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Volumn 32, Issue 2, 2015, Pages 440-455

Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history

Author keywords

amino acid replacements; ancestral proteins; molecular evolution

Indexed keywords

LEUCINE; LYSINE; METHIONINE; PENICILLINASE; THIOREDOXIN; THREONINE; AMINO ACID;

EID: 84988239865     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/msu312     Document Type: Article
Times cited : (69)

References (72)
  • 2
    • 84891364264 scopus 로고    scopus 로고
    • Mutational effects on stability are largely conserved during protein evolution
    • Ashenberg O, Gong LI, Bloom JD. 2013. Mutational effects on stability are largely conserved during protein evolution. Proc Natl Acad Sci USA. 110(52):21071-21076
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.52 , pp. 21071-21076
    • Ashenberg, O.1    Gong, L.I.2    Bloom, J.D.3
  • 4
    • 84882392687 scopus 로고    scopus 로고
    • The evolutionary origins of detoxifying enzymes the mammalian serum paraoxonases (pons) relate to bacterial homoserine lactonases
    • Bar-Rogovsky H, Hugenmatter A, Tawfik DS. 2013. The evolutionary origins of detoxifying enzymes. The mammalian serum paraoxonases (PONs) relate to bacterial homoserine lactonases. J Biol Chem. 288:23914-23927
    • (2013) J Biol Chem , vol.288 , pp. 23914-23927
    • Bar-Rogovsky, H.1    Hugenmatter, A.2    Tawfik, D.S.3
  • 6
    • 33845864966 scopus 로고    scopus 로고
    • Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein
    • Bershtein S, Segal M, Bekerman R, Tokuriki N, Tawfik DS. 2006. Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein. Nature 444:929-932
    • (2006) Nature , vol.444 , pp. 929-932
    • Bershtein, S.1    Segal, M.2    Bekerman, R.3    Tokuriki, N.4    Tawfik, D.S.5
  • 7
    • 84905001681 scopus 로고    scopus 로고
    • An experimentally determined evolutionary model dramatically improves phylogenetic fit
    • Bloom JD. 2014. An experimentally determined evolutionary model dramatically improves phylogenetic fit. Mol Biol Evol. 31: 1956-1978
    • (2014) Mol Biol Evol , vol.31 , pp. 1956-1978
    • Bloom, J.D.1
  • 8
    • 33846704424 scopus 로고    scopus 로고
    • Breaking proteins with mutations: Threads and thresholds in evolution
    • Bloom JD, Arnold FH, Wilke CO. 2007. Breaking proteins with mutations: threads and thresholds in evolution. Mol Syst Biol. 3:76
    • (2007) Mol Syst Biol , vol.3 , pp. 76
    • Bloom, J.D.1    Arnold, F.H.2    Wilke, C.O.3
  • 11
    • 0015967881 scopus 로고
    • Conformational parameters of amino acids in helical, b-sheet, and random coil regions calculated from proteins
    • Chou PY, Fasman G. 1974. Conformational parameters of amino acids in helical, b-sheet, and random coil regions calculated from proteins. Biochemistry 13:211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.2
  • 12
    • 31544474634 scopus 로고    scopus 로고
    • Long-term survival during stationary phase: Evolution and the GASP phenotype
    • Finkel SE. 2006. Long-term survival during stationary phase: evolution and the GASP phenotype. Nat Rev Microbiol. 4:113-120
    • (2006) Nat Rev Microbiol , vol.4 , pp. 113-120
    • Finkel, S.E.1
  • 14
    • 38949093003 scopus 로고    scopus 로고
    • Palaeotemperature trend for Precambrian life inferred from resurrected proteins
    • Gaucher EA, Govindarajan S, Ganesh OK. 2008. Palaeotemperature trend for Precambrian life inferred from resurrected proteins. Nature 451:704-707
    • (2008) Nature , vol.451 , pp. 704-707
    • Gaucher, E.A.1    Govindarajan, S.2    Ganesh, O.K.3
  • 15
    • 33748454832 scopus 로고    scopus 로고
    • Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments
    • Godoy-Ruiz R, Ariza F, Rodriguez-Larrea D, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM. 2006. Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. J Mol Biol. 362:966-978
    • (2006) J Mol Biol , vol.362 , pp. 966-978
    • Godoy-Ruiz, R.1    Ariza, F.2    Rodriguez-Larrea, D.3    Perez-Jimenez, R.4    Ibarra-Molero, B.5    Sanchez-Ruiz, J.M.6
  • 16
    • 0742289618 scopus 로고    scopus 로고
    • Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations
    • Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM. 2004. Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations. J Mol Biol. 336: 313-318
    • (2004) J Mol Biol , vol.336 , pp. 313-318
    • Godoy-Ruiz, R.1    Perez-Jimenez, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 17
    • 27744443713 scopus 로고    scopus 로고
    • A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization
    • Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM. 2005. A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization. Biophys J. 89:3320-3331
    • (2005) Biophys J. , vol.89 , pp. 3320-3331
    • Godoy-Ruiz, R.1    Perez-Jimenez, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 18
    • 84874797243 scopus 로고    scopus 로고
    • Hydrophobic environment is a key factor for the stability of thermophilic proteins
    • Gromiha MM, Pathak MC, Saraboji K, Ortlund EA, Gaucher EA. 2013. Hydrophobic environment is a key factor for the stability of thermophilic proteins. Proteins 81:715-721
    • (2013) Proteins , vol.81 , pp. 715-721
    • Gromiha, M.M.1    Pathak, M.C.2    Saraboji, K.3    Ortlund, E.A.4    Gaucher, E.A.5
  • 19
    • 0031875569 scopus 로고    scopus 로고
    • Evolutionary distances for protein-coding sequences: Modeling site-specific residue frequencies
    • Halpern AL, Bruno WJ. 1998. Evolutionary distances for protein-coding sequences: modeling site-specific residue frequencies. Mol Biol Evol. 15:910-917
    • (1998) Mol Biol Evol , vol.15 , pp. 910-917
    • Halpern, A.L.1    Bruno, W.J.2
  • 20
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: The capping box
    • Harper ET, Rose GD. 1993. Helix stop signals in proteins and peptides: the capping box. Biochemistry 32:7605-7669
    • (1993) Biochemistry , vol.32 , pp. 7605-7669
    • Harper, E.T.1    Rose, G.D.2
  • 22
    • 0022376431 scopus 로고
    • Phage lambda repressor revertants. Amino acid mutations that restore activity to mutant proteins
    • Hetch MH, Sauer RT. 1985. Phage lambda repressor revertants. Amino acid mutations that restore activity to mutant proteins. J Mol Biol. 186:53-63
    • (1985) J Mol Biol , vol.186 , pp. 53-63
    • Hetch, M.H.1    Sauer, R.T.2
  • 25
  • 26
    • 0030788941 scopus 로고    scopus 로고
    • A natural polymorphism in beta-lactamase is a global suppressor
    • Huang W, Palzkill T. 1997. A natural polymorphism in beta-lactamase is a global suppressor. Proc Natl Acad Sci USA. 94(16):8801-8806
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.16 , pp. 8801-8806
    • Huang, W.1    Palzkill, T.2
  • 29
    • 52049112316 scopus 로고    scopus 로고
    • Increased folding stability of TEM-1 b-lactamase by in vitro selection
    • Kather I, Jakob RP, Dobbek H, Schmid FX. 2008. Increased folding stability of TEM-1 b-lactamase by in vitro selection. J Mol Biol. 383:238-251
    • (2008) J Mol Biol , vol.383 , pp. 238-251
    • Kather, I.1    Jakob, R.P.2    Dobbek, H.3    Schmid, F.X.4
  • 30
    • 0027411181 scopus 로고
    • Thermodynamic b-sheet propensities measured using a zinc-finger host peptide
    • Kim CA, Berg JM. 1993. Thermodynamic b-sheet propensities measured using a zinc-finger host peptide. Nature 362:267-270
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 32
    • 0038322915 scopus 로고    scopus 로고
    • High archean climatic temperature inferred from oxygen isotope geochemistry of cherts in the 3.5 ga swaziland supergroup, south africa
    • Knauth LP, Lowe DR. 2003. High Archean climatic temperature inferred from oxygen isotope geochemistry of cherts in the 3.5 Ga Swaziland Supergroup, South Africa. Geol Soc Am Bull. 115:566-580
    • (2003) Geol Soc Am Bull , vol.115 , pp. 566-580
    • Knauth, L.P.1    Lowe, D.R.2
  • 34
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
    • Kumar JK, Tabor S, Richardson CC. 2004. Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proc Natl Acad Sci USA. 101:3759-3764
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 35
    • 84871587989 scopus 로고    scopus 로고
    • The origin of membrane bioenergetics
    • Lane N, Martin WF. 2013. The origin of membrane bioenergetics. Cell 151:1406-1416
    • (2013) Cell , vol.151 , pp. 1406-1416
    • Lane, N.1    Martin, W.F.2
  • 36
    • 2442691520 scopus 로고    scopus 로고
    • A Bayesian mixture model for across-site heterogeneities in the amino acid replacement process
    • Lartillot N, Philippe H. 2004. A Bayesian mixture model for across-site heterogeneities in the amino acid replacement process. Mol Biol Evol. 21:1095-1109
    • (2004) Mol Biol Evol , vol.21 , pp. 1095-1109
    • Lartillot, N.1    Philippe, H.2
  • 38
    • 0024507791 scopus 로고
    • Alternative packing arrangements in the hydrophobic core of lambda repressor
    • Lim WA, Sauer RT. 1989. Alternative packing arrangements in the hydrophobic core of lambda repressor. Nature 339:31-36
    • (1989) Nature , vol.339 , pp. 31-36
    • Lim, W.A.1    Sauer, R.T.2
  • 39
    • 0025850262 scopus 로고
    • Global suppression of protein foding defects and inclusion body formation
    • Mitraki A, Fane B, Haase-Penttingel C, Sturtevant J, King J. 1991. Global suppression of protein foding defects and inclusion body formation. Science 253:54-58
    • (1991) Science , vol.253 , pp. 54-58
    • Mitraki, A.1    Fane, B.2    Haase-Penttingel, C.3    Sturtevant, J.4    King, J.5
  • 40
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in peptides and proteins
    • Myers JK, Pace CN, Scholtz JM. 1997. A direct comparison of helix propensity in peptides and proteins. Proc Natl Acad Sci USA. 94: 2833-2837
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 41
    • 0034141471 scopus 로고    scopus 로고
    • Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations
    • Nikolova PV, Wong KB, DeDecker B, Henckel J, Fersht AR. 2000. Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. EMBO J. 19:370-378
    • (2000) Embo J. , vol.19 , pp. 370-378
    • Nikolova, P.V.1    Wong, K.B.2    Dedecker, B.3    Henckel, J.4    Fersht, A.R.5
  • 44
    • 34548040966 scopus 로고    scopus 로고
    • Crystal structure of an ancient protein: Evolution by conformational epistasis
    • Ortlund EA, Bridgham JT, Redinbo MR, Thornton JW. 2007. Crystal structure of an ancient protein: evolution by conformational epistasis. Science 317:1544-1548
    • (2007) Science , vol.317 , pp. 1544-1548
    • Ortlund, E.A.1    Bridgham, J.T.2    Redinbo, M.R.3    Thornton, J.W.4
  • 45
    • 0031808074 scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CM, Scholtz JM. 1988. A helix propensity scale based on experimental studies of peptides and proteins. Biophys J. 75:422-427
    • (1988) Biophys J. , vol.75 , pp. 422-427
    • Pace, C.M.1    Scholtz, J.M.2
  • 46
    • 0002725360 scopus 로고
    • Chemical paleogenetics: Molecular restoration studies of extinct forms of life
    • Pauling L, Zuckerkandl E. 1963. Chemical paleogenetics: molecular restoration studies of extinct forms of life. Acta Chem Scan. 17: S9-S16
    • (1963) Acta Chem Scan , vol.17 , pp. S9-S16
    • Pauling, L.1    Zuckerkandl, E.2
  • 49
    • 84898811791 scopus 로고    scopus 로고
    • Strong evidence for protein epistasis, weak evidence against it
    • Pollock DD, Goldstein RA. 2014. Strong evidence for protein epistasis, weak evidence against it. Proc Natl Acad Sci USA. 111(15):E1450
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.15 , pp. E1450
    • Pollock, D.D.1    Goldstein, R.A.2
  • 50
    • 84861422981 scopus 로고    scopus 로고
    • Amino acid coevolution induces an evolutionary Stokes shift
    • Pollock DD, Thiltgen G, Goldstein RA. 2012. Amino acid coevolution induces an evolutionary Stokes shift. Proc Natl Acad Sci USA. 109(21):E1352-E1359
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.21 , pp. E1352-E1359
    • Pollock, D.D.1    Thiltgen, G.2    Goldstein, R.A.3
  • 51
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of helices
    • Richardson JS, Richardson DC. 1988. Amino acid preferences for specific locations at the ends of helices. Science 240:1648-1652
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 52
    • 84900832991 scopus 로고    scopus 로고
    • Phenotypic comparisons of consensus variants versus laboratory resurrections of precambrian proteins
    • Risso VA, Gavira JA, Gaucher EA, Sanchez-Ruiz JM. 2014. Phenotypic comparisons of consensus variants versus laboratory resurrections of Precambrian proteins. Proteins 82:887-896
    • (2014) Proteins , vol.82 , pp. 887-896
    • Risso, V.A.1    Gavira, J.A.2    Gaucher, E.A.3    Sanchez-Ruiz, J.M.4
  • 53
    • 84874602326 scopus 로고    scopus 로고
    • Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian b-lactamases
    • Risso VA, Gavira JA, Mejia-Carmona DF, Gaucher EA, Sanchez-Ruiz JM. 2013. Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian b-lactamases. J Am Chem Soc. 135: 2899-2902
    • (2013) J Am Chem Soc , vol.135 , pp. 2899-2902
    • Risso, V.A.1    Gavira, J.A.2    Mejia-Carmona, D.F.3    Gaucher, E.A.4    Sanchez-Ruiz, J.M.5
  • 55
    • 77949536563 scopus 로고    scopus 로고
    • Mutation-selection models of coding sequence evolution with site-heterogeneous amino acid fitness profiles
    • Rodrigue N, Philippe H, Lartillot N. 2010. Mutation-selection models of coding sequence evolution with site-heterogeneous amino acid fitness profiles. Proc Natl Acad Sci USA. 107(10):4629-4634
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.10 , pp. 4629-4634
    • Rodrigue, N.1    Philippe, H.2    Lartillot, N.3
  • 56
    • 78649360645 scopus 로고    scopus 로고
    • Natural evolution of TEM-1 b-lactamase: Experimental reconstruction and clinical relevance
    • Salverda ML, De Visser JA, Barlow M. 2010. Natural evolution of TEM-1 b-lactamase: experimental reconstruction and clinical relevance. FEMS Microbiol Rev. 34:1015-1036
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 1015-1036
    • Salverda, M.L.1    De Visser, J.A.2    Barlow, M.3
  • 57
    • 0023068366 scopus 로고
    • The thermodynamic stability of proteins
    • Schellman JA. 1987. The thermodynamic stability of proteins. Annu Rev Biophys Biophys Chem. 16:115-137
    • (1987) Annu Rev Biophys Biophys Chem , vol.16 , pp. 115-137
    • Schellman, J.A.1
  • 58
    • 0027441807 scopus 로고
    • Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability
    • Serrano L, Day AG, Fersht AR. 1993. Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J Mol Biol. 233:305-312
    • (1993) J Mol Biol , vol.233 , pp. 305-312
    • Serrano, L.1    Day, A.G.2    Fersht, A.R.3
  • 59
    • 0021968408 scopus 로고
    • Genetic analysis of staphylococcal nuclease: Identification of three intragenic global suppressors of nuclease-minus mutations
    • Shortle D, Lin B. 1985. Genetic analysis of staphylococcal nuclease: identification of three intragenic global suppressors of nuclease-minus mutations. Genetics 110:539-555
    • (1985) Genetics , vol.110 , pp. 539-555
    • Shortle, D.1    Lin, B.2
  • 60
    • 84908154345 scopus 로고    scopus 로고
    • Biophysics of protein evolution and evolutionary protein biophysics
    • Sikosek T, Chan HS. 2014. Biophysics of protein evolution and evolutionary protein biophysics. J R Soc Interface. 11:20140419
    • (2014) J R Soc Interface , vol.11 , pp. 20140419
    • Sikosek, T.1    Chan, H.S.2
  • 61
    • 0028175780 scopus 로고
    • A thermodynamic scale for the b-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L. 1994. A thermodynamic scale for the b-sheet forming tendencies of the amino acids. Biochemistry 33: 5510-5517
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 62
    • 0014935646 scopus 로고
    • Natural selection and the concept of a protein space
    • Smith JM. 1970. Natural selection and the concept of a protein space. Nature 225:563-564
    • (1970) Nature , vol.225 , pp. 563-564
    • Smith, J.M.1
  • 63
    • 84858184390 scopus 로고    scopus 로고
    • Estimating the distribution of selection coefficients from phylogenetic data using sitewise mutation-selection models
    • Tamuri AU, dos Reis M, Goldstein RA. 2012. Estimating the distribution of selection coefficients from phylogenetic data using sitewise mutation-selection models. Genetics 190:1101-1115
    • (2012) Genetics , vol.190 , pp. 1101-1115
    • Tamuri, A.U.1    Dos Reis, M.2    Goldstein, R.A.3
  • 64
    • 0036139093 scopus 로고    scopus 로고
    • Why are proteins marginally stable?
    • Taverna DR, Goldstein RA. 2002. Why are proteins marginally stable?. Proteins 46:105-109
    • (2002) Proteins , vol.46 , pp. 105-109
    • Taverna, D.R.1    Goldstein, R.A.2
  • 65
    • 34248674895 scopus 로고    scopus 로고
    • The stability effects of protein mutations appear to be universally distributed
    • Tokuriki N, Stricher F, Schymkowitz J, Serrano L, Tawfik DS. 2007. The stability effects of protein mutations appear to be universally distributed. J Mol Biol. 369:1318-1332
    • (2007) J Mol Biol , vol.369 , pp. 1318-1332
    • Tokuriki, N.1    Stricher, F.2    Schymkowitz, J.3    Serrano, L.4    Tawfik, D.S.5
  • 66
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki N, Tawfik DS. 2009. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 459:668-673
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 67
    • 84871697209 scopus 로고    scopus 로고
    • Reconstruction of ancestral metabolic enzymes reveals molecular mechanisms underlying evolutionary innovation through gene duplication
    • Voordeckers K, Brown CA, Vanneste K, van Der Zande E, Voet A, Maere S, Verstrepen KJ. 2012. Reconstruction of ancestral metabolic enzymes reveals molecular mechanisms underlying evolutionary innovation through gene duplication. PLoS Biol. 10:e1001446
    • (2012) Plos Biol , vol.10 , pp. e1001446
    • Voordeckers, K.1    Brown, C.A.2    Vanneste, K.3    Van Der Zande, E.4    Voet, A.5    Maere, S.6    Verstrepen, K.J.7
  • 68
    • 60049091295 scopus 로고    scopus 로고
    • A class frequencymixture model that adjusts for site-specific amino acid frequencies and improves inference of protein phylogeny
    • Wang HC, Li K, Susko E, Roger AJ. 2008. A class frequencymixture model that adjusts for site-specific amino acid frequencies and improves inference of protein phylogeny. BMC Evol Biol. 8:331
    • (2008) BMC Evol Biol , vol.8 , pp. 331
    • Wang, H.C.1    Li, K.2    Susko, E.3    Roger, A.J.4
  • 69
    • 0036295508 scopus 로고    scopus 로고
    • Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs
    • Wang X, Minasov G, Shoichet BK. 2002. Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs. J Mol Biol. 320:85-95
    • (2002) J Mol Biol , vol.320 , pp. 85-95
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 70
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich DM, Delaney NF, DePristo MA, Hartl DL. 2006. Darwinian evolution can follow only very few mutational paths to fitter proteins. Science 312:111-114
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    Depristo, M.A.3    Hartl, D.L.4
  • 71
    • 0026757625 scopus 로고
    • Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme
    • Wilson KP, Malcolm BA, Matthews BA. 1992. Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. J Biol Chem. 267:10842-10849
    • (1992) J Biol Chem , vol.267 , pp. 10842-10849
    • Wilson, K.P.1    Malcolm, B.A.2    Matthews, B.A.3
  • 72
    • 84883283836 scopus 로고    scopus 로고
    • Groel/es buffering and compensatory mutations promote protein evolution by stabilizing folding intermediates
    • Wyganowski KT, Kallenback M, Tokuriki N. 2013. GroEL/ES buffering and compensatory mutations promote protein evolution by stabilizing folding intermediates. J Mol Biol. 425:3403-3414
    • (2013) J Mol Biol , vol.425 , pp. 3403-3414
    • Wyganowski, K.T.1    Kallenback, M.2    Tokuriki, N.3


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