palfrey, D., Picardo, M., and Hine, A. V. (2000) A new randomization assay reveals unexpected elements of sequence bias in model 'randomized' gene libraries: implications for biopanning Gene 251, 91-99
    • (2000) Gene , vol.251 , pp. 91-99
    • Palfrey, D.1    Picardo, M.2    Hine, A.V.3
  • 64
    • 0023958999 scopus 로고
    • Acinetobacter cyclohexanone monooxygenase - Gene cloning and sequence determination
    • Chen, Y. C. J., Peoples, O. P., and Walsh, C. T. (1988) Acinetobacter cyclohexanone monooxygenase-gene cloning and sequence determination J. Bacteriol. 170, 781-789
    • (1988) J. Bacteriol. , vol.170 , pp. 781-789
    • Chen, Y.C.J.1    Peoples, O.P.2    Walsh, C.T.3


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