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Volumn 8, Issue 10, 1999, Pages 2186-2193

Design of highly stable functional GroEL minichaperones

Author keywords

Protein engineering; Protein stability; Refolding chromatography; Sequence homology

Indexed keywords

CHAPERONIN; MUTANT PROTEIN;

EID: 0032885223     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.10.2186     Document Type: Article
Times cited : (65)

References (50)
  • 3
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW. 1993. The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science 262:1715-1718.
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase, W.A.3    Matthews, B.W.4
  • 5
    • 0027485997 scopus 로고
    • Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala → Ser and Val → Thr substitutions in T4 lysozyme
    • Blaber M, Lindstrom JD, Gassner N, Xu J, Heinz DW, Matthews BW. 1993. Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala → Ser and Val → Thr substitutions in T4 lysozyme. Biochemistry 32:11363-11373.
    • (1993) Biochemistry , vol.32 , pp. 11363-11373
    • Blaber, M.1    Lindstrom, J.D.2    Gassner, N.3    Xu, J.4    Heinz, D.W.5    Matthews, B.W.6
  • 6
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig K, Adams PD, Brünger AT. 1995. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct Biol 2:1083-1094.
    • (1995) Nature Struct Biol , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 7
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavity-creating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • Buckle AM, Cramer P, Fersht AR. 1996. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry 35:4298-4305.
    • (1996) Biochemistry , vol.35 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 8
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroEL-polypeptide recognition
    • Buckle AM, Zahn R, Fersht AR. 1997. A structural model for GroEL-polypeptide recognition. Proc. Natl Acad Sci USA 94:3571-3575.
    • (1997) Proc. Natl Acad Sci USA , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computational Project, Number 4). 1994. The CCP4 suite: Programs for protein crystallography. Acta Cryst 050:760-763.
    • (1994) Acta Cryst , vol.50 , pp. 760-763
  • 11
    • 0027764465 scopus 로고
    • Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants
    • Chen YW, Fersht AR, Henrick K. 1993. Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants. J Mol Biol 234:1158-1170.
    • (1993) J Mol Biol , vol.234 , pp. 1158-1170
    • Chen, Y.W.1    Fersht, A.R.2    Henrick, K.3
  • 12
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke J, Fersht AR. 1993. Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation. Biochemistry .72:4322-4329.
    • (1993) Biochemistry . , vol.72 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 14
    • 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
  • 16
    • 0026655355 scopus 로고
    • Increasing the thermostabilily of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding
    • Eijsink VG, Vriend G, Van der Zee JR, Van den Burg B, Venema G. 1992b. Increasing the thermostabilily of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding. Biochem J 285:625-628.
    • (1992) Biochem J , vol.285 , pp. 625-628
    • Eijsink, V.G.1    Vriend, G.2    Van Der Zee, J.R.3    Van Den Burg, B.4    Venema, G.5
  • 17
    • 0000484499 scopus 로고
    • Hydrophobic parameters II of amino acid sidechains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere J-L. Pliska V. 1983. Hydrophobic parameters II of amino acid sidechains from the partitioning of N-acetyl-amino-acid amides. Eur J Med Chem 18:369-375.
    • (1983) Eur J Med Chem , vol.18 , pp. 369-375
    • Fauchere, J.-L.1    Pliska, V.2
  • 18
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton WA, Kashi Y, Furtak K, Horwich AL. 1994. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 377:614-619.
    • (1994) Nature , vol.377 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 19
    • 0023662562 scopus 로고
    • Structure-activity relationships in engineered proteins: Analysis of use of binding energy by linear free energy relationships
    • Fersht AR, Leatherbarrow RJ, Wells TN. 1987. Structure-activity relationships in engineered proteins: Analysis of use of binding energy by linear free energy relationships. Biochemistry 26:6030-6038.
    • (1987) Biochemistry , vol.26 , pp. 6030-6038
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.3
  • 20
    • 0021689983 scopus 로고
    • Conformational specificity of chymotrypsin toward proline-containing substrates
    • Fischer G, Bang H, Berger E, Schellenberger A. 1984. Conformational specificity of chymotrypsin toward proline-containing substrates. Biochim Biophys Acta 791:87-97.
    • (1984) Biochim Biophys Acta , vol.791 , pp. 87-97
    • Fischer, G.1    Bang, H.2    Berger, E.3    Schellenberger, A.4
  • 21
    • 0029958604 scopus 로고    scopus 로고
    • A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
    • Gassner NC, Baase WA, Matthews BW. 1996. A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. Proc Natl Acatl Sci USA 93:12155-12158.
    • (1996) Proc Natl Acatl Sci USA , vol.93 , pp. 12155-12158
    • Gassner, N.C.1    Baase, W.A.2    Matthews, B.W.3
  • 22
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J. 1992. Protein folding in the cell. Nature 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 23
    • 0032548994 scopus 로고    scopus 로고
    • Thermodynamic stability and folding of GroEL minichaperones
    • Golbik R, Zahn R, Harding SE, Fersht AR. 1998. Thermodynamic stability and folding of GroEL minichaperones. J Mol Biol 276:505-515.
    • (1998) J Mol Biol , vol.276 , pp. 505-515
    • Golbik, R.1    Zahn, R.2    Harding, S.E.3    Fersht, A.R.4
  • 25
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig B, Yang AS. 1995. Free energy balance in protein folding. Adv Protein Chem 46:27-58.
    • (1995) Adv Protein Chem , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.S.2
  • 26
    • 0027314187 scopus 로고
    • Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core
    • Ishikawa K, Nakamura H, Morikawa K, Kanaya S. 1993. Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. Biochemistry 32:6171-6178.
    • (1993) Biochemistry , vol.32 , pp. 6171-6178
    • Ishikawa, K.1    Nakamura, H.2    Morikawa, K.3    Kanaya, S.4
  • 27
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR. 1993. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32:11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    Elmasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 28
    • 0024295240 scopus 로고
    • Contribution of hydrophobic interactions to protein stability
    • Kellis JT Jr, Nyberg K, Sali D, Fersht AR. 1988. Contribution of hydrophobic interactions to protein stability. Nature 333:784-786.
    • (1988) Nature , vol.333 , pp. 784-786
    • Kellis J.T., Jr.1    Nyberg, K.2    Sali, D.3    Fersht, A.R.4
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0029094346 scopus 로고
    • Enthalpic contribution to protein stability: Insights from atom-based calculations and statistical mechanics
    • Lazaridis T, Archontis G, Karplus M. 1995. Enthalpic contribution to protein stability: Insights from atom-based calculations and statistical mechanics. Adv Protein Chem 47:231-306.
    • (1995) Adv Protein Chem , vol.47 , pp. 231-306
    • Lazaridis, T.1    Archontis, G.2    Karplus, M.3
  • 31
    • 0027522362 scopus 로고
    • Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size
    • Lee B. 1993. Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size. Protein Sci 2:733-738.
    • (1993) Protein Sci , vol.2 , pp. 733-738
    • Lee, B.1
  • 32
    • 0026766573 scopus 로고
    • Structural and energetic consequences of disruptive mutations in a protein core
    • Lim WA, Farruggio DC, Sauer RT 1992. Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry 31:4324-4333.
    • (1992) Biochemistry , vol.31 , pp. 4324-4333
    • Lim, W.A.1    Farruggio, D.C.2    Sauer, R.T.3
  • 33
    • 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
  • 34
    • 0030045089 scopus 로고    scopus 로고
    • Structural and genetic analysis of the folding and function of T4 lysozyme
    • Matthews BW. 1996. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J 10:35-41.
    • (1996) FASEB J , vol.10 , pp. 35-41
    • Matthews, B.W.1
  • 35
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt EA, Murphy MEP. 1994. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr D50:869-873.
    • (1994) Acta Crystallogr , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 36
  • 37
    • 0028608066 scopus 로고
    • Redesigning the hydrophobic core of a four-helix-bundle protein
    • Munson M, O'Brien R, Sturtevant JM, Regan L. 1994. Redesigning the hydrophobic core of a four-helix-bundle protein. Protein Sci 3:2015-2022.
    • (1994) Protein Sci , vol.3 , pp. 2015-2022
    • Munson, M.1    O'Brien, R.2    Sturtevant, J.M.3    Regan, L.4
  • 38
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilizes globular proteins
    • Myers JK, Pace CN. 1996. Hydrogen bonding stabilizes globular proteins. Biophys J 71:2033-2039.
    • (1996) Biophys J , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 39
    • 0032437592 scopus 로고    scopus 로고
    • Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability
    • Nikolova PV, Henckel J, Lane DP, Fersht AR. 1998. Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Proc Natl Acad Sci USA 95:14675-14680.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14675-14680
    • Nikolova, P.V.1    Henckel, J.2    Lane, D.P.3    Fersht, A.R.4
  • 42
    • 0024400292 scopus 로고
    • Influence of interior packing and hydrophobicity on the stability of a protein
    • Sandberg WS, Terwilliger TC. 1989. Influence of interior packing and hydrophobicity on the stability of a protein. Science 245:54-57.
    • (1989) Science , vol.245 , pp. 54-57
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 44
    • 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
  • 45
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano L, Kellis JT Jr, Cann P, Matouschek A, Fersht AR. 1992. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J Mol Biol 224:783-804.
    • (1992) J Mol Biol , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis J.T., Jr.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 46
    • 0028807466 scopus 로고
    • Design and structural analysis of an engineered thermostable chicken lysozyme
    • Shih P, Kirsch JF. 1995. Design and structural analysis of an engineered thermostable chicken lysozyme. Protein Sci 4:2063-2072.
    • (1995) Protein Sci , vol.4 , pp. 2063-2072
    • Shih, P.1    Kirsch, J.F.2
  • 47
    • 0028111743 scopus 로고
    • Sequence statistics reliably predict stabilising mutations in a protein domain
    • Steipe B, Schiller B, Pluckthun A, Steinbacher S. 1994. Sequence statistics reliably predict stabilising mutations in a protein domain. J Mol Biol 240:188-192.
    • (1994) J Mol Biol , vol.240 , pp. 188-192
    • Steipe, B.1    Schiller, B.2    Pluckthun, A.3    Steinbacher, S.4
  • 48
    • 0033580613 scopus 로고    scopus 로고
    • Contribution of hydrogen bonds to the contorinational stability of human lysozyme: Calorimetry and X-ray analysis of six Ser → Ala mutants
    • Takano K, Yamagata Y, Kubota M, Funahashi J, Fujii S, Yutani K. 1999. Contribution of hydrogen bonds to the contorinational stability of human lysozyme: Calorimetry and X-ray analysis of six Ser → Ala mutants. Biochemistry 38:6623-6629.
    • (1999) Biochemistry , vol.38 , pp. 6623-6629
    • Takano, K.1    Yamagata, Y.2    Kubota, M.3    Funahashi, J.4    Fujii, S.5    Yutani, K.6
  • 50
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zahn R, Spitzfaden C, Ottiger M, Wüthrich K, Pluckthun A. 1994. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 368:261-265.
    • (1994) Nature , vol.368 , pp. 261-265
    • Zahn, R.1    Spitzfaden, C.2    Ottiger, M.3    Wüthrich, K.4    Pluckthun, A.5


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