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Volumn 363, Issue 2, 2006, Pages 545-557

In Vitro Evolution of a Hyperstable Gβ1 Variant

Author keywords

computational protein design; error prone PCR; in vitro selection; phage display; protein stability

Indexed keywords

PROTEIN G;

EID: 33748942644     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.034     Document Type: Article
Times cited : (16)

References (61)
  • 4
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • Korkegian A., Black M.E., Baker D., and Stoddard B.L. Computational thermostabilization of an enzyme. Science 308 (2005) 857-860
    • (2005) Science , vol.308 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 6
    • 1342324030 scopus 로고    scopus 로고
    • Exploring folding free energy landscapes using computational protein design
    • Kuhlman B., and Baker D. Exploring folding free energy landscapes using computational protein design. Curr. Opin. Struct. Biol. 14 (2004) 89-95
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 89-95
    • Kuhlman, B.1    Baker, D.2
  • 7
    • 1842839788 scopus 로고    scopus 로고
    • Simulating protein evolution in sequence and structure space
    • Xia Y., and Levitt M. Simulating protein evolution in sequence and structure space. Curr. Opin. Struct. Biol. 14 (2004) 202-207
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 202-207
    • Xia, Y.1    Levitt, M.2
  • 8
    • 23044447796 scopus 로고    scopus 로고
    • New genotype-phenotype linkages for directed evolution of functional proteins
    • Leemhuis H., Stein V., Griffiths A.D., and Hollfelder F. New genotype-phenotype linkages for directed evolution of functional proteins. Curr. Opin. Struct. Biol. 15 (2005) 472-478
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 472-478
    • Leemhuis, H.1    Stein, V.2    Griffiths, A.D.3    Hollfelder, F.4
  • 9
    • 13844281394 scopus 로고    scopus 로고
    • Directed evolution of proteins for heterologous expression and stability
    • Roodveldt C., Aharoni A., and Tawfik D.S. Directed evolution of proteins for heterologous expression and stability. Curr. Opin. Struct. Biol. 15 (2005) 50-56
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 50-56
    • Roodveldt, C.1    Aharoni, A.2    Tawfik, D.S.3
  • 11
    • 0035424963 scopus 로고    scopus 로고
    • In vitro display technologies: novel developments and applications
    • Amstutz P., Forrer P., Zahnd C., and Plückthun A. In vitro display technologies: novel developments and applications. Curr. Opin. Biotechnol. 12 (2001) 400-405
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 400-405
    • Amstutz, P.1    Forrer, P.2    Zahnd, C.3    Plückthun, A.4
  • 12
    • 0033779402 scopus 로고    scopus 로고
    • Temperature adaptation of enzymes: lessons from laboratory evolution
    • Wintrode P.L., and Arnold F.H. Temperature adaptation of enzymes: lessons from laboratory evolution. Adv. Protein Chem. 55 (2000) 161-225
    • (2000) Adv. Protein Chem. , vol.55 , pp. 161-225
    • Wintrode, P.L.1    Arnold, F.H.2
  • 13
    • 25444463283 scopus 로고    scopus 로고
    • Structural perturbation and compensation by directed evolution at physiological temperature leads to thermostabilization of beta-lactamase
    • Hecky J., and Müller K.M. Structural perturbation and compensation by directed evolution at physiological temperature leads to thermostabilization of beta-lactamase. Biochemistry 44 (2005) 12640-12654
    • (2005) Biochemistry , vol.44 , pp. 12640-12654
    • Hecky, J.1    Müller, K.M.2
  • 15
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom H.R. Selecting and screening recombinant antibody libraries. Nature Biotechnol. 23 (2005) 1105-1116
    • (2005) Nature Biotechnol. , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 17
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber V., Plückthun A., and Schmid F.X. Selecting proteins with improved stability by a phage-based method. Nature Biotechnol. 16 (1998) 955-960
    • (1998) Nature Biotechnol. , vol.16 , pp. 955-960
    • Sieber, V.1    Plückthun, A.2    Schmid, F.X.3
  • 18
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • Kristensen P., and Winter G. Proteolytic selection for protein folding using filamentous bacteriophages. Fold. Des. 3 (1998) 321-328
    • (1998) Fold. Des. , vol.3 , pp. 321-328
    • Kristensen, P.1    Winter, G.2
  • 19
    • 0033533503 scopus 로고    scopus 로고
    • Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries
    • Finucane M.D., Tuna M., Lees J.H., and Woolfson D.N. Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries. Biochemistry 38 (1999) 11604-11612
    • (1999) Biochemistry , vol.38 , pp. 11604-11612
    • Finucane, M.D.1    Tuna, M.2    Lees, J.H.3    Woolfson, D.N.4
  • 20
    • 0035827175 scopus 로고    scopus 로고
    • In vitro selection of highly stabilized protein variants with optimized surface
    • Martin A., Sieber V., and Schmid F.X. In vitro selection of highly stabilized protein variants with optimized surface. J. Mol. Biol. 309 (2001) 717-726
    • (2001) J. Mol. Biol. , vol.309 , pp. 717-726
    • Martin, A.1    Sieber, V.2    Schmid, F.X.3
  • 21
    • 0037427448 scopus 로고    scopus 로고
    • Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins
    • Martin A., and Schmid F.X. Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins. J. Mol. Biol. 328 (2003) 863-875
    • (2003) J. Mol. Biol. , vol.328 , pp. 863-875
    • Martin, A.1    Schmid, F.X.2
  • 22
    • 0141888974 scopus 로고    scopus 로고
    • Proside: a phage-based method for selecting thermostable proteins
    • Martin A., Schmid F.X., and Sieber V. Proside: a phage-based method for selecting thermostable proteins. Methods Mol. Biol. 230 (2003) 57-70
    • (2003) Methods Mol. Biol. , vol.230 , pp. 57-70
    • Martin, A.1    Schmid, F.X.2    Sieber, V.3
  • 23
    • 2342528494 scopus 로고    scopus 로고
    • Selection of stably folded proteins by phage-display with proteolysis
    • Bai Y., and Feng H. Selection of stably folded proteins by phage-display with proteolysis. Eur. J. Biochem. 271 (2004) 1609-1614
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1609-1614
    • Bai, Y.1    Feng, H.2
  • 24
    • 15244350748 scopus 로고    scopus 로고
    • Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions
    • Wunderlich M., Martin A., and Schmid F.X. Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. J. Mol. Biol. 347 (2005) 1063-1076
    • (2005) J. Mol. Biol. , vol.347 , pp. 1063-1076
    • Wunderlich, M.1    Martin, A.2    Schmid, F.X.3
  • 25
    • 23644443403 scopus 로고    scopus 로고
    • Evolutionary protein stabilization in comparison with computational design
    • Wunderlich M., Martin A., Staab C.A., and Schmid F.X. Evolutionary protein stabilization in comparison with computational design. J. Mol. Biol. 351 (2005) 1160-1168
    • (2005) J. Mol. Biol. , vol.351 , pp. 1160-1168
    • Wunderlich, M.1    Martin, A.2    Staab, C.A.3    Schmid, F.X.4
  • 26
    • 27744457705 scopus 로고    scopus 로고
    • A stable disulfide-free gene-3-protein of phage fd generated by in vitro evolution
    • Kather I., Bippes C.A., and Schmid F.X. A stable disulfide-free gene-3-protein of phage fd generated by in vitro evolution. J. Mol. Biol. 354 (2005) 666-678
    • (2005) J. Mol. Biol. , vol.354 , pp. 666-678
    • Kather, I.1    Bippes, C.A.2    Schmid, F.X.3
  • 27
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites
    • Stengele I., Bross P., Garces X., Giray J., and Rasched I. Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites. J. Mol. Biol. 212 (1990) 143-149
    • (1990) J. Mol. Biol. , vol.212 , pp. 143-149
    • Stengele, I.1    Bross, P.2    Garces, X.3    Giray, J.4    Rasched, I.5
  • 29
    • 0027421911 scopus 로고
    • Identification of the contact surface of a streptococcal protein G domain complexed with a human Fc fragment
    • Gronenborn A.M., and Clore G.M. Identification of the contact surface of a streptococcal protein G domain complexed with a human Fc fragment. J. Mol. Biol. 233 (1993) 331-335
    • (1993) J. Mol. Biol. , vol.233 , pp. 331-335
    • Gronenborn, A.M.1    Clore, G.M.2
  • 30
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher T., Alexander P., Bryan P., and Gilliland G.L. Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33 (1994) 4721-4729
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 31
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malakauskas S.M., and Mayo S.L. Design, structure and stability of a hyperthermophilic protein variant. Nature Struct. Biol. 5 (1998) 470-475
    • (1998) Nature Struct. Biol. , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 32
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: fully automated sequence selection
    • Dahiyat B.I., and Mayo S.L. De novo protein design: fully automated sequence selection. Science 278 (1997) 82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 33
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat B.I., and Mayo S.L. Probing the role of packing specificity in protein design. Proc. Natl Acad. Sci. USA 94 (1997) 10172-10177
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 34
    • 23644443403 scopus 로고    scopus 로고
    • Evolutionary protein stabilization in comparison with computational design
    • Wunderlich M., Martin A., Staab C.A., and Schmid F.X. Evolutionary protein stabilization in comparison with computational design. J. Mol. Biol. 351 (2005) 1160-1168
    • (2005) J. Mol. Biol. , vol.351 , pp. 1160-1168
    • Wunderlich, M.1    Martin, A.2    Staab, C.A.3    Schmid, F.X.4
  • 35
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat B.I., and Mayo S.L. Probing the role of packing specificity in protein design. Proc. Natl Acad. Sci. USA 94 (1997) 10172-10177
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 36
    • 0028792105 scopus 로고
    • Guidelines for protein design: the energetics of beta sheet side chain interactions
    • Smith C.K., and Regan L. Guidelines for protein design: the energetics of beta sheet side chain interactions. Science 270 (1995) 980-982
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 37
    • 0033571653 scopus 로고    scopus 로고
    • Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings
    • Merkel J.S., Sturtevant J.M., and Regan L. Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings. Structure 7 (1999) 1333-1343
    • (1999) Structure , vol.7 , pp. 1333-1343
    • Merkel, J.S.1    Sturtevant, J.M.2    Regan, L.3
  • 38
    • 0028175780 scopus 로고
    • A thermodynamic scale for the beta-sheet forming tendencies of the amino acids
    • Smith C.K., Withka J.M., and Regan L. A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. Biochemistry 33 (1994) 5510-5517
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 39
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures
    • Alexander P., Fahnestock S., Lee T., Orban J., and Bryan P. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures. Biochemistry 31 (1992) 3597-3603
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 40
    • 20544449855 scopus 로고    scopus 로고
    • Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins
    • Drummond D.A., Iverson B.L., Georgiou G., and Arnold F.H. Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. J. Mol. Biol. 350 (2005) 806-816
    • (2005) J. Mol. Biol. , vol.350 , pp. 806-816
    • Drummond, D.A.1    Iverson, B.L.2    Georgiou, G.3    Arnold, F.H.4
  • 41
    • 23944462537 scopus 로고    scopus 로고
    • Statistics of protein library construction
    • Firth A.E., and Patrick W.M. Statistics of protein library construction. Bioinformatics 21 (2005) 3314-3315
    • (2005) Bioinformatics , vol.21 , pp. 3314-3315
    • Firth, A.E.1    Patrick, W.M.2
  • 42
    • 29144503012 scopus 로고    scopus 로고
    • A statistical analysis of random mutagenesis methods used for directed protein evolution
    • Wong T.S., Roccatano D., Zacharias M., and Schwaneberg U. A statistical analysis of random mutagenesis methods used for directed protein evolution. J. Mol. Biol. 355 (2006) 858-871
    • (2006) J. Mol. Biol. , vol.355 , pp. 858-871
    • Wong, T.S.1    Roccatano, D.2    Zacharias, M.3    Schwaneberg, U.4
  • 43
    • 25144470141 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins
    • Cho J.H., and Raleigh D.P. Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J. Mol. Biol. 353 (2005) 174-185
    • (2005) J. Mol. Biol. , vol.353 , pp. 174-185
    • Cho, J.H.1    Raleigh, D.P.2
  • 44
    • 0033852796 scopus 로고    scopus 로고
    • Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    • Pace C.N., Alston R.W., and Shaw K.L. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci. 9 (2000) 1395-1398
    • (2000) Protein Sci. , vol.9 , pp. 1395-1398
    • Pace, C.N.1    Alston, R.W.2    Shaw, K.L.3
  • 45
    • 0001117058 scopus 로고    scopus 로고
    • Construction and design of beta-sheets
    • Smith C.K., and Regan L. Construction and design of beta-sheets. Acc. Chem. Res. 30 (1997) 153-161
    • (1997) Acc. Chem. Res. , vol.30 , pp. 153-161
    • Smith, C.K.1    Regan, L.2
  • 46
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of beta-hairpin formation in protein G folding
    • McCallister E.L., Alm E., and Baker D. Critical role of beta-hairpin formation in protein G folding. Nature Struct. Biol. 7 (2000) 669-673
    • (2000) Nature Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 47
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: fully automated sequence selection
    • Dahiyat B.I., and Mayo S.L. De novo protein design: fully automated sequence selection. Science 278 (1997) 82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 48
    • 14144256681 scopus 로고    scopus 로고
    • Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity
    • Pokala N., and Handel T.M. Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity. J. Mol. Biol. 347 (2005) 203-227
    • (2005) J. Mol. Biol. , vol.347 , pp. 203-227
    • Pokala, N.1    Handel, T.M.2
  • 49
    • 0033533387 scopus 로고    scopus 로고
    • Core-directed protein design. II. Rescue of a multiply mutated and destabilized variant of ubiquitin
    • Finucane M.D., and Woolfson D.N. Core-directed protein design. II. Rescue of a multiply mutated and destabilized variant of ubiquitin. Biochemistry 38 (1999) 11613-11623
    • (1999) Biochemistry , vol.38 , pp. 11613-11623
    • Finucane, M.D.1    Woolfson, D.N.2
  • 51
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu J., Baase W.A., Baldwin E., and Matthews B.W. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7 (1998) 158-177
    • (1998) Protein Sci. , vol.7 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 52
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger C.D., Schildbach J.F., and Sauer R.T. Are buried salt bridges important for protein stability and conformational specificity?. Nature Struct. Biol. 2 (1995) 122-128
    • (1995) Nature Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 53
    • 0036310988 scopus 로고    scopus 로고
    • Origins of the high stability of an in vitro-selected cold-shock protein
    • Martin A., Kather I., and Schmid F.X. Origins of the high stability of an in vitro-selected cold-shock protein. J. Mol. Biol. 318 (2002) 1341-1349
    • (2002) J. Mol. Biol. , vol.318 , pp. 1341-1349
    • Martin, A.1    Kather, I.2    Schmid, F.X.3
  • 55
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz M., and Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature 255 (1975) 256-259
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.1    Raidt, H.2
  • 56
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R., and Böhm G. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8 (1998) 738-748
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 57
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads
    • Karshikoff A., and Ladenstein R. Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem. Sci. 26 (2001) 550-556
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 58
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D., Mueller U., Heinemann U., and Schmid F.X. Two exposed amino acid residues confer thermostability on a cold shock protein. Nature Struct. Biol. 7 (2000) 380-383
    • (2000) Nature Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 60
    • 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., and Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27 (1988) 8063-8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 61
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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