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Volumn 5, Issue 6, 1998, Pages 470-475

Design, structure and stability of a hyperthermophilic protein variant

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; IMMUNOGLOBULIN G;

EID: 0031779918     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0698-470     Document Type: Article
Times cited : (315)

References (47)
  • 1
    • 0030855080 scopus 로고    scopus 로고
    • Stabilization of protein structures
    • Lee, B. & Vasmatzis, G. Stabilization of protein structures. Curr. Opin. Biotech. 8, 423-428 (1997).
    • (1997) Curr. Opin. Biotech. , vol.8 , pp. 423-428
    • Lee, B.1    Vasmatzis, G.2
  • 3
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees, D.C. & Adams, M.W.W. Hyperthermophiles: taking the heat and loving it. Structure 3, 251-254 (1995).
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 4
    • 0030808566 scopus 로고    scopus 로고
    • Dissecting contributions to the thermostability of pyrococcus furiosus rubredoxin: β-sheet chimeras
    • Eidsness, M.K., Richie, K.A., Burden, A.E., Kurtz, J., D. M. & Scott, R.A. Dissecting contributions to the thermostability of pyrococcus furiosus rubredoxin: β-sheet chimeras. Biochemistry 36, 10406-10413 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10406-10413
    • Eidsness, M.K.1    Richie, K.A.2    Burden, A.E.3    Kurtz, J.4    M., D.5    Scott, R.A.6
  • 5
    • 0031048122 scopus 로고    scopus 로고
    • A de novo designed protein with properties that characterize natural hyperthermophilic proteins
    • Jiang, X., Bishop, E.J. & Farid, R.S. A de novo designed protein with properties that characterize natural hyperthermophilic proteins. J. Amer. Chem. Soc. 119, 838-839 (1997).
    • (1997) J. Amer. Chem. Soc. , vol.119 , pp. 838-839
    • Jiang, X.1    Bishop, E.J.2    Farid, R.S.3
  • 6
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat, B.I. & Mayo, S.L. Protein design automation. Protein Sci. 5, 895-903 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 895-903
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 7
    • 0343742614 scopus 로고    scopus 로고
    • Automated design of the surface positions of protein helices
    • Dahiyat, B.I., Gordon, D.B. & Mayo, S.L. Automated design of the surface positions of protein helices. Protein Sci. 6, 1333-1337 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 1333-1337
    • Dahiyat, B.I.1    Gordon, D.B.2    Mayo, S.L.3
  • 8
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat, B.I. & Mayo, S.L. Probing the role of packing specificity in protein design. Proc. Natl. Acad. Sci. USA 94, 10172-10177 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 9
    • 0031558762 scopus 로고    scopus 로고
    • De novo protein design: Towards fully automated sequence selection
    • Dahiyat, B.I., Sarisky, C.A. & Mayo, S.L. De novo protein design: towards fully automated sequence selection. J. Mol. Biol. 273, 789-796 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 789-796
    • Dahiyat, B.I.1    Sarisky, C.A.2    Mayo, S.L.3
  • 10
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat, B.I. & Mayo, S.L. De novo protein design: fully automated sequence selection. Science 278, 82-87 (1997).
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 11
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • Desmet, J., De Maeyer, M., Hazes, B. & Lasters, I. The dead-end elimination theorem and its use in protein side-chain positioning. Nature 356, 539-542 (1992).
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    De Maeyer, M.2    Hazes, B.3    Lasters, I.4
  • 12
    • 0028212927 scopus 로고
    • Efficient rotamer elimination applied to protein side-chains and related spin-glasses
    • Goldstein, R.F. Efficient rotamer elimination applied to protein side-chains and related spin-glasses. Biophys. J. 66, 1335-1340 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 1335-1340
    • Goldstein, R.F.1
  • 13
    • 0030623575 scopus 로고    scopus 로고
    • All in one: A highly detailed rotamer library improves both accuracy and speed in the modeling of sidechains by dead-end elimination
    • De Maeyer, M., Desmet, J. & Lasters, I. All in one: a highly detailed rotamer library improves both accuracy and speed in the modeling of sidechains by dead-end elimination. Folding & Design 2, 53-66 (1997).
    • (1997) Folding & Design , vol.2 , pp. 53-66
    • De Maeyer, M.1    Desmet, J.2    Lasters, I.3
  • 14
    • 0025769350 scopus 로고
    • A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G
    • Gronenborn, A.M. et al. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science 253, 657-661 (1991).
    • (1991) Science , vol.253 , pp. 657-661
    • Gronenborn, A.M.1
  • 15
    • 0028354429 scopus 로고
    • Two crystal structures of the β1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher, T., Alexander, P., Bryan, P. & Gilliland, G.L. Two crystal structures of the β1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33, 4721-4729 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 16
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C. et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542 (1977).
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1
  • 17
    • 0030762021 scopus 로고    scopus 로고
    • Coupling backbone flexibility and amino acid sequence selection in protein design
    • Su, A. & Mayo, S.L. Coupling backbone flexibility and amino acid sequence selection in protein design. Protein Sci. 6, 1701-1707 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 1701-1707
    • Su, A.1    Mayo, S.L.2
  • 18
    • 0018115846 scopus 로고
    • Conformation of amino acid side-chains in proteins
    • Janin, J., Wodak, S., Levitt, M. & Maigret, B. Conformation of amino acid side-chains in proteins. J. Mol. Biol. 125, 357-386 (1978).
    • (1978) J. Mol. Biol. , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2    Levitt, M.3    Maigret, B.4
  • 19
    • 0023155210 scopus 로고
    • Tertiary templates for proteins-use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder, J.W. & Richards, F.M. Tertiary templates for proteins-use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775-791 (1987).
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 20
    • 0027160197 scopus 로고
    • Backbone dependent rotamer library for proteins -an application to side-chain prediction
    • Dunbrack, R.L. & Karplus, M. Backbone dependent rotamer library for proteins -an application to side-chain prediction. J. Mol. Biol. 230, 543-574 (1993).
    • (1993) J. Mol. Biol. , vol.230 , pp. 543-574
    • Dunbrack, R.L.1    Karplus, M.2
  • 21
    • 0029585945 scopus 로고
    • Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
    • Zhang, X.J., Baase, W.A., Shoichet, B.K., Wilson, K.P. & Matthews, B.W. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Prot. Engng. 8, 1017-1022 (1995).
    • (1995) Prot. Engng. , vol.8 , pp. 1017-1022
    • Zhang, X.J.1    Baase, W.A.2    Shoichet, B.K.3    Wilson, K.P.4    Matthews, B.W.5
  • 22
    • 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, A.G. & Fersht, A.R. 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).
    • (1993) J. Mol. Biol. , vol.233 , pp. 305-312
    • Serrano, L.1    Day, A.G.2    Fersht, A.R.3
  • 23
    • 0024962392 scopus 로고
    • Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding
    • Pantoliano, M.W. et al. Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Biochemistry 28, 7205-7213 (1989).
    • (1989) Biochemistry , vol.28 , pp. 7205-7213
    • Pantoliano, M.W.1
  • 24
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553 (1979).
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 25
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sorensen, O.W. & Ernst, R.R. Multiple quantum filters for elucidating NMR coupling networks. J. Amer. Chem. Soc. 104, 6800-6801 (1982).
    • (1982) J. Amer. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sorensen, O.W.2    Ernst, R.R.3
  • 26
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360 (1985).
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 29
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry- Dynamical simulated annealing calculations
    • Nilges, M., Clore, G.M. & Gronenborn, A.M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett. 229, 317-324 (1988).
    • (1988) FEBS Lett. , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 30
    • 0001708879 scopus 로고
    • Sampling properties of simulated annealing and distance geometry
    • eds Hoch, J.C., Poulsen, F.M. & Redfield, C. Plenum Press, New York
    • Nilges, M., Kuszewski, J. & Brünger, A.T. Sampling properties of simulated annealing and distance geometry. in Computational Aspects of the Study of Biological Macromolecules by NMR (eds Hoch, J.C., Poulsen, F.M. & Redfield, C.) 451-457 (Plenum Press, New York, 1991).
    • (1991) Computational Aspects of the Study of Biological Macromolecules by NMR , pp. 451-457
    • Nilges, M.1    Kuszewski, J.2    Brünger, A.T.3
  • 31
    • 0026676167 scopus 로고
    • Sampling and efficiency of metric matrix distance geometry - A novel partial metrization algorithm
    • Kuszewski, J., Nilges, M. & Brünger, A.T. Sampling and efficiency of metric matrix distance geometry - a novel partial metrization algorithm. J. Biomol. NMR 2, 33-56 (1992).
    • (1992) J. Biomol. NMR , vol.2 , pp. 33-56
    • Kuszewski, J.1    Nilges, M.2    Brünger, A.T.3
  • 32
    • 0027092679 scopus 로고
    • The solution structure of eglin-c based on measurements of many NOEs and coupling-constants and its comparison with X-ray structures
    • Hyberts, S.G., Goldberg, M.S., Havel, T.F. & Wagner, G. The solution structure of eglin-c based on measurements of many NOEs and coupling-constants and its comparison with X-ray structures. Protein Sci. 1, 736-751 (1992).
    • (1992) Protein Sci. , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Macarthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0027421911 scopus 로고
    • Identification of the contact surface of a streptococcal protein G-domain complexed with a human Fc fragment
    • Gronenborn, A.M. & Clore, G.M. Identification of the contact surface of a streptococcal protein G-domain complexed with a human Fc fragment. J. Mol. Biol. 233, 331-335 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 331-335
    • Gronenborn, A.M.1    Clore, G.M.2
  • 35
    • 0027359429 scopus 로고
    • Effect of a single aspartate on helix stability at different positions in a neutral alanine based peptide
    • Huyghues-Despointes, B.M.P., Scholtz, J.M. & Baldwin, R.L. Effect of a single aspartate on helix stability at different positions in a neutral alanine based peptide. Protein Sci. 2, 1604-1611 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 1604-1611
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 36
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl, C.A., Chakrabartty, A. & Baldwin, R.L. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5, 2623-2637 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 37
    • 0029554952 scopus 로고
    • Designing amino acid sequences to fold with good hydrophobic cores
    • Sun, S., Brem, R., Chan, H.S. & Dill, K.A. Designing amino acid sequences to fold with good hydrophobic cores. Protein Engng. 8, 1205-1213 (1995).
    • (1995) Protein Engng. , vol.8 , pp. 1205-1213
    • Sun, S.1    Brem, R.2    Chan, H.S.3    Dill, K.A.4
  • 38
    • 0027411181 scopus 로고
    • Thermodynamic β-sheet propensities measured using a zinc-finger host peptide
    • Kim, C.A. & Berg, J.M. Thermodynamic β-sheet propensities measured using a zinc-finger host peptide. Nature 362, 267-270 (1993).
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 39
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor, D.L. & Kim, P.S. Measurement of the β-sheet-forming propensities of amino acids. Nature 367, 660-663 (1994).
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor, D.L.1    Kim, P.S.2
  • 40
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith, C.K., Withka, J.M. & Regan, L. A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry 33, 5510-5517 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 41
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains β1 and β2 - Why small proteins tend to have high denaturation temperatures
    • Alexander, P., Fahnestock, S., Lee, T., Orban, J. & Bryan, P. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains β1 and β2 - why small proteins tend to have high denaturation temperatures. Biochemistry 31, 3597-3603 (1992).
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 42
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing
    • Johnson, B.H. & Hecht, M.H. Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Biotechnology 12, 1357-1360 (1994).
    • (1994) Biotechnology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 43
    • 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. & Bolen, D.W. Unfolding free-energy changes determined by the linear extrapolation method .1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068 (1988).
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 44
    • 0026951903 scopus 로고
    • Gradient tailored excitation for single quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenar, V. Gradient tailored excitation for single quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665 (1992).
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 45
    • 0001250026 scopus 로고
    • 1H 2D NMR spectra by interactive computer graphics
    • 1H 2D NMR spectra by interactive computer graphics. J. Magn. Reson. 84, 627-633 (1989).
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-Continues (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 51
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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