메뉴 건너뛰기




Volumn 385, Issue 2, 2005, Pages 511-517

Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy

Author keywords

Candida rugosa lipase; Conformational stability; Heterologous protein glycosylation; Infrared spectroscopy; MS; Secondary structure

Indexed keywords

CONFORMATIONS; DATA ACQUISITION; FERMENTATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; THERMODYNAMIC STABILITY; X RAYS;

EID: 12844274977     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041296     Document Type: Article
Times cited : (171)

References (39)
  • 1
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mantsch, H. H. and Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry 32, 389-394
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 2
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo, J. L. R. and Goni, F. M. (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog. Biophys. Mol. Biol. 72, 367-405
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 3
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris, P. I. and Severcan, F. (1999) FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J. Mol. Catal. B Enzym. 7, 207-221
    • (1999) J. Mol. Catal. B Enzym. , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 4
    • 0028062558 scopus 로고
    • Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy
    • (Jones, C., Mulloy, B. and Thomas, A. H., eds.), Humana Press, Totowa, NJ
    • Haris, P. I. and Chapman, D. (1994) Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. In Methods in Molecular Biology, vol. 22: Microscopy, Optical Spectroscopy, and Macroscopic Techniques (Jones, C., Mulloy, B. and Thomas, A. H., eds.), pp. 183-202, Humana Press, Totowa, NJ
    • (1994) Methods in Molecular Biology, Vol. 22: Microscopy, Optical Spectroscopy, and Macroscopic Techniques , vol.22 , pp. 183-202
    • Haris, P.I.1    Chapman, D.2
  • 5
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi, H. and Byler, D. M. (1986) Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130, 291-311
    • (1986) Methods Enzymol. , vol.130 , pp. 291-311
    • Susi, H.1    Byler, D.M.2
  • 6
    • 0027354020 scopus 로고
    • Quantitative studies of the structures of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo, J. L. R., Muga, A., Castresana, J. and Goni, F. M. (1993) Quantitative studies of the structures of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59, 23-56
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 7
    • 0032479388 scopus 로고    scopus 로고
    • Upases: Interfacial enzymes with attractive applications
    • Schmid, R. D. and Verger, R. (1998) upases: interfacial enzymes with attractive applications. Angew. Chem. Int. Ed. 37, 1608-1633
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 1608-1633
    • Schmid, R.D.1    Verger, R.2
  • 8
    • 0031777548 scopus 로고    scopus 로고
    • Design, total synthesis and functional overexpression of the Candida rugosa gene coding for a major industrial lipase
    • Brocca, S., Schmidt-Dannert, C., Lotti, M., Alberghina, L. and Schmid, R. D. (1998) Design, total synthesis and functional overexpression of the Candida rugosa gene coding for a major industrial lipase. Protein Sci. 7, 1415-1422
    • (1998) Protein Sci. , vol.7 , pp. 1415-1422
    • Brocca, S.1    Schmidt-Dannert, C.2    Lotti, M.3    Alberghina, L.4    Schmid, R.D.5
  • 10
    • 0028103723 scopus 로고
    • Two conformational states of Candida rugosa lipase
    • Grochulski, P., Li, Y., Schrag, J. D. and Cygler, M. (1994) Two conformational states of Candida rugosa lipase. Protein Sci. 3, 82-91
    • (1994) Protein Sci. , vol.3 , pp. 82-91
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3    Cygler, M.4
  • 11
    • 0036228355 scopus 로고    scopus 로고
    • Conformational changes and orientation of Humicola lanuginosa lipase on solid hydrophobic surface: An in situ interface Fourier transform infrared-attenuated total reflection study
    • Noinville, S., Revault, M., Baron, M.-H., Tiss, A., Yapoudjian, S., Ivanova, M. and Verger, R. (2002) Conformational changes and orientation of Humicola lanuginosa lipase on solid hydrophobic surface: an in situ interface Fourier transform infrared-attenuated total reflection study. Biophys. J. 82, 2709-2719
    • (2002) Biophys. J. , vol.82 , pp. 2709-2719
    • Noinville, S.1    Revault, M.2    Baron, M.-H.3    Tiss, A.4    Yapoudjian, S.5    Ivanova, M.6    Verger, R.7
  • 12
    • 0345085739 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy study of dehydrated upases from Candida antarctica B and Pseudomonas cepacia
    • Vecchio, G., Zambianchi, F., Zacchetti, P., Secundo, F. and Carrea, G. (1999) Fourier-transform infrared spectroscopy study of dehydrated upases from Candida antarctica B and Pseudomonas cepacia. Biotechnol. Bioeng. 64, 545-551
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 545-551
    • Vecchio, G.1    Zambianchi, F.2    Zacchetti, P.3    Secundo, F.4    Carrea, G.5
  • 13
    • 0034663653 scopus 로고    scopus 로고
    • The esterase from thethermophilic eubacterium Bacillus acidocaldarius: Structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus tulgidus
    • D'Auria, S., Herman, P., Lakowicz, J. R., Tanfani, F., Bertoli, E., Manco, G. and Rossi, M. (2000) The esterase from thethermophilic eubacterium Bacillus acidocaldarius: structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus tulgidus. Proteins 40, 473-481
    • (2000) Proteins , vol.40 , pp. 473-481
    • D'Auria, S.1    Herman, P.2    Lakowicz, J.R.3    Tanfani, F.4    Bertoli, E.5    Manco, G.6    Rossi, M.7
  • 14
    • 0041562558 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy suggests unfolding of loop structures precedes complete unfolding of pig citrate synthase
    • Severcan, F. and Haris, P. I. (2003) Fourier transform infrared spectroscopy suggests unfolding of loop structures precedes complete unfolding of pig citrate synthase. Biopolymers 69, 440-447
    • (2003) Biopolymers , vol.69 , pp. 440-447
    • Severcan, F.1    Haris, P.I.2
  • 15
    • 0037335714 scopus 로고    scopus 로고
    • Pressure- and temperature-induce unfolding and aggregation of recombinant human interteron-γ: A Fourier transform infrared spectroscopy study
    • Goossens, K., Haelewyn, J., Meersman, F., De Ley, M. and Heremans, K. (2003) Pressure- and temperature-induce unfolding and aggregation of recombinant human interteron-γ: a Fourier transform infrared spectroscopy study. Biochem. J. 370, 529-535
    • (2003) Biochem. J. , vol.370 , pp. 529-535
    • Goossens, K.1    Haelewyn, J.2    Meersman, F.3    De Ley, M.4    Heremans, K.5
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0031150139 scopus 로고    scopus 로고
    • -1 range and quantitative infrared spectroscopy of aqueous solutions
    • -1 range and quantitative infrared spectroscopy of aqueous solutions. Anal. Biochem. 248, 234-245
    • (1997) Anal. Biochem. , vol.248 , pp. 234-245
    • Venyaminov, S.Y.1    Prendergast, F.G.2
  • 19
    • 0031070340 scopus 로고    scopus 로고
    • Infrared spectroscopy in aqueous solution: Difficulties and accuracy of water subtraction
    • Rahmelow, K. and Hubner, W. (1997) Infrared spectroscopy in aqueous solution: difficulties and accuracy of water subtraction. Appl. Spectrosc. 51, 160-170
    • (1997) Appl. Spectrosc. , vol.51 , pp. 160-170
    • Rahmelow, K.1    Hubner, W.2
  • 22
    • 0027281270 scopus 로고
    • Secondary structure and temperature behaviour of acetylcholinesterase studies by Fourier transform infrared spectroscopy
    • Görne-Tschelnokow, U., Naumann, D., Weise, C. and Hucho, F. (1993) Secondary structure and temperature behaviour of acetylcholinesterase studies by Fourier transform infrared spectroscopy. Eur. J. Biochem. 213, 1235-1242
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1235-1242
    • Görne-Tschelnokow, U.1    Naumann, D.2    Weise, C.3    Hucho, F.4
  • 23
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm, L. K. and Tatulian, S. A. (1997) Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 304, 365-429
    • (1997) Q. Rev. Biophys. , vol.304 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 24
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri, S., Khurana, R. and Fink, A. L. (1999) Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol. 309, 559-576
    • (1999) Methods Enzymol. , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 26
    • 0028916491 scopus 로고
    • A comparison of infrared spectra of proteins in solution and crystalline forms
    • Hadden, J. M., Chapman, D. and Lee, D. C. (1995) A comparison of infrared spectra of proteins in solution and crystalline forms. Biochim. Biophys. Acta 1248, 115-122
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 115-122
    • Hadden, J.M.1    Chapman, D.2    Lee, D.C.3
  • 27
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier transform infrared spectroscopy on hydrated films
    • Goormaghtigh, E., Cabiaux, V. and Ruysschaert, J. M. (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 193, 409-420
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 28
    • 0033898373 scopus 로고    scopus 로고
    • Secondary structure components and properties of the melibiose permease from Escherichia coli: A Fourier transform infrared spectroscopy analysis
    • Dave, N., Troullier, A., Mus-Veteau, I., Dunach, M., Leblanc, G. and Padros, E. (2000) Secondary structure components and properties of the melibiose permease from Escherichia coli: a Fourier transform infrared spectroscopy analysis. Biophys. J. 79, 747-755
    • (2000) Biophys. J. , vol.79 , pp. 747-755
    • Dave, N.1    Troullier, A.2    Mus-Veteau, I.3    Dunach, M.4    Leblanc, G.5    Padros, E.6
  • 29
    • 0031584275 scopus 로고    scopus 로고
    • Structural changes in a secretory phospholipase A2 induced by membrane binding: A clue to interfacial activation?
    • Tatulian, S. A., Biltonen, R. L. and Tamm, L. K. (1997) Structural changes in a secretory phospholipase A2 induced by membrane binding: a clue to interfacial activation? J. Mol. Biol. 268, 809-815
    • (1997) J. Mol. Biol. , vol.268 , pp. 809-815
    • Tatulian, S.A.1    Biltonen, R.L.2    Tamm, L.K.3
  • 31
    • 0031573469 scopus 로고    scopus 로고
    • Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution
    • Dong, A., Kendrick, B., Kreilgard, L., Matsuura, J., Manning, M. C. and Carpenter, J. F. (1997) Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution. Arch. Biochem. Biophys. 347, 213-220
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 213-220
    • Dong, A.1    Kendrick, B.2    Kreilgard, L.3    Matsuura, J.4    Manning, M.C.5    Carpenter, J.F.6
  • 32
    • 0030739097 scopus 로고    scopus 로고
    • Formation of stable polypeptide monolayers at interfaces: Controlling molecular conformation and orientation
    • Boncheva, M. and Vogel, H. (1997) Formation of stable polypeptide monolayers at interfaces: controlling molecular conformation and orientation. Biophys. J. 73, 1056-1072
    • (1997) Biophys. J. , vol.73 , pp. 1056-1072
    • Boncheva, M.1    Vogel, H.2
  • 33
    • 0028847040 scopus 로고
    • Lyophilization-induced reversible changes in the secondary structure of proteins
    • Griebenow, K. and Klibanov, A. M. (1995) Lyophilization-induced reversible changes in the secondary structure of proteins. Proc. Natl. Acad. Sci. U.S.A. 92, 10969-10976
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 34
    • 0034114845 scopus 로고    scopus 로고
    • Mutants provide evidence of the importance of glycosydic chains in the activation of lipase 1 from Candida rugosa
    • Brocca, S., Persson, M., Wehtje, E., Adlercreutz, P., Alberghina, L. and Lotti, M. (2000) Mutants provide evidence of the importance of glycosydic chains in the activation of lipase 1 from Candida rugosa. Protein Sci. 9, 985-990
    • (2000) Protein Sci. , vol.9 , pp. 985-990
    • Brocca, S.1    Persson, M.2    Wehtje, E.3    Adlercreutz, P.4    Alberghina, L.5    Lotti, M.6
  • 35
    • 0000823705 scopus 로고
    • High-level secretion of glycosylated invertase in the methylotrophic yeast Pichia pastoris
    • Tschopp, J. F., Sverlow, G., Kosson, R., Craig, W. and Grinna, L. (1987) High-level secretion of glycosylated invertase in the methylotrophic yeast Pichia pastoris. Bio/Technology 5, 1305-1308
    • (1987) Bio/Technology , vol.5 , pp. 1305-1308
    • Tschopp, J.F.1    Sverlow, G.2    Kosson, R.3    Craig, W.4    Grinna, L.5
  • 36
    • 0342538887 scopus 로고    scopus 로고
    • Developments in mid-infrared FT-IR spectroscopy of selected carbohydrates
    • Kacurakova, M. and Wilson, R. H. (2001) Developments in mid-infrared FT-IR spectroscopy of selected carbohydrates. Carbohydr. Polymers 44, 291-303
    • (2001) Carbohydr. Polymers , vol.44 , pp. 291-303
    • Kacurakova, M.1    Wilson, R.H.2
  • 37
    • 0035260294 scopus 로고    scopus 로고
    • Identification of protein-bound carbohydrates by mass spectrometry
    • Harvey, D. J. (2001) Identification of protein-bound carbohydrates by mass spectrometry. Proteomics 1, 311-328
    • (2001) Proteomics , vol.1 , pp. 311-328
    • Harvey, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.