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Volumn 71, Issue 1, 2008, Pages 165-174

Engineering proteins with tunable thermodynamic and kinetic stabilities

Author keywords

Free energy barriers; Kinetic stability; Protein stability; Salt effects

Indexed keywords

SODIUM CHLORIDE;

EID: 40549116348     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21670     Document Type: Article
Times cited : (41)

References (41)
  • 1
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malaskauskas SM, Mayo SL. Design, structure and stability of a hyperthermophilic protein variant. Nat Struct Biol 1998;5:470-475.
    • (1998) Nat Struct Biol , vol.5 , pp. 470-475
    • Malaskauskas, S.M.1    Mayo, S.L.2
  • 3
    • 0037019469 scopus 로고    scopus 로고
    • Genetic algorithm to design stabilizing surface-charge distributions in proteins
    • Ibarra-Molero B, Sanchez-Ruiz JM. Genetic algorithm to design stabilizing surface-charge distributions in proteins. J Phys Chem B 2002;106:6609-6613.
    • (2002) J Phys Chem B , vol.106 , pp. 6609-6613
    • Ibarra-Molero, B.1    Sanchez-Ruiz, J.M.2
  • 6
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D, Mueller U, Heinemann U, Schmid FX. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat Struct Biol 2000;7:380-383.
    • (2000) Nat Struct Biol , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 7
    • 0034020833 scopus 로고    scopus 로고
    • Single surface stabilizer
    • Pace CN. Single surface stabilizer. Nat Struc Biol 2000;7:345-346.
    • (2000) Nat Struc Biol , vol.7 , pp. 345-346
    • Pace, C.N.1
  • 8
    • 0034731381 scopus 로고    scopus 로고
    • The consensus concept for thermostability engineering of proteins
    • Lehman M, Pasamontes L, Lassen SF, Wyss M. The consensus concept for thermostability engineering of proteins. Biochim Biophys Acta 2000;1543:408-415.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 408-415
    • Lehman, M.1    Pasamontes, L.2    Lassen, S.F.3    Wyss, M.4
  • 9
    • 4043142209 scopus 로고    scopus 로고
    • Consensus-based engineering of protein stability: From intrabodies to thermostable enzymes
    • Steipe B. Consensus-based engineering of protein stability: from intrabodies to thermostable enzymes. Methods Enzymol 2004;388:176-186.
    • (2004) Methods Enzymol , vol.388 , pp. 176-186
    • Steipe, B.1
  • 11
    • 0035018435 scopus 로고    scopus 로고
    • Cancer chemotherapy - ribonucleases to the rescue
    • Leland PA, Raines RT. Cancer chemotherapy - ribonucleases to the rescue. Chem Biol 2000;8:405-413.
    • (2000) Chem Biol , vol.8 , pp. 405-413
    • Leland, P.A.1    Raines, R.T.2
  • 12
    • 0029811964 scopus 로고    scopus 로고
    • Molecular determinants in the plasma clearance and tissue distribution of ribonucleases of the ribonuclease A superfamily
    • Vasandani VM, Wu YN, Mikulski SM, Youle RJ, Sung C. Molecular determinants in the plasma clearance and tissue distribution of ribonucleases of the ribonuclease A superfamily Cancer Res 1996;56:4180-4186.
    • (1996) Cancer Res , vol.56 , pp. 4180-4186
    • Vasandani, V.M.1    Wu, Y.N.2    Mikulski, S.M.3    Youle, R.J.4    Sung, C.5
  • 13
    • 0033051964 scopus 로고    scopus 로고
    • Reversible nephrotoxicity of onconase and effect of lysine pH on renal onconase uptake
    • Vasandani VM, Burris JA, Sung C. Reversible nephrotoxicity of onconase and effect of lysine pH on renal onconase uptake. Cancer Chemoter Pharmacol 1999;44;164-169.
    • (1999) Cancer Chemoter Pharmacol , vol.44 , pp. 164-169
    • Vasandani, V.M.1    Burris, J.A.2    Sung, C.3
  • 16
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein termal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases
    • Plaza del Pino IM, Ibarra-Molero B, Sanchez-Ruiz JM. Lower kinetic limit to protein termal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins: Struct Funct Genet 2000;40:58-70.
    • (2000) Proteins: Struct Funct Genet , vol.40 , pp. 58-70
    • Plaza del Pino, I.M.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3
  • 17
    • 0001002352 scopus 로고
    • Conformational changes in proteins
    • Lumry R, Eyring H. Conformational changes in proteins. J Phys Chem 1954;58:110-120.
    • (1954) J Phys Chem , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 18
    • 0002127271 scopus 로고
    • Thermal stability of proteins
    • Oxender DL, Fox CF, editors, New York: Liss;
    • Klibanov AM, Ahern TJ. Thermal stability of proteins. In: Oxender DL, Fox CF, editors. Protein engineering. New York: Liss; 1987. pp 213-218.
    • (1987) Protein engineering , pp. 213-218
    • Klibanov, A.M.1    Ahern, T.J.2
  • 19
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz JM. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys J 1992;61:921-935.
    • (1992) Biophys J , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 20
    • 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, Rodríguez-Larrea D, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM. 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 2006;362:966-978.
    • (2006) J Mol Biol , vol.362 , pp. 966-978
    • Godoy-Ruiz, R.1    Ariza, F.2    Rodríguez-Larrea, D.3    Perez-Jimenez, R.4    Ibarra-Molero, B.5    Sanchez-Ruiz, J.M.6
  • 21
    • 23944522022 scopus 로고    scopus 로고
    • Downhill protein folding: Evolution meets physics
    • Gruebele M. Downhill protein folding: evolution meets physics. C R Biol 2005;328:701-712.
    • (2005) C R Biol , vol.328 , pp. 701-712
    • Gruebele, M.1
  • 22
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci 1999;24:329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 23
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Böhm G. The stability of proteins in extreme environments. Curr Opin Struct Biol 1998;8:738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 24
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • Jaenicke R. Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc Natl Acad Sci USA 2000;97:2962-2964.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 25
    • 0346500473 scopus 로고    scopus 로고
    • Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus
    • Zeeb M, Lipps G, Lilie H, Balbach J. Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus. J Mol Biol 2004;336:227-240.
    • (2004) J Mol Biol , vol.336 , pp. 227-240
    • Zeeb, M.1    Lipps, G.2    Lilie, H.3    Balbach, J.4
  • 26
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of alphabetic protease are more stable than its native state
    • Sohl JL, Jaswal SS, Agard DA. Unfolded conformations of alphabetic protease are more stable than its native state. Nature 1998;395:817-819.
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1    Jaswal, S.S.2    Agard, D.A.3
  • 27
    • 34247180735 scopus 로고    scopus 로고
    • Energetics-based profiling on a proteomic scale: Identification of proteins resistant to proteolysis
    • doi: 10.1016/j.jmb.2007.02.091
    • Park C, Zhou S, Gilmore J, Marqusee S. Energetics-based profiling on a proteomic scale: identification of proteins resistant to proteolysis. J Mol Biol 2007; doi: 10.1016/j.jmb.2007.02.091.
    • (2007) J Mol Biol
    • Park, C.1    Zhou, S.2    Gilmore, J.3    Marqusee, S.4
  • 28
    • 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. A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization. Biophys J 2005;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
  • 29
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibarra-Molero B, Loladze W, Makhatadze GI, Sanchez-Ruiz JM. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 1999;38:8138-8149.
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, W.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 30
    • 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. Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations. J Mol Biol 2004;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
  • 31
    • 40549119584 scopus 로고    scopus 로고
    • The efficiency of different salts to screen charge interactions in proteins: A Hofmeister effect?
    • Perez-Jimenez R, Godoy-Ruiz R, Ibarra-Molero B, Sanchez-Ruiz JM. The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect? Biophys J 2005;35:14689-14702.
    • (2005) Biophys J , vol.35 , pp. 14689-14702
    • Perez-Jimenez, R.1    Godoy-Ruiz, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 32
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 1979;254:9627-9632.
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 33
    • 0018788324 scopus 로고
    • Structure and enzymatic functions of thioredoxin refolded by complementation of two tryptic peptide fragments
    • Slaby I, Holmgren A. Structure and enzymatic functions of thioredoxin refolded by complementation of two tryptic peptide fragments. Biochemistry 1979;18:5584-5591.
    • (1979) Biochemistry , vol.18 , pp. 5584-5591
    • Slaby, I.1    Holmgren, A.2
  • 35
    • 0030458930 scopus 로고    scopus 로고
    • A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data
    • Ibarra-Molero B, Sanchez-Ruiz JM. A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data. Biochemistry 1996;35:14689-14702.
    • (1996) Biochemistry , vol.35 , pp. 14689-14702
    • Ibarra-Molero, B.1    Sanchez-Ruiz, J.M.2
  • 36
    • 7044224471 scopus 로고    scopus 로고
    • Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimization
    • Campos LA, Garcia-Mira MM, Godoy-Ruiz R, Sanchez-Ruiz JM, Sancho J. Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimization. J Mol Biol 2004;344:223-237.
    • (2004) J Mol Biol , vol.344 , pp. 223-237
    • Campos, L.A.1    Garcia-Mira, M.M.2    Godoy-Ruiz, R.3    Sanchez-Ruiz, J.M.4    Sancho, J.5
  • 37
    • 0028111743 scopus 로고
    • Sequence statistics reliably predicts stabilizing mutations in a protein domain
    • Steipe B, Schiller B, Plückthun A, Steinbacher S. Sequence statistics reliably predicts stabilizing mutations in a protein domain. J Mol Biol 1994;240:182-192.
    • (1994) J Mol Biol , vol.240 , pp. 182-192
    • Steipe, B.1    Schiller, B.2    Plückthun, A.3    Steinbacher, S.4
  • 39
    • 33748945709 scopus 로고    scopus 로고
    • Point mutations in protein globular domains: Contributions from function, stability and misfolding
    • Sanchez IE, Tejero J, Gomez-Moreno C, Medina M, Serrano L. Point mutations in protein globular domains: contributions from function, stability and misfolding. J Mol Biol 2006;363:422-432.
    • (2006) J Mol Biol , vol.363 , pp. 422-432
    • Sanchez, I.E.1    Tejero, J.2    Gomez-Moreno, C.3    Medina, M.4    Serrano, L.5
  • 40
    • 0019837215 scopus 로고
    • Nature of the charge distribution in proteins
    • Wada A, Nakamura H. Nature of the charge distribution in proteins. Nature 1981;293:757-758.
    • (1981) Nature , vol.293 , pp. 757-758
    • Wada, A.1    Nakamura, H.2


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