메뉴 건너뛰기




Volumn 3, Issue 2, 2008, Pages 193-201

Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusionbodies

Author keywords

Fourier transform infrared spectroscopy; Inclusion bodies; Recombinant proteins; Solubility

Indexed keywords

INCLUSION BODY; POLYPETIDES; RECOMBINANT PROTEIN;

EID: 41049088527     PISSN: 18606768     EISSN: None     Source Type: Journal    
DOI: 10.1002/biot.200700238     Document Type: Review
Times cited : (73)

References (60)
  • 1
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx, F., Mujacic, M., Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399-1408.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 3
    • 0037071907 scopus 로고    scopus 로고
    • Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for their applicability in biotechnology
    • Schlieker, C., Bukau, B., Mogk, A., Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for their applicability in biotechnology. J. Biotechnol. 2002, 96, 13-21.
    • (2002) J. Biotechnol , vol.96 , pp. 13-21
    • Schlieker, C.1    Bukau, B.2    Mogk, A.3
  • 4
    • 2942755215 scopus 로고    scopus 로고
    • Stress induced by recombinant protein production in Escherichia coli
    • Hoffmann, F., Rinas, U., Stress induced by recombinant protein production in Escherichia coli. Adv. Biochem. Eng. Biotechnol. 2004, 89, 73-92.
    • (2004) Adv. Biochem. Eng. Biotechnol , vol.89 , pp. 73-92
    • Hoffmann, F.1    Rinas, U.2
  • 5
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: Biological role of inclusion bodies
    • Villaverde, A., Carrió, M. M., Protein aggregation in recombinant bacteria: Biological role of inclusion bodies. Biotechnol. Lett. 2003, 25, 1385-1395.
    • (2003) Biotechnol. Lett , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Carrió, M.M.2
  • 6
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion bodies composition
    • Speed, M. A., Wang D. I., King J., Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion bodies composition. Nat. Biotechnol. 1996, 14, 1283-1287.
    • (1996) Nat. Biotechnol , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.2    King, J.3
  • 7
    • 13644268136 scopus 로고    scopus 로고
    • Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins
    • Vallejo, L. F., Rinas, U., Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins. Microb. Cell Fact. 2004, 3, 11.
    • (2004) Microb. Cell Fact , vol.3 , pp. 11
    • Vallejo, L.F.1    Rinas, U.2
  • 8
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • Clark, E. D., Protein refolding for industrial processes. Curr. Opin. Biotechnol. 2001, 12, 202-207.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 202-207
    • Clark, E.D.1
  • 9
    • 25444461690 scopus 로고    scopus 로고
    • How to find soluble proteins: A comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli. BCM
    • Koschorreck, M., Fischer, M., Barth, S., Pleiss, J., How to find soluble proteins: A comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli. BCM Genomics 2005, 6, 49.
    • (2005) Genomics , vol.6 , pp. 49
    • Koschorreck, M.1    Fischer, M.2    Barth, S.3    Pleiss, J.4
  • 10
    • 13644262805 scopus 로고    scopus 로고
    • Sørensen, H. P., Mortensen, K. K., Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell. Fact. 2005, 4, 1.
    • Sørensen, H. P., Mortensen, K. K., Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell. Fact. 2005, 4, 1.
  • 11
    • 29244442950 scopus 로고    scopus 로고
    • Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors
    • Dummler, A., Lawrence, A. M., de Marco, A., Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors. Microb. Cell Fact. 2005, 4, 34.
    • (2005) Microb. Cell Fact , vol.4 , pp. 34
    • Dummler, A.1    Lawrence, A.M.2    de Marco, A.3
  • 12
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh, D. S., Making the most of affinity tags. Trends Biotechnol. 2005, 23, 316-320.
    • (2005) Trends Biotechnol , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 13
    • 1842582929 scopus 로고    scopus 로고
    • Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning
    • De Marco, A., De Marco, V., Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J. Biotechnol. 2004, 109, 45-52.
    • (2004) J. Biotechnol , vol.109 , pp. 45-52
    • De Marco, A.1    De Marco, V.2
  • 14
    • 29144469368 scopus 로고    scopus 로고
    • Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolites, plasmid- or benzyl alcohol-over-expressed molecular chaperones
    • De Marco, A., Vigh, L., Diamant, S., Goloubinoff, P., Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolites, plasmid- or benzyl alcohol-over-expressed molecular chaperones. Cell Stress Chaperones 2005, 10, 329-339.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 329-339
    • De Marco, A.1    Vigh, L.2    Diamant, S.3    Goloubinoff, P.4
  • 16
    • 26844498710 scopus 로고    scopus 로고
    • Sequence determinants of protein aggregation: Tools to increase protein solubility
    • Ventura, S., Sequence determinants of protein aggregation: Tools to increase protein solubility. Microb. Cell Fact. 2005, 4, 11.
    • (2005) Microb. Cell Fact , vol.4 , pp. 11
    • Ventura, S.1
  • 17
    • 0037029006 scopus 로고    scopus 로고
    • Influence of backbone conformation on protein aggregation
    • Srisailam, S., Kumar, T. K., Srimathi, T., Yu, C., Influence of backbone conformation on protein aggregation. J. Am. Chem. Soc. 2002, 124, 1884-1888.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 1884-1888
    • Srisailam, S.1    Kumar, T.K.2    Srimathi, T.3    Yu, C.4
  • 18
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A., M., Rousseau, F., Schymkowitz, J., Serrano, L., Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22, 1302-1306.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 19
    • 4143133235 scopus 로고    scopus 로고
    • A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins
    • Linding, R., Schymkowitz, J., Rousseau, F, Diella, F., Serrano, L., A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. J. Mol. Biol. 2004, 342, 345-353.
    • (2004) J. Mol. Biol , vol.342 , pp. 345-353
    • Linding, R.1    Schymkowitz, J.2    Rousseau, F.3    Diella, F.4    Serrano, L.5
  • 20
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti, F, Stefani, M., Taddei, N., Ramponi, G., Dobson, C. M., Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003, 424, 805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 21
    • 0034616258 scopus 로고    scopus 로고
    • Fine architecture of bacterial inclusion bodies
    • Carrió, M. M., Cubarsi, R., Villaverde, A., Fine architecture of bacterial inclusion bodies. FEBS Lett. 2000, 471, 7-11.
    • (2000) FEBS Lett , vol.471 , pp. 7-11
    • Carrió, M.M.1    Cubarsi, R.2    Villaverde, A.3
  • 22
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • Carrió, M. M., Villaverde, A., Construction and deconstruction of bacterial inclusion bodies. J. Biotechnol. 2002, 96, 3-12.
    • (2002) J. Biotechnol , vol.96 , pp. 3-12
    • Carrió, M.M.1    Villaverde, A.2
  • 23
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones
    • Ben-Zvi, A., De Los Rios, P., Dietler, G., Goloubinoff, P., Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones. J. Biol. Chem. 2004, 279, 37298-37303.
    • (2004) J. Biol. Chem , vol.279 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 24
    • 33646557371 scopus 로고    scopus 로고
    • Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling
    • De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A., Goloubinoff, P., Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl. Acad. Sci. USA 2006, 103, 6166-6171.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6166-6171
    • De Los Rios, P.1    Ben-Zvi, A.2    Slutsky, O.3    Azem, A.4    Goloubinoff, P.5
  • 25
    • 0028260192 scopus 로고
    • Native-like secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR
    • Oberg, K., Chrunyk, B. A., Wetzel, R., Fink. A. L., Native-like secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry 1994, 33, 2628-2634.
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 26
    • 33646589053 scopus 로고    scopus 로고
    • Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy
    • Ami, D., Natalello, A., Taylor, G., Tonon, G., Doglia, S. M., Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy. Biochim. Biophys. Acta 2006, 1764, 793-799.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 793-799
    • Ami, D.1    Natalello, A.2    Taylor, G.3    Tonon, G.4    Doglia, S.M.5
  • 27
    • 0025921901 scopus 로고
    • High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D
    • Tokatlidis, K., Dhurjati, P., Millet, J., Beguin, P., Aubert, J. P., High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBS Lett. 1991, 282, 205-208.
    • (1991) FEBS Lett , vol.282 , pp. 205-208
    • Tokatlidis, K.1    Dhurjati, P.2    Millet, J.3    Beguin, P.4    Aubert, J.P.5
  • 28
    • 34247516876 scopus 로고    scopus 로고
    • The conformational quality of insoluble recombinant proteins is enhanced at low growth temperature
    • Vera, A., Gonzáles-Montalbán, N., Arís, A., Villaverde, A., The conformational quality of insoluble recombinant proteins is enhanced at low growth temperature. Biotechnol. Bioeng. 2007, 96, 1101-1106.
    • (2007) Biotechnol. Bioeng , vol.96 , pp. 1101-1106
    • Vera, A.1    Gonzáles-Montalbán, N.2    Arís, A.3    Villaverde, A.4
  • 29
    • 26844569776 scopus 로고    scopus 로고
    • Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
    • Garcia-Fruitos, E., Gonzàlez-Montalbàn, N., Morell, M., Vera, A. et al., Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb. Cell Fact. 2005, 4, 27.
    • (2005) Microb. Cell Fact , vol.4 , pp. 27
    • Garcia-Fruitos, E.1    Gonzàlez-Montalbàn, N.2    Morell, M.3    Vera, A.4
  • 30
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • De Marco, A., Schrödel, A., Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem. 2005, 6, 10.
    • (2005) BMC Biochem , vol.6 , pp. 10
    • De Marco, A.1    Schrödel, A.2
  • 31
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura, S., Villaverde, A., Protein quality in bacterial inclusion bodies. Trends Biotech. 2006, 24, 179-185.
    • (2006) Trends Biotech , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 32
    • 33748132184 scopus 로고    scopus 로고
    • The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells
    • Gonzàlez-Montalbàn, N., Garcia-Fruitos, E., Ventura, S., Aris, A., Villaverde, A., The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microb. Cell Fact. 2006, 5, 26.
    • (2006) Microb. Cell Fact , vol.5 , pp. 26
    • Gonzàlez-Montalbàn, N.1    Garcia-Fruitos, E.2    Ventura, S.3    Aris, A.4    Villaverde, A.5
  • 34
    • 35348948549 scopus 로고    scopus 로고
    • Divergent genetic control of protein solubility and conformational quality in Escherichia coli
    • Garcia-Fruitos, E., Martinez-Alonso, M., Gonzàlez-Montalbàn, N., Valli, M. et al., Divergent genetic control of protein solubility and conformational quality in Escherichia coli. J. Mol. Biol. 2007, 374, 195-205.
    • (2007) J. Mol. Biol , vol.374 , pp. 195-205
    • Garcia-Fruitos, E.1    Martinez-Alonso, M.2    Gonzàlez-Montalbàn, N.3    Valli, M.4
  • 35
    • 16344363078 scopus 로고    scopus 로고
    • Production of nonclassical inclusion bodies from which correctly folded protein can be extracted
    • Jevsevar, S., Gaberc-Porekar, V., Fonda, I., Podobnik, B. et al., Production of nonclassical inclusion bodies from which correctly folded protein can be extracted. Biotechnol. Prog. 2005, 21, 632-639.
    • (2005) Biotechnol. Prog , vol.21 , pp. 632-639
    • Jevsevar, S.1    Gaberc-Porekar, V.2    Fonda, I.3    Podobnik, B.4
  • 36
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh, S. M., Panda, A. K., Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 2005, 99, 303-310.
    • (2005) J. Biosci. Bioeng , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 39
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson, M. R., Techniques to study amyloid fibril formation in vitro. Methods 2004, 34, 151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 40
    • 33645704194 scopus 로고    scopus 로고
    • Methods for measuring protein aggregation
    • Bondos, S. E., Methods for measuring protein aggregation. Curr. Anal. Chem. 2006, 2, 157-170.
    • (2006) Curr. Anal. Chem , vol.2 , pp. 157-170
    • Bondos, S.E.1
  • 41
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo, J. L. R., Goni, F. M., Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog. Biophys. Mol. Biol. 1999, 72, 367-405.
    • (1999) Prog. Biophys. Mol. Biol , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 42
    • 0025357111 scopus 로고
    • Protein secondary structures in water from 2nd-derivative amide-I infrared spectra
    • Dong, A., Huang, P., Caughey, W. S., Protein secondary structures in water from 2nd-derivative amide-I infrared spectra. Biochemistry 1990, 29, 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 43
    • 12844274977 scopus 로고    scopus 로고
    • Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    • Natalello, A., Ami, D., Brocca, S., Lotti, M., Doglia, S. M., Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy. Biochem. J. 2005, 385, 511-517.
    • (2005) Biochem. J , vol.385 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3    Lotti, M.4    Doglia, S.M.5
  • 44
    • 0344395589 scopus 로고    scopus 로고
    • FT-IR study of heterologous protein expression in recombinant Escherichia coli strains
    • Ami, D., Bonecchi, L., Calì, S., Orsini, G., Tonon, G., Doglia, S. M., FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim. Biophys. Acta 2003, 1624, 6-10.
    • (2003) Biochim. Biophys. Acta , vol.1624 , pp. 6-10
    • Ami, D.1    Bonecchi, L.2    Calì, S.3    Orsini, G.4    Tonon, G.5    Doglia, S.M.6
  • 45
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • Ami, D., Natalello, A., Gatti Lafranconi, P., Lotti, M., Doglia, S. M., Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy.FEBS Lett. 2005, 579, 3433-3436.
    • (2005) FEBS Lett , vol.579 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti Lafranconi, P.3    Lotti, M.4    Doglia, S.M.5
  • 46
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth, A., Zscherp, C., What vibrations tell us about proteins. Q. Rev. Biophys. 2002, 35, 369-430.
    • (2002) Q. Rev. Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 47
    • 41149085398 scopus 로고    scopus 로고
    • Natalello, A., Ami, D., Doglia, S. M., Protein aggregation studied in intact cells by Fourier transform infrared spectroscopy. In: Uversky, V. N., Permyakov, A. E. (Eds.). Methods in Protein Structure and Stability Analysis: Vibrational Spectroscopy, Nova Science. Hauppauge 2007, pp. 249-265.
    • Natalello, A., Ami, D., Doglia, S. M., Protein aggregation studied in intact cells by Fourier transform infrared spectroscopy. In: Uversky, V. N., Permyakov, A. E. (Eds.). Methods in Protein Structure and Stability Analysis: Vibrational Spectroscopy, Nova Science. Hauppauge 2007, pp. 249-265.
  • 48
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F,. Dobson, C. M., Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 49
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., Fandrich, M., FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Sci. 2004, 13, 3314-3321.
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fandrich, M.4
  • 50
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri, S., Khurana, R., Fink, A. L., Fourier transform infrared spectroscopy in analysis of protein deposits. Method Enzymol. 1999, 309, 559-576.
    • (1999) Method Enzymol , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 51
    • 6344287936 scopus 로고    scopus 로고
    • Fourier transform infrared microspectroscopy as a new tool for nematode studies
    • Ami, D., Natalello, A., Zullini, A., Doglia, S. M., Fourier transform infrared microspectroscopy as a new tool for nematode studies. FEBS Lett. 2004, 576, 297-300.
    • (2004) FEBS Lett , vol.576 , pp. 297-300
    • Ami, D.1    Natalello, A.2    Zullini, A.3    Doglia, S.M.4
  • 52
    • 38049077453 scopus 로고    scopus 로고
    • Embryonic stem cell differentiation studied by FT-IR spectroscopy
    • in press, DOI:10.1016/j.bbam-cr.2007.08.003
    • Ami, D., Neri, T., Natalello, A., Mereghetti, P. et al., Embryonic stem cell differentiation studied by FT-IR spectroscopy. Biochim. Biophys. Acta 2007 (in press). DOI:10.1016/j.bbam-cr.2007.08.003.
    • (2007) Biochim. Biophys. Acta
    • Ami, D.1    Neri, T.2    Natalello, A.3    Mereghetti, P.4
  • 53
    • 0026413442 scopus 로고
    • Microbiological characterizations by FT-IR spectroscopy
    • Naumann, D., Helm, D., Labischinski, H., Microbiological characterizations by FT-IR spectroscopy. Nature 1991, 351, 81-82.
    • (1991) Nature , vol.351 , pp. 81-82
    • Naumann, D.1    Helm, D.2    Labischinski, H.3
  • 54
    • 0010872598 scopus 로고
    • Infrared spectroscopic characterization of Alzheimer plaques
    • Fabian, H., Choo, L. P., Szendrei, G. I., Jackson, M. et al., Infrared spectroscopic characterization of Alzheimer plaques. Appl. Spectrosc. 1993, 47, 1513-1518.
    • (1993) Appl. Spectrosc , vol.47 , pp. 1513-1518
    • Fabian, H.1    Choo, L.P.2    Szendrei, G.I.3    Jackson, M.4
  • 55
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy
    • Choo, L. P., Wetzel, D. L., Halliday, W. C., Jackson, M. et al., In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy. Biophys. J. 1996, 71, 1672-1679.
    • (1996) Biophys. J , vol.71 , pp. 1672-1679
    • Choo, L.P.1    Wetzel, D.L.2    Halliday, W.C.3    Jackson, M.4
  • 56
    • 33747351061 scopus 로고    scopus 로고
    • FTIR-microspectroscopy of prion-infected nervous tissue
    • Kretlow, A., Wang, Q., Kneipp, J., Lasch, P. et al., FTIR-microspectroscopy of prion-infected nervous tissue. Biochim. Biophys. Acta 2006, 1758, 948-959.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 948-959
    • Kretlow, A.1    Wang, Q.2    Kneipp, J.3    Lasch, P.4
  • 57
    • 34250351307 scopus 로고    scopus 로고
    • Fast quantification of recombinant protein inclusion bodies within intact cells by FT-IR spectroscopy
    • Gross-Selbeck, S., Margreiter, G., Obinger, C., Bayer, K., Fast quantification of recombinant protein inclusion bodies within intact cells by FT-IR spectroscopy. Biotechnol. Prog. 2007, 23, 762-766.
    • (2007) Biotechnol. Prog , vol.23 , pp. 762-766
    • Gross-Selbeck, S.1    Margreiter, G.2    Obinger, C.3    Bayer, K.4
  • 58
    • 0033795976 scopus 로고    scopus 로고
    • FT-IR microspectroscopy for microbiological studies
    • Orsini, F., Ami, D., Villa, A. M., Sala, G. et al., FT-IR microspectroscopy for microbiological studies. J. Microbiol. Methods 2000, 42, 17-27.
    • (2000) J. Microbiol. Methods , vol.42 , pp. 17-27
    • Orsini, F.1    Ami, D.2    Villa, A.M.3    Sala, G.4
  • 59
    • 12844284637 scopus 로고    scopus 로고
    • Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by L-arginine
    • Umetsu, M., Tsumoto, K., Nitta, S., Adschiri, T. et al., Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by L-arginine. Biochem. Biophys. Res. Commun. 2005, 328, 189-197.
    • (2005) Biochem. Biophys. Res. Commun , vol.328 , pp. 189-197
    • Umetsu, M.1    Tsumoto, K.2    Nitta, S.3    Adschiri, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.