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Volumn 17, Issue 9, 2008, Pages 1630-1635

NMR spectroscopy as a tool for the rapid assessment of the conformation of GST-fusion proteins

Author keywords

GST fusion; GST pulldown; NMR spectroscopy; Protein conformation

Indexed keywords

GLUTATHIONE TRANSFERASE; HYBRID PROTEIN;

EID: 50049088243     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.034983.108     Document Type: Article
Times cited : (9)

References (26)
  • 2
    • 40549097122 scopus 로고    scopus 로고
    • Protein-protein interactions identified by pulldown experiments and mass spectrometry
    • Section 17.5. Unlimited Learning Resources, Winston-Salem, NC
    • Brymora, A., Valova, V.A., and Robinson, P.J 2004. Protein-protein interactions identified by pulldown experiments and mass spectrometry. In Current protocols in cell biology, Section 17.5. Unlimited Learning Resources, Winston-Salem, NC.
    • (2004) Current protocols in cell biology
    • Brymora, A.1    Valova, V.A.2    Robinson, P.J.3
  • 3
    • 1942537173 scopus 로고    scopus 로고
    • Catanzariti, A.M., Soboleva, T.A., Jans, D.A., Board, P.G., and Baker, R.T. 2004. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13: 1331-1339.
    • Catanzariti, A.M., Soboleva, T.A., Jans, D.A., Board, P.G., and Baker, R.T. 2004. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13: 1331-1339.
  • 5
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew, E. and Williams, K. 1999. Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Tech. 10: 51-63.
    • (1999) J. Biomol. Tech , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.2
  • 6
    • 0032509511 scopus 로고    scopus 로고
    • Key residues characteristic of GATA N-fingers are recognized by FOG
    • Fox, A.H., Kowalski, K., King, G.F., Mackay, J.P., and Crossley, M. 1998. Key residues characteristic of GATA N-fingers are recognized by FOG. J. Biol. Chem. 273: 33595-33603.
    • (1998) J. Biol. Chem , vol.273 , pp. 33595-33603
    • Fox, A.H.1    Kowalski, K.2    King, G.F.3    Mackay, J.P.4    Crossley, M.5
  • 8
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarstrom, M., Hellgren, N., van Den Berg, S., Berglund, H., and Hard, T. 2002. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11: 313-321.
    • (2002) Protein Sci , vol.11 , pp. 313-321
    • Hammarstrom, M.1    Hellgren, N.2    van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 9
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • Huth, J.R., Bewley, C.A., Jackson, B.M., Hinnebusch, A.G., Clore, G.M., and Gronenborn, A.M. 1997. Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci. 6: 2359-2364.
    • (1997) Protein Sci , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 11
    • 0011962568 scopus 로고    scopus 로고
    • Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
    • LaVallie, E.R., Lu, Z., Diblasio-Smith, E.A., Collins-Racie, L.A., and McCoy, J.M. 2000. Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli. Methods Enzymol. 326: 322-340.
    • (2000) Methods Enzymol , vol.326 , pp. 322-340
    • LaVallie, E.R.1    Lu, Z.2    Diblasio-Smith, E.A.3    Collins-Racie, L.A.4    McCoy, J.M.5
  • 12
    • 34547593865 scopus 로고    scopus 로고
    • Embryonic neural inducing factor Churchill is not a DNA-binding zinc finger protein: Solution structure reveals a solvent-exposed β-sheet and zinc binuclear cluster
    • Lee, B.M., Buck-Koehntop, B.A., Martinez-Yamout, M.A., Dyson, H.J., and Wright, P.E. 2007. Embryonic neural inducing factor Churchill is not a DNA-binding zinc finger protein: Solution structure reveals a solvent-exposed β-sheet and zinc binuclear cluster. J. Mol. Biol. 371: 1274-1289.
    • (2007) J. Mol. Biol , vol.371 , pp. 1274-1289
    • Lee, B.M.1    Buck-Koehntop, B.A.2    Martinez-Yamout, M.A.3    Dyson, H.J.4    Wright, P.E.5
  • 13
    • 33846336737 scopus 로고    scopus 로고
    • Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP)
    • Liew, C.K., Crossley, M., Mackay, J.P., and Nicholas, H.R. 2007. Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP). J. Mol. Biol. 366: 382-390.
    • (2007) J. Mol. Biol , vol.366 , pp. 382-390
    • Liew, C.K.1    Crossley, M.2    Mackay, J.P.3    Nicholas, H.R.4
  • 14
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • Masino, L., Kelly, G., Leonard, K., Trottier, Y., and Pastore, A. 2002. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett. 513: 267-272.
    • (2002) FEBS Lett , vol.513 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 17
    • 0029962007 scopus 로고    scopus 로고
    • Multimer formation as a consequence of separate homodimerization domains: The human c-Jun leucine zipper is a transplantable dimerization module
    • Riley, L.G., Ralston, G.B., and Weiss, A.S. 1996. Multimer formation as a consequence of separate homodimerization domains: The human c-Jun leucine zipper is a transplantable dimerization module. Protein Eng. 9: 223-230.
    • (1996) Protein Eng , vol.9 , pp. 223-230
    • Riley, L.G.1    Ralston, G.B.2    Weiss, A.S.3
  • 19
    • 0033809233 scopus 로고    scopus 로고
    • Fusions to maltose-binding protein: Control of folding and solubility in protein purification
    • Sachdev, D. and Chirgwin, J.M. 2000. Fusions to maltose-binding protein: Control of folding and solubility in protein purification. Methods Enzymol. 326: 312-321.
    • (2000) Methods Enzymol , vol.326 , pp. 312-321
    • Sachdev, D.1    Chirgwin, J.M.2
  • 20
    • 0027939211 scopus 로고
    • Characterization of RNA binding specificity of the Drosophila sex-lethal protein by in vitro ligand selection
    • Sakashita, E. and Sakamoto, H. 1994. Characterization of RNA binding specificity of the Drosophila sex-lethal protein by in vitro ligand selection. Nucleic Acids Res. 22: 4082-4086.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4082-4086
    • Sakashita, E.1    Sakamoto, H.2
  • 21
    • 0033809095 scopus 로고    scopus 로고
    • Generating fusions to glutathione S-transferase for protein studies
    • Smith, D.B. 2000. Generating fusions to glutathione S-transferase for protein studies. Methods Enzymol. 326: 254-270.
    • (2000) Methods Enzymol , vol.326 , pp. 254-270
    • Smith, D.B.1
  • 23
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang, C., Ndassa, Y., and Summers, M.F. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9: 537-543.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 24
    • 0037189901 scopus 로고    scopus 로고
    • Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G
    • Tugarinov, V., Muhandiram, R., Ayed, A., and Kay, L.E. 2002. Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G. J. Am. Chem. Soc. 124: 10025-10035.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 10025-10035
    • Tugarinov, V.1    Muhandiram, R.2    Ayed, A.3    Kay, L.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.