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Volumn 373, Issue 1, 2008, Pages 164-166

15N isotope labeling of a protein secreted by Brevibacillus choshinensis for NMR study

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BIOCHEMISTRY;

EID: 37049010948     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.10.011     Document Type: Article
Times cited : (9)

References (20)
  • 3
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto N.K., and Kay L.E. New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol. 10 (2000) 585-592
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 4
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson W.A., Horton J.R., and LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J. 9 (1990) 1665-1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 5
    • 0028774540 scopus 로고
    • Expression of highly disulfide-bonded proteins in Pichia pastoris
    • White C.E., Kempi N.M., and Komives E.A. Expression of highly disulfide-bonded proteins in Pichia pastoris. Structure 2 (1994) 1003-1005
    • (1994) Structure , vol.2 , pp. 1003-1005
    • White, C.E.1    Kempi, N.M.2    Komives, E.A.3
  • 7
    • 0038386883 scopus 로고    scopus 로고
    • Amino-acid-type selective isotope labeling of proteins expressed in baculovirus-infected insect cells useful for NMR studies
    • Strauss A., Bitsch F., Cutting B., Fendrich G., Graff P., Liebetanz J., Zurini M., and Jahnke W. Amino-acid-type selective isotope labeling of proteins expressed in baculovirus-infected insect cells useful for NMR studies. J. Biomol. NMR 26 (2003) 367-372
    • (2003) J. Biomol. NMR , vol.26 , pp. 367-372
    • Strauss, A.1    Bitsch, F.2    Cutting, B.3    Fendrich, G.4    Graff, P.5    Liebetanz, J.6    Zurini, M.7    Jahnke, W.8
  • 8
    • 30344446652 scopus 로고    scopus 로고
    • Preparation of amino-acid-type selective isotope labeling of protein expressed in Pichia pastoris
    • Chen C.Y., Cheng C.H., Chen Y.C., Lee J.C., Chou S.H., Huang W., and Chuang W.J. Preparation of amino-acid-type selective isotope labeling of protein expressed in Pichia pastoris. Proteins 62 (2006) 279-287
    • (2006) Proteins , vol.62 , pp. 279-287
    • Chen, C.Y.1    Cheng, C.H.2    Chen, Y.C.3    Lee, J.C.4    Chou, S.H.5    Huang, W.6    Chuang, W.J.7
  • 9
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • Kigawa T., Muto Y., and Yokoyama S. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J. Biomol. NMR 6 (1995) 129-134
    • (1995) J. Biomol. NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 11
    • 0038583721 scopus 로고    scopus 로고
    • A wheat germ cell-free system is a novel way to screen protein folding and function
    • Morita E.H., Sawasaki T., Tanaka R., Endo Y., and Kohno T. A wheat germ cell-free system is a novel way to screen protein folding and function. Protein Sci. 12 (2003) 1216-1221
    • (2003) Protein Sci. , vol.12 , pp. 1216-1221
    • Morita, E.H.1    Sawasaki, T.2    Tanaka, R.3    Endo, Y.4    Kohno, T.5
  • 12
    • 0027297667 scopus 로고
    • High-level secretion of heterologous proteins by Bacillus brevis
    • Udaka S., and Yamagata H. High-level secretion of heterologous proteins by Bacillus brevis. Methods Enzymol. 217 (1993) 23-33
    • (1993) Methods Enzymol. , vol.217 , pp. 23-33
    • Udaka, S.1    Yamagata, H.2
  • 14
    • 0033217254 scopus 로고    scopus 로고
    • Structural conversion from non-native to native form of recombinant human epidermal growth factor by Brevibacillus choshinensis
    • Miyauchi A., Ozawa M., Mizukami M., Yashiro K., Ebisu S., Tojo T., Fujii T., and Takagi H. Structural conversion from non-native to native form of recombinant human epidermal growth factor by Brevibacillus choshinensis. Biosci. Biotechnol. Biochem. 63 (1999) 1965-1969
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1965-1969
    • Miyauchi, A.1    Ozawa, M.2    Mizukami, M.3    Yashiro, K.4    Ebisu, S.5    Tojo, T.6    Fujii, T.7    Takagi, H.8
  • 15
    • 0038061502 scopus 로고    scopus 로고
    • Cloning and expression of the ccdA-associated thiol-disulfide oxidoreductase (catA) gene from Brevibacillus choshinensis: Stimulation of human epidermal growth factor production
    • Tanaka R., Mizukami M., Ishibashi M., Tokunaga H., and Tokunaga M. Cloning and expression of the ccdA-associated thiol-disulfide oxidoreductase (catA) gene from Brevibacillus choshinensis: Stimulation of human epidermal growth factor production. J. Biotechnol. 103 (2003) 1-10
    • (2003) J. Biotechnol. , vol.103 , pp. 1-10
    • Tanaka, R.1    Mizukami, M.2    Ishibashi, M.3    Tokunaga, H.4    Tokunaga, M.5
  • 18
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: A multifaceted approach to macromolecular structure
    • Ferentz A.E., and Wagner G. NMR spectroscopy: A multifaceted approach to macromolecular structure. Q. Rev. Biophys. 33 (2000) 29-65
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 19
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A., and Grzesiek S. Methodological advances in protein NMR. Acc. Chem. Res. 26 (1993) 131-138
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 20
    • 0034723142 scopus 로고    scopus 로고
    • X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies
    • Burkhard P., Taylor P., and Walkinshaw M.D. X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies. J. Mol. Biol. 295 (2000) 953-962
    • (2000) J. Mol. Biol. , vol.295 , pp. 953-962
    • Burkhard, P.1    Taylor, P.2    Walkinshaw, M.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.