메뉴 건너뛰기




Volumn 105, Issue 2, 2010, Pages 374-383

Prediction of protein solubility in Escherichia coli using logistic regression

Author keywords

Discriminant analysis; Escherichia coli; Inclusion bodies; Logistic regression; Protein solubility

Indexed keywords

ACCURATE PREDICTION; CROSS VALIDATION; INCLUSION BODIES; LOGISTIC REGRESSIONS; PREDICTION ACCURACY; PROTEIN DATABASE; PROTEIN SOLUBILITY; STATISTICAL TECHNIQUES;

EID: 74849085755     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22537     Document Type: Article
Times cited : (73)

References (31)
  • 1
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F, Mujacic M. 2004. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22:1399-1408.
    • (2004) Nat Biotechnol , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 2
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley P, Misura KM, Baker D. 2005. Toward high-resolution de novo structure prediction for small proteins. Science 309:1868-1871.
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.2    Baker, D.3
  • 4
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou PY, Fasman GD. 1978. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol 47:45-148.
    • (1978) Adv Enzymol Relat Areas Mol Biol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 5
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • Davis GD, Elisee C, Newham DM, Harrison RG. 1999. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol Bioeng 65:382-388.
    • (1999) Biotechnol Bioeng , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 6
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 7
    • 20744445059 scopus 로고    scopus 로고
    • Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroEL
    • Douette P, Navet R, Gerkens P, Galleni M, Levy D, Sluse FE. 2005. Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroEL. Biochem Biophys Res Commun 333:686-693.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 686-693
    • Douette, P.1    Navet, R.2    Gerkens, P.3    Galleni, M.4    Levy, D.5    Sluse, F.E.6
  • 8
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: Identification of protein features that correlate with successful expression
    • Dyson MR, Shadbolt SP, Vincent KJ, Perera RL, McCafferty J. 2004. Production of soluble mammalian proteins in Escherichia coli: Identification of protein features that correlate with successful expression. BMC Biotechnol 4:32-49.
    • (2004) BMC Biotechnol , vol.4 , pp. 32-49
    • Dyson, M.R.1    Shadbolt, S.P.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 9
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp TP, Woods KR. 1981. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 78:3824-3828.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 11
    • 14144255127 scopus 로고    scopus 로고
    • Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli
    • Idicula-Thomas S, Balaji PV. 2005. Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli. Protein Sci 14:582-592.
    • (2005) Protein Sci , vol.14 , pp. 582-592
    • Idicula-Thomas, S.1    Balaji, P.V.2
  • 12
    • 32144443802 scopus 로고    scopus 로고
    • A support vector machine-based method for predicting the propensity of a protein to be soluble or to form inclusion body on overexpression in Escherichia coli
    • Idicula-Thomas S, Kulkarni AJ, Kulkarni BD, Jayaraman VK, Balaji PV. 2006. A support vector machine-based method for predicting the propensity of a protein to be soluble or to form inclusion body on overexpression in Escherichia coli. Bioinformatics 22:278-284.
    • (2006) Bioinformatics , vol.22 , pp. 278-284
    • Idicula-Thomas, S.1    Kulkarni, A.J.2    Kulkarni, B.D.3    Jayaraman, V.K.4    Balaji, P.V.5
  • 13
    • 0031892702 scopus 로고    scopus 로고
    • Three solutions of the protein solubility problem
    • Jenkins WT. 1998. Three solutions of the protein solubility problem. Protein Sci 7:376-382.
    • (1998) Protein Sci , vol.7 , pp. 376-382
    • Jenkins, W.T.1
  • 14
    • 0000812896 scopus 로고    scopus 로고
    • Polymers, biopolymers, and complex systems - Free energy calculations for peptides via deterministic global optimization
    • Klepeis JL, Floudas CA. 1999. Polymers, biopolymers, and complex systems - Free energy calculations for peptides via deterministic global optimization. J Chem Phys 110:7491-7512.
    • (1999) J Chem Phys , vol.110 , pp. 7491-7512
    • Klepeis, J.L.1    Floudas, C.A.2
  • 15
    • 0037305932 scopus 로고    scopus 로고
    • Biophysical theory and modeling - Hybrid global optimization algorithms for protein structure prediction: Alternating hybrids
    • Klepeis JL, Pieja MJ, Floudas CA. 2003. Biophysical theory and modeling - Hybrid global optimization algorithms for protein structure prediction: Alternating hybrids. Biophys J 84:869-882.
    • (2003) Biophys J , vol.84 , pp. 869-882
    • Klepeis, J.L.1    Pieja, M.J.2    Floudas, C.A.3
  • 16
    • 22844445557 scopus 로고    scopus 로고
    • Towards protein folding with evolutionary techniques
    • Koskowski F, Hartke B. 2005. Towards protein folding with evolutionary techniques. J Comput Chem 26:1169-1179.
    • (2005) J Comput Chem , vol.26 , pp. 1169-1179
    • Koskowski, F.1    Hartke, B.2
  • 18
    • 74849124859 scopus 로고    scopus 로고
    • Misbehaving proteins: Protein (mis)folding, aggregation, and stability
    • 353 p
    • Murphy RM, Tsai AM. 2006. Misbehaving proteins: Protein (mis)folding, aggregation, and stability. New York: Springer, viii, 353 p.
    • (2006) New York: Springer, viii
    • Murphy, R.M.1    Tsai, A.M.2
  • 19
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CN, Scholtz JM. 1998. A helix propensity scale based on experimental studies of peptides and proteins. Biophys J 75:422-427.
    • (1998) Biophys J , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 20
    • 0028057034 scopus 로고
    • Secondary structure characterization of beta-lactamase inclusion bodies
    • Przybycien TM, Dunn JP, Valax P, Georgiou G. 1994. Secondary structure characterization of beta-lactamase inclusion bodies. Protein Eng 7:131-136.
    • (1994) Protein Eng , vol.7 , pp. 131-136
    • Przybycien, T.M.1    Dunn, J.P.2    Valax, P.3    Georgiou, G.4
  • 21
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • Schein CH, Noteborn MHM. 1988. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Biotechnology (NY) 6:291-294.
    • (1988) Biotechnology (NY) , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 22
    • 0029889474 scopus 로고    scopus 로고
    • Recent developments in the theory of protein folding: Searching for the global energy minimum
    • Scheraga HA. 1996. Recent developments in the theory of protein folding: Searching for the global energy minimum. Biophys Chem 59:329-339.
    • (1996) Biophys Chem , vol.59 , pp. 329-339
    • Scheraga, H.A.1
  • 23
    • 0035055990 scopus 로고    scopus 로고
    • Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues
    • Schwartz R, Istrail S, King J. 2001. Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues. Protein Sci 10:1023-1031.
    • (2001) Protein Sci , vol.10 , pp. 1023-1031
    • Schwartz, R.1    Istrail, S.2    King, J.3
  • 24
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh SM, Panda AK. 2005. Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng 99:303-310.
    • (2005) J Biosci Bioeng , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 25
    • 0033529861 scopus 로고    scopus 로고
    • Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone
    • Street AG, Mayo SL. 1999. Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone. Proc Natl Acad Sci USA 96:9074-9076.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9074-9076
    • Street, A.G.1    Mayo, S.L.2
  • 26
    • 35648986678 scopus 로고    scopus 로고
    • The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein
    • Thaker YR, Roessle M, Gruber G. 2007. The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein. J Bioenerg Biomembr 39:275-289.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 275-289
    • Thaker, Y.R.1    Roessle, M.2    Gruber, G.3
  • 28
    • 33344476459 scopus 로고    scopus 로고
    • Kinetics of amyloid aggregation of mammal apomyoglobins and correlation with their amino acid sequences
    • Vilasi S, Dosi R, Iannuzzi C, Malmo C, Parente A, Irace G, Sirangelo I. 2006. Kinetics of amyloid aggregation of mammal apomyoglobins and correlation with their amino acid sequences. FEBS Lett 580:1681-1684.
    • (2006) FEBS Lett , vol.580 , pp. 1681-1684
    • Vilasi, S.1    Dosi, R.2    Iannuzzi, C.3    Malmo, C.4    Parente, A.5    Irace, G.6    Sirangelo, I.7
  • 29
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones - Cellular machines for protein folding
    • Walter S, Buchner J. 2002. Molecular chaperones - Cellular machines for protein folding. Angew Chem Int Ed Engl 41:1098-1113.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 1098-1113
    • Walter, S.1    Buchner, J.2
  • 30
    • 0025953577 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • Wilkinson DL, Harrison RG. 1991. Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology (NY) 9:443-448.
    • (1991) Biotechnology (NY) , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 31
    • 0020036666 scopus 로고
    • Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins
    • Williams DC, Van Frank RM, Muth WL, Burnett JP. 1982. Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins. Science 215:687-689.
    • (1982) Science , vol.215 , pp. 687-689
    • Williams, D.C.1    Van Frank, R.M.2    Muth, W.L.3    Burnett, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.