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Volumn 13, Issue 8, 2004, Pages 2078-2088

Biophysical characterization of ZSPA-1 - A phage-display selected binder to protein A

Author keywords

Affibody; NMR spectroscopy; Osmolyte; Protein engineering; Protein stability

Indexed keywords

MUTANT PROTEIN; PROTEIN A; STAPHYLOCOCCUS PROTEIN A; TRIMETHYLAMINE OXIDE;

EID: 3342879396     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04728604     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 0032570873 scopus 로고    scopus 로고
    • Forcing thermodynamically unfolded proteins to fold
    • Baskakov, I.V. and Bolen, D.W. 1998. Forcing thermodynamically unfolded proteins to fold. J. Biol. Chem. 273: 4831-4834.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4831-4834
    • Baskakov, I.V.1    Bolen, D.W.2
  • 2
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen, D.W. and Baskakov, I.V. 2001. The osmophobic effect: Natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310: 955-963.
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 4
    • 0036076894 scopus 로고    scopus 로고
    • Osmolyte effects on helix formation in peptides and stability of coiled-coils
    • Celinski, S.A. and Scholtz, J.M. 2002. Osmolyte effects on helix formation in peptides and stability of coiled-coils. Protein Sci. 11: 2048-2051.
    • (2002) Protein Sci. , vol.11 , pp. 2048-2051
    • Celinski, S.A.1    Scholtz, J.M.2
  • 5
    • 0034161321 scopus 로고    scopus 로고
    • NPS@: Network protein sequence analysis
    • Combet, C., Blanchet, C., Geourjon, C., and Deléage, G. 2000. NPS@: Network protein sequence analysis. TIBS 25: 147-150.
    • (2000) TIBS , vol.25 , pp. 147-150
    • Combet, C.1    Blanchet, C.2    Geourjon, C.3    Deléage, G.4
  • 6
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphyloccocus aureus at 2.9- and 2.8-Å resolution
    • Deisenhofer, J. 1981. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphyloccocus aureus at 2.9- and 2.8-Å resolution. Biochemistry 20: 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 7
    • 0029400480 scopus 로고
    • NMRpipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRpipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 8
    • 0028466243 scopus 로고
    • Solid evidence for molten globules
    • Dobson, C.M. 1994. Solid evidence for molten globules. Curr. Biol. 4: 636-640.
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 9
    • 0037102973 scopus 로고    scopus 로고
    • Anti-idiotypic protein domains selected from protein A-based affibody libraries
    • Eklund, M., Axelsson, L., Uhlén, M., and Nygren, P.-Å. 2002. Anti-idiotypic protein domains selected from protein A-based affibody libraries. Proteins 48: 454-462.
    • (2002) Proteins , vol.48 , pp. 454-462
    • Eklund, M.1    Axelsson, L.2    Uhlén, M.3    Nygren, P.-Å.4
  • 10
    • 1842608323 scopus 로고    scopus 로고
    • Site-specific and reversible anchoring of active proteins onto cellulose using a cellulosome-like complex
    • Eklund, M., Sandström, K., Teeri, T.T., and Nygren, P.-Å. 2004. Site-specific and reversible anchoring of active proteins onto cellulose using a cellulosome-like complex. J. Biotechnol. 109: 277-286.
    • (2004) J. Biotechnol. , vol.109 , pp. 277-286
    • Eklund, M.1    Sandström, K.2    Teeri, T.T.3    Nygren, P.-Å.4
  • 13
    • 0000715884 scopus 로고
    • A new method for the study of moderately rapid chemical exchange rates employing nuclear magnetic double resonance
    • Forsén, S. and Hoffman, R.A. 1963. A new method for the study of moderately rapid chemical exchange rates employing nuclear magnetic double resonance. Acta Chem. Scand. 17: 1787-1788.
    • (1963) Acta Chem. Scand. , vol.17 , pp. 1787-1788
    • Forsén, S.1    Hoffman, R.A.2
  • 14
    • 0037048525 scopus 로고    scopus 로고
    • A novel affinity gene fusion system allowing protein A-based recovery of non-immunoglobulin gene products
    • Gräslund, S., Eklund, M., Falk, R., Uhlén, M., Nygren, P.-Å., and Ståhl, S. 2002. A novel affinity gene fusion system allowing protein A-based recovery of non-immunoglobulin gene products. J. Biotechnol. 99: 41-50.
    • (2002) J. Biotechnol. , vol.99 , pp. 41-50
    • Gräslund, S.1    Eklund, M.2    Falk, R.3    Uhlén, M.4    Nygren, P.-Å.5    Ståhl, S.6
  • 15
    • 0032717780 scopus 로고    scopus 로고
    • Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling
    • Gunneriusson, E., Nord, K., Uhlén, M., and Nygren, P.-Å. 1999. Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling. Protein Eng. 12: 873-878.
    • (1999) Protein Eng. , vol.12 , pp. 873-878
    • Gunneriusson, E.1    Nord, K.2    Uhlén, M.3    Nygren, P.-Å.4
  • 16
    • 0033103888 scopus 로고    scopus 로고
    • An in vitro selected binding protein (affibody) shows conformation-dependent recognition of the respiratory syncytial virus (RSV) G protein
    • Hansson, M., Ringdahl, J., Robert, A., Power, U., Goetsch, L., Nguyen, T., Uhlén, M., Ståhl, S., and Nygren, P.-Å. 1999. An in vitro selected binding protein (affibody) shows conformation-dependent recognition of the respiratory syncytial virus (RSV) G protein. Immunotechnology 4: 237-252.
    • (1999) Immunotechnology , vol.4 , pp. 237-252
    • Hansson, M.1    Ringdahl, J.2    Robert, A.3    Power, U.4    Goetsch, L.5    Nguyen, T.6    Uhlén, M.7    Ståhl, S.8    Nygren, P.-Å.9
  • 17
    • 0035951350 scopus 로고    scopus 로고
    • Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase
    • Hansson, H., Okoh, M.P., Smith, C.I.E., Vihinen, M., and Härd, T. 2001. Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase. FEBS Lett. 489: 67-70.
    • (2001) FEBS Lett. , vol.489 , pp. 67-70
    • Hansson, H.1    Okoh, M.P.2    Smith, C.I.E.3    Vihinen, M.4    Härd, T.5
  • 18
    • 0034515845 scopus 로고    scopus 로고
    • Ansig for Windows: An interactive computer program for semiautomatic assignment of protein NMR spectra
    • Helgstrand, M., Kraulis, P., Allard, P., and Härd, T. 2000. Ansig for Windows: An interactive computer program for semiautomatic assignment of protein NMR spectra. J. Biomol. NMR 18: 329-336.
    • (2000) J. Biomol. NMR , vol.18 , pp. 329-336
    • Helgstrand, M.1    Kraulis, P.2    Allard, P.3    Härd, T.4
  • 19
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M., and Hecht, M.H. 1993. Protein design by binary patterning of polar and nonpolar amino acids. Science 262: 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S., Janin, J., Lesk, A.M., and Chothia, C. 1987. Interior and surface of monomeric proteins. J. Mol. Biol. 196: 641-656.
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4
  • 25
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain
    • Nord, K., Gunneriusson, E., Ringdahl, J., Ståhl, S., Uhlén, M., and Nygren, P.-Å. 1997. Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain. Nat. Biotechnol. 15: 772-777.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Ståhl, S.4    Uhlén, M.5    Nygren, P.-Å.6
  • 26
    • 0034832744 scopus 로고    scopus 로고
    • Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A
    • Nord, K., Nord, O., Uhlén, M., Kelley, B., Ljungqvist, C., and Nygren, P.-Å. 2001. Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A. Eur. J. Biochem. 268: 4269-4277.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4269-4277
    • Nord, K.1    Nord, O.2    Uhlén, M.3    Kelley, B.4    Ljungqvist, C.5    Nygren, P.-Å.6
  • 27
    • 0030822252 scopus 로고    scopus 로고
    • Scaffolds for engineering novel binding sites in proteins
    • Nygren, P.-Å. and Uhlén, M. 1997. Scaffolds for engineering novel binding sites in proteins. Curr. Opin. Struct. Biol. 7: 463-469.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 463-469
    • Nygren, P.-Å.1    Uhlén, M.2
  • 28
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer III, A.G. 2001. NMR probes of molecular dynamics: Overview and comparison with other techniques. Annu. Rev. Biophys. Biomol. Struct. 30: 129-155.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 29
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn, O.B. 1995. Structures of folding intermediates. Curr. Opin. Struc. Biol. 5: 74-78.
    • (1995) Curr. Opin. Struc. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 30
    • 0033528858 scopus 로고    scopus 로고
    • Molten globules
    • Redfield, C. 1999. Molten globules. Curr. Biol. 9: R313.
    • (1999) Curr. Biol. , vol.9
    • Redfield, C.1
  • 31
    • 0028367331 scopus 로고
    • Structural characterization of a highly-ordered 'molten globule' at low pH
    • Redfield, C., Smith, R.A.G., and Dobson, C.M. 1994. Structural characterization of a highly-ordered 'molten globule' at low pH. Nat. Struct. Biol. 1: 23-29.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 23-29
    • Redfield, C.1    Smith, R.A.G.2    Dobson, C.M.3
  • 32
    • 0036275295 scopus 로고    scopus 로고
    • Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A
    • Rönnmark, J., Grönlund, H., Uhlén, M., and Nygren, P.-Å. 2002. Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A. Eur. J. Biochem. 269: 2647-2655.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2647-2655
    • Rönnmark, J.1    Grönlund, H.2    Uhlén, M.3    Nygren, P.-Å.4
  • 33
    • 0142184270 scopus 로고    scopus 로고
    • Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding ligand developed by combinatorial protein engineering
    • Sandström, K., Xu, Z., Forsberg, G., and Nygren, P.-Å. 2003. Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding ligand developed by combinatorial protein engineering. Protein Eng. 6: 691-697.
    • (2003) Protein Eng. , vol.6 , pp. 691-697
    • Sandström, K.1    Xu, Z.2    Forsberg, G.3    Nygren, P.-Å.4
  • 34
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman, B.A., Kim, P.S., Dobson, C.M., and Redfield, C. 1997. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat. Struct. Biol. 4: 630-634.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 37
  • 39
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong, H., Buckwalter, B.L., Shieh, H.-M., and Hecht, M.H. 1995. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc. Natl. Acad. Sci. 92: 6349-6353.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Shieh, H.-M.3    Hecht, M.H.4
  • 40
    • 0347694974 scopus 로고    scopus 로고
    • On the extended β-conformation propensity of polypeptides at high temperature
    • Yang, W.Y., Larios, E., and Gruebele, M. 2003. On the extended β-conformation propensity of polypeptides at high temperature. J. Am. Chem. Soc. 125: 16220-16227.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16220-16227
    • Yang, W.Y.1    Larios, E.2    Gruebele, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.