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Volumn 330, Issue 5, 2003, Pages 1153-1164

Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein - A static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study

Author keywords

FT IR; GFP; High pressure; Protein folding; Red shifted green fluorescent protein

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 0038690115     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00657-0     Document Type: Article
Times cited : (93)

References (55)
  • 1
    • 0029969436 scopus 로고    scopus 로고
    • Use of green fluorescent protein for detection of cell specific gene expression and subcellular protein localization during sporulation in Bacillus subtilis
    • Lewis P.J., Errington J. Use of green fluorescent protein for detection of cell specific gene expression and subcellular protein localization during sporulation in Bacillus subtilis. Microbiology. 142:1996;733-740.
    • (1996) Microbiology , vol.142 , pp. 733-740
    • Lewis, P.J.1    Errington, J.2
  • 2
    • 0029815312 scopus 로고    scopus 로고
    • The Bacillus subtilis soj-spo0J locus is required for a centromere-like function involved in prespore chromosome partitioning
    • Sharpe M.E., Errington J. The Bacillus subtilis soj-spo0J locus is required for a centromere-like function involved in prespore chromosome partitioning. Mol. Microbiol. 21:1996;501-509.
    • (1996) Mol. Microbiol. , vol.21 , pp. 501-509
    • Sharpe, M.E.1    Errington, J.2
  • 3
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., Prasher D.C. Green fluorescent protein as a marker for gene expression. Science. 263:1994;802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 4
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein
    • Cormack B.P., Valdivia R.H., Falkow S. FACS-optimized mutants of the green fluorescent protein. Gene. 173:1996;33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 5
    • 0002587779 scopus 로고    scopus 로고
    • Use of the A. victoria green fluorescent protein to study protein dynamics in vivo
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.E. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: Wiley
    • Kahana J.A., Silver P.A. Use of the A. victoria green fluorescent protein to study protein dynamics in vivo. Ausubel F.M., Brent R., Kingston R.E., Moore D.E., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. 1996;9.6.13-9.6.19 Wiley, New York.
    • (1996) Current Protocols in Molecular Biology , pp. 9613-9619
    • Kahana, J.A.1    Silver, P.A.2
  • 6
    • 0030069686 scopus 로고    scopus 로고
    • In vivo examination of membrane protein localization and degradation with the green fluorescent protein
    • Hampton R.Y., Koning A., Wright R., Rine J. In vivo examination of membrane protein localization and degradation with the green fluorescent protein. Proc. Natl Acad. Sci. USA. 93:1996;828-833.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 828-833
    • Hampton, R.Y.1    Koning, A.2    Wright, R.3    Rine, J.4
  • 7
    • 0029943554 scopus 로고    scopus 로고
    • Green fluorescent protein and its derivatives as versatile markers for gene expression in living Drosophila melanogaster
    • Plautz J.D., Day R.N., Dailey G.M., Welsh S.B., Hall J.C., Halpain S., Kay S.A. Green fluorescent protein and its derivatives as versatile markers for gene expression in living Drosophila melanogaster. Gene. 173:1996;83-87.
    • (1996) Gene , vol.173 , pp. 83-87
    • Plautz, J.D.1    Day, R.N.2    Dailey, G.M.3    Welsh, S.B.4    Hall, J.C.5    Halpain, S.6    Kay, S.A.7
  • 8
    • 0031281917 scopus 로고    scopus 로고
    • GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila
    • Edward K.A., Demsky M., Montague R.A., Weymouth N., Kiehart D.P. GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila. Dev. Biol. 191:1997;103-117.
    • (1997) Dev. Biol. , vol.191 , pp. 103-117
    • Edward, K.A.1    Demsky, M.2    Montague, R.A.3    Weymouth, N.4    Kiehart, D.P.5
  • 9
    • 0001141671 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive stress probe in resting Escherichia coli cells
    • Cha H.J., Srivastava R., Vakharia V.N., Rao G., Bentley W.B. Green fluorescent protein as a noninvasive stress probe in resting Escherichia coli cells. Appl. Environ. Microbiol. 65:1999;409-414.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 409-414
    • Cha, H.J.1    Srivastava, R.2    Vakharia, V.N.3    Rao, G.4    Bentley, W.B.5
  • 11
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67:1998;509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 13
    • 0035075272 scopus 로고    scopus 로고
    • In-vitro stability and expression of green fluorescent protein under high pressure conditions
    • Ehrmann M.A., Scheyhing C.H., Vogel R.F. In-vitro stability and expression of green fluorescent protein under high pressure conditions. Letters Appl. Microbiol. 32:2001;230-234.
    • (2001) Letters Appl. Microbiol. , vol.32 , pp. 230-234
    • Ehrmann, M.A.1    Scheyhing, C.H.2    Vogel, R.F.3
  • 14
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F., Moss L.G., Phillips G.N. Jr. The molecular structure of green fluorescent protein. Nature Biotechnol. 4:1996;1246-1251.
    • (1996) Nature Biotechnol. , vol.4 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips G.N., Jr.3
  • 17
    • 0032374089 scopus 로고    scopus 로고
    • Characterization of the photoconversion of green fluorescent protein with FT-IR spectroscopy
    • Van Thor J.J., Pierik A.J., Nugteren-Roodzant I., Xie A., Hellingwerf K.J. Characterization of the photoconversion of green fluorescent protein with FT-IR spectroscopy. Biochemistry. 37:1998;16915-16921.
    • (1998) Biochemistry , vol.37 , pp. 16915-16921
    • Van Thor, J.J.1    Pierik, A.J.2    Nugteren-Roodzant, I.3    Xie, A.4    Hellingwerf, K.J.5
  • 19
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K., Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta. 1386:1998;353-370.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 20
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter R. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Biochim. Biophys. Acta. 1595:2002;160-184.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 160-184
    • Winter, R.1
  • 21
    • 0003988003 scopus 로고    scopus 로고
    • R. Winter, & J. Jonas. Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Winter R., Jonas J. High Pressure Molecular Science, NATO ASI E 358. 1999;Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1999) High Pressure Molecular Science, NATO ASI E 358
  • 22
    • 0037171122 scopus 로고    scopus 로고
    • High pressure effects on biological macromolecules: From structural changes to alteration of cellular processes
    • Balny C., Masson P., Heremans K. High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes. Biochim. Biophys. Acta. 1595:2002;3-10.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 3-10
    • Balny, C.1    Masson, P.2    Heremans, K.3
  • 23
    • 0032536156 scopus 로고    scopus 로고
    • Structure characterization of the pressure-unfolded state of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy
    • Panick G., Malessa R., Winter R., Rapp G., Frye K.J., Royer C.A. Structure characterization of the pressure-unfolded state of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy. J. Mol. Biol. 275:1998;389-402.
    • (1998) J. Mol. Biol. , vol.275 , pp. 389-402
    • Panick, G.1    Malessa, R.2    Winter, R.3    Rapp, G.4    Frye, K.J.5    Royer, C.A.6
  • 25
    • 0034700971 scopus 로고    scopus 로고
    • Pressure-induced unfolding/refolding of ribonuclease A: Static and kinetic Fourier transform infrared spectroscopy study
    • Panick G., Winter R. Pressure-induced unfolding/refolding of ribonuclease A: static and kinetic Fourier transform infrared spectroscopy study. Biochemistry. 39:2000;1862-1869.
    • (2000) Biochemistry , vol.39 , pp. 1862-1869
    • Panick, G.1    Winter, R.2
  • 26
    • 0033531967 scopus 로고    scopus 로고
    • Pressure-jump studies of the folding/unfolding of trp repressor
    • Desai G., Panick G., Zein M., Winter R., Royer C.A. Pressure-jump studies of the folding/unfolding of trp repressor. J. Mol. Biol. 288:1999;461-475.
    • (1999) J. Mol. Biol. , vol.288 , pp. 461-475
    • Desai, G.1    Panick, G.2    Zein, M.3    Winter, R.4    Royer, C.A.5
  • 27
    • 0037133197 scopus 로고    scopus 로고
    • Temperature- and pressure-induced unfolding and refolding of ubiquitin: A static and kinetic Fourier transform infrared spectroscopy study
    • Herberhold H., Winter R. Temperature- and pressure-induced unfolding and refolding of ubiquitin: a static and kinetic Fourier transform infrared spectroscopy study. Biochemistry. 41:2002;2396-2401.
    • (2002) Biochemistry , vol.41 , pp. 2396-2401
    • Herberhold, H.1    Winter, R.2
  • 28
    • 0029915110 scopus 로고    scopus 로고
    • Conformation of bovine pancreatic trypsin inhibitor studied by Fourier transform infrared spectroscopy
    • Goossens K., Smeller L., Frank J., Heremans K. Conformation of bovine pancreatic trypsin inhibitor studied by Fourier transform infrared spectroscopy. Eur. J. Biochem. 236:1996;254-262.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 254-262
    • Goossens, K.1    Smeller, L.2    Frank, J.3    Heremans, K.4
  • 29
    • 0037111322 scopus 로고    scopus 로고
    • Temperature-pressure stability of green fluorescent protein: A Fourier transform infrared spectroscopy study
    • Scheyhing C.H., Meersman F., Ehrmann M.A., Heremans K., Vogel R.F. Temperature-pressure stability of green fluorescent protein: a Fourier transform infrared spectroscopy study. Biopolymers. 65:2003;244-253.
    • (2003) Biopolymers , vol.65 , pp. 244-253
    • Scheyhing, C.H.1    Meersman, F.2    Ehrmann, M.A.3    Heremans, K.4    Vogel, R.F.5
  • 30
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley S.A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry. 10:1971;2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 32
    • 0028220701 scopus 로고
    • Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M., Jaenicke R. Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221:1994;617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 33
    • 0028905560 scopus 로고
    • Evidence for a molten globule-like transition state in protein folding from determination of activation volumes
    • Vidugiris G.J.A., Markley J.L., Royer C.A. Evidence for a molten globule-like transition state in protein folding from determination of activation volumes. Biochemistry. 34:1995;4909-4912.
    • (1995) Biochemistry , vol.34 , pp. 4909-4912
    • Vidugiris, G.J.A.1    Markley, J.L.2    Royer, C.A.3
  • 35
    • 0035399676 scopus 로고    scopus 로고
    • Absorption spectra of the GFP chromophore in solution: Comparison of theoretical and experimental results
    • Voityuk A.A., Kummer A.D., Michel-Beyerle M.-E., Rösch N. Absorption spectra of the GFP chromophore in solution: comparison of theoretical and experimental results. Chem. Phys. 269:2001;83-91.
    • (2001) Chem. Phys. , vol.269 , pp. 83-91
    • Voityuk, A.A.1    Kummer, A.D.2    Michel-Beyerle, M.-E.3    Rösch, N.4
  • 36
    • 0037171141 scopus 로고    scopus 로고
    • UV-visible derivative spectroscopy under high pressure
    • Lange R., Balny C. UV-visible derivative spectroscopy under high pressure. Biochim. Biophys. Acta. 1595:2002;80-93.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 80-93
    • Lange, R.1    Balny, C.2
  • 37
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta. 1595:2002;201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 39
    • 0030781508 scopus 로고    scopus 로고
    • Extreme heat- and pressure-resistant 7-kDa protein P2 from the Archeon Sulfolobus solfataricus is dramatically destabilized by a single-point amino acid substitution
    • Fusi P., Goossens K., Consonni R., Grisa M., Puricelli P., Vecchio G., et al. Extreme heat- and pressure-resistant 7-kDa protein P2 from the Archeon Sulfolobus solfataricus is dramatically destabilized by a single-point amino acid substitution. Proteins: Struct. Funct. Genet. 29:1997;381-390.
    • (1997) Proteins: Struct. Funct. Genet. , vol.29 , pp. 381-390
    • Fusi, P.1    Goossens, K.2    Consonni, R.3    Grisa, M.4    Puricelli, P.5    Vecchio, G.6
  • 40
    • 0037390283 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cubic monoolein mesophases: The effects of concentration, temperature and pressure
    • Lendermann, J. & Winter, R. (2003). Interaction of cytochrome c with cubic monoolein mesophases: the effects of concentration, temperature and pressure. Phys. Chem. Chem. Phys. 5, 1440-1450.
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 1440-1450
    • Lendermann, J.1    Winter, R.2
  • 41
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G., Garde S., García A.E., Paulaitis M.E., Pratt L.R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl Acad. Sci. USA. 95:1998;1552-1555.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    García, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 42
    • 0035823844 scopus 로고    scopus 로고
    • Molecular dynamics simulations of pressure effects on hydrophobic interactions
    • Ghosh T., García A.E., Garde S. Molecular dynamics simulations of pressure effects on hydrophobic interactions. J. Am. Chem. Soc. 123:2001;10997-11003.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10997-11003
    • Ghosh, T.1    García, A.E.2    Garde, S.3
  • 43
    • 0003903343 scopus 로고
    • J. Sambrook, E.F. Fritsch, & T. Maniatis. Cold Spring Harbor, NY: Cold Spring Habor Laboratory Press
    • Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning - A Laboratory Manual. 2nd edit. 1989;Cold Spring Habor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning - A Laboratory Manual 2nd edit.
  • 45
    • 0029347056 scopus 로고
    • Rapid purification of recombinant green fluorescent protein using hydrophobic properties of an HPLC size-exclusion column
    • Deschamps J.R., Miller C.E., Ward K.B. Rapid purification of recombinant green fluorescent protein using hydrophobic properties of an HPLC size-exclusion column. Protein Express. Purif. 6:1995;555-558.
    • (1995) Protein Express. Purif. , vol.6 , pp. 555-558
    • Deschamps, J.R.1    Miller, C.E.2    Ward, K.B.3
  • 46
    • 0023657740 scopus 로고
    • Effects of cis and trans unsaturation of the structure of phospholipid bilayers: A high-pressure infrared spectroscopic study
    • Siminovitch D.J., Wong P.T.T., Mantsch H.H. Effects of cis and trans unsaturation of the structure of phospholipid bilayers: a high-pressure infrared spectroscopic study. Biochemistry. 26:1987;3277-3287.
    • (1987) Biochemistry , vol.26 , pp. 3277-3287
    • Siminovitch, D.J.1    Wong, P.T.T.2    Mantsch, H.H.3
  • 47
    • 0030021044 scopus 로고    scopus 로고
    • The effect of high external pressure on DPPC-cholesterol multilamellar vesicles: A pressure-tuning Fourier transform infrared spectroscopic study
    • Reis O., Winter R., Zerda T.W. The effect of high external pressure on DPPC-cholesterol multilamellar vesicles: a pressure-tuning Fourier transform infrared spectroscopic study. Biochim. Biophys. Acta. 1279:1996;5-16.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 5-16
    • Reis, O.1    Winter, R.2    Zerda, T.W.3
  • 48
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FT-IR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FT-IR spectra. Biopolymers. 25:1986;469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 49
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 32:1993;389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 50
    • 0029018548 scopus 로고
    • The use and misuse of FT-IR spectroscopy in the determination of protein structure
    • Jackson M., Mantsch H.H. The use and misuse of FT-IR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:1995;95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 51
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris P.I., Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers. 37:1995;251-263.
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 52
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo J.L.R., Muga A., Castresana J., Goñi F.M. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:1993;23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 53
    • 0037171130 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in high-pressure studies on proteins
    • Dzwolak W., Kato M., Taniguchi Y. Fourier transform infrared spectroscopy in high-pressure studies on proteins. Biochim. Biophys. Acta. 1595:2002;131-144.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 131-144
    • Dzwolak, W.1    Kato, M.2    Taniguchi, Y.3
  • 54
    • 0029742801 scopus 로고    scopus 로고
    • Fourth derivative UV-spectroscopy of proteins under high pressure. I. Factors affecting the fourth derivative spectrum of the aromatic amino acids
    • Lange R., Frank J., Saldana J.L., Balny C. Fourth derivative UV-spectroscopy of proteins under high pressure. I. Factors affecting the fourth derivative spectrum of the aromatic amino acids. Eur. Biophys. J. 24:1996;277-283.
    • (1996) Eur. Biophys. J. , vol.24 , pp. 277-283
    • Lange, R.1    Frank, J.2    Saldana, J.L.3    Balny, C.4
  • 55
    • 0029761217 scopus 로고    scopus 로고
    • Fourth derivative spectroscopy of proteins under high pressure. II. Application to reversible structural changes
    • Lange R., Bec N., Mozhaev V., Frank J. Fourth derivative spectroscopy of proteins under high pressure. II. Application to reversible structural changes. Eur. Biophys. J. 24:1996;284-292.
    • (1996) Eur. Biophys. J. , vol.24 , pp. 284-292
    • Lange, R.1    Bec, N.2    Mozhaev, V.3    Frank, J.4


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