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Volumn 1764, Issue 3, 2006, Pages 481-488

Folding studies of two hydrostatic pressure sensitive proteins

Author keywords

High pressure; Pressure jump; Protein stabilization; Unfolding folding of protein

Indexed keywords

PROTEIN;

EID: 33645994817     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.12.019     Document Type: Article
Times cited : (5)

References (50)
  • 1
    • 0028349704 scopus 로고
    • Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea
    • Buck M., Radford S.E., and Dobson C.M. Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea. J. Mol. Biol. 237 (1994) 247-254
    • (1994) J. Mol. Biol. , vol.237 , pp. 247-254
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 3
    • 0001751429 scopus 로고    scopus 로고
    • Protein faltung aus theoretischer und experimenteller
    • Dobson C.M., Sali A., and Karplus M. Protein faltung aus theoretischer und experimenteller. Sicht. Angew. Chem. 110 (1998) 908-935
    • (1998) Sicht. Angew. Chem. , vol.110 , pp. 908-935
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 4
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim P.S., and Baldwin R.L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51 (1982) 459-489
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 5
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P.S., and Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59 (1990) 631-660
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 6
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • Heremans K. High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11 (1982) 1-21
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 7
    • 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., and Pratt L.R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc.Natl. Acad. Sci. U. S. A. 95 (1998) 1552-1555
    • (1998) Proc.Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    García, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 10
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber G., and Drickamer H.G. The effect of high pressure upon proteins and other biomolecules. Q. Rev. Biophys. 16 (1983) 89-112
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 11
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp A., and Kauzmann W. Pressure denaturation of metmyoglobin. Biochemistry 12 (1973) 4217-4228
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2
  • 12
  • 13
    • 0037171119 scopus 로고    scopus 로고
    • High-resolution nuclear magnetic resonance studies of proteins
    • Jonas J. High-resolution nuclear magnetic resonance studies of proteins. Biochim. Biophys. Acta 1595 (2002) 145-159
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 145-159
    • Jonas, J.1
  • 14
    • 0037171141 scopus 로고    scopus 로고
    • UV-visible derivative spectroscopy under high pressure
    • Lange R., and 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
  • 16
    • 0037171142 scopus 로고    scopus 로고
    • High pressure static fluorescence to study macromoleclar structure-function
    • Ruan K., and Balny C. High pressure static fluorescence to study macromoleclar structure-function. Biochim. Biophys. Acta 1595 (2002) 94-102
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 94-102
    • Ruan, K.1    Balny, C.2
  • 17
    • 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
  • 19
    • 0032575495 scopus 로고    scopus 로고
    • Unusual effect of high hydrostatic pressure on basic phospholipase A2 from venom of Agkistrodon halys Pallas
    • Ruan K., Lange R., Zhou Y., and Balny C. Unusual effect of high hydrostatic pressure on basic phospholipase A2 from venom of Agkistrodon halys Pallas. Biochem. Biophys. Res. Commun. 249 (1998) 844-848
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 844-848
    • Ruan, K.1    Lange, R.2    Zhou, Y.3    Balny, C.4
  • 20
    • 0033214555 scopus 로고    scopus 로고
    • Fluorescence and FTIR study of the pressure-induced denaturation of bovine pancreas trypsin
    • Ruan K., Lange R., Meersman F., Heremans K., and Balny C. Fluorescence and FTIR study of the pressure-induced denaturation of bovine pancreas trypsin. Eur. J. Biochem. 265 (1999) 79-85
    • (1999) Eur. J. Biochem. , vol.265 , pp. 79-85
    • Ruan, K.1    Lange, R.2    Meersman, F.3    Heremans, K.4    Balny, C.5
  • 21
    • 0033939878 scopus 로고    scopus 로고
    • Effects of hydrostatic pressure on the structure and biological activity of infectious bursal disease virus
    • Tian S.-M., Ruan K.-C., Qian J.-F., Shao G.-Q., and Balny C. Effects of hydrostatic pressure on the structure and biological activity of infectious bursal disease virus. Eur. J. Biochem. 267 (2000) 4486-4494
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4486-4494
    • Tian, S.-M.1    Ruan, K.-C.2    Qian, J.-F.3    Shao, G.-Q.4    Balny, C.5
  • 22
    • 0027180821 scopus 로고
    • Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy
    • Royer C.A., Hinck A.P., Loh S.N., Prehoda K.E., Peng X., Jonas J., and Markley J.L. Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry 32 (1993) 5222-5232
    • (1993) Biochemistry , vol.32 , pp. 5222-5232
    • Royer, C.A.1    Hinck, A.P.2    Loh, S.N.3    Prehoda, K.E.4    Peng, X.5    Jonas, J.6    Markley, J.L.7
  • 23
    • 0036296247 scopus 로고    scopus 로고
    • A rare protein fluorescence behavior where the emission is dominated by tyrosine. Case of the 33-kDa protein from spinach photosystem II
    • Ruan K., Li J., Liang R., Xu C., Yu Y., Lange R., and Balny C. A rare protein fluorescence behavior where the emission is dominated by tyrosine. Case of the 33-kDa protein from spinach photosystem II. Biochem. Biophys. Res. Commun. 293 (2002) 593-597
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 593-597
    • Ruan, K.1    Li, J.2    Liang, R.3    Xu, C.4    Yu, Y.5    Lange, R.6    Balny, C.7
  • 24
    • 0034850269 scopus 로고    scopus 로고
    • Pressure-exploration of the 33-kDa protein from spinach photosystem II particle
    • Ruan K., Xu C., Yu Y., Li J., Lange R., Bec N., and Balny C. Pressure-exploration of the 33-kDa protein from spinach photosystem II particle. Eur. J. Biochem. 268 (2001) 2742-2750
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2742-2750
    • Ruan, K.1    Xu, C.2    Yu, Y.3    Li, J.4    Lange, R.5    Bec, N.6    Balny, C.7
  • 25
    • 0038071510 scopus 로고    scopus 로고
    • The thermodynamic analysis of protein stabilization by sucrose and glycerol against pressure-induced unfolding-The typical example of the 33-kDa protein from spinach photosystem II
    • Ruan K., Xu C., Li T., Li J., Lange R., and Balny C. The thermodynamic analysis of protein stabilization by sucrose and glycerol against pressure-induced unfolding-The typical example of the 33-kDa protein from spinach photosystem II. Eur. J. Biochem. 270 (2003) 1654-1661
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1654-1661
    • Ruan, K.1    Xu, C.2    Li, T.3    Li, J.4    Lange, R.5    Balny, C.6
  • 27
    • 0002181672 scopus 로고
    • Complete amino acid sequence of 33-kDa protein isolated from spinach photosystem II particles
    • Murata N. Complete amino acid sequence of 33-kDa protein isolated from spinach photosystem II particles. FEBS Lett. 197 (1986) 63-66
    • (1986) FEBS Lett. , vol.197 , pp. 63-66
    • Murata, N.1
  • 28
    • 0028142413 scopus 로고
    • Expression of 23 kDa protein from the oxygen-evolving complex of higher plants in Escherichia coli
    • Seidler A. Expression of 23 kDa protein from the oxygen-evolving complex of higher plants in Escherichia coli. Biochim. Biophys. Acta 1187 (1994) 73-79
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 73-79
    • Seidler, A.1
  • 29
    • 33645963020 scopus 로고    scopus 로고
    • J.R. Lakowicz, Principles of fluorescence spectroscopy, Sec. Edition Kluwer Academic/Plenum Publisher, New York, 1999.
  • 30
    • 0033616751 scopus 로고    scopus 로고
    • Exploring the temperature-pressure phase diagram of staphylococcal nuclease
    • Panick G., Vidugiris G.J., Malessa R., Rapp G., Winter R., and Royer C.A. Exploring the temperature-pressure phase diagram of staphylococcal nuclease. Biochemistry 38 (1999) 4157-4164
    • (1999) Biochemistry , vol.38 , pp. 4157-4164
    • Panick, G.1    Vidugiris, G.J.2    Malessa, R.3    Rapp, G.4    Winter, R.5    Royer, C.A.6
  • 31
    • 0032536156 scopus 로고    scopus 로고
    • Structural characterization of the pressure-denatured state and unfolding/refolding kinetics 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., and Royer C.A. Structural characterization of the pressure-denatured state and unfolding/refolding kinetics 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
  • 32
    • 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
  • 33
    • 0037171132 scopus 로고    scopus 로고
    • Pressure-temperature diagrams of biomolecules
    • Smeller L. Pressure-temperature diagrams of biomolecules. Biochim. Biophys. Acta 1595 (2002) 11-29
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 11-29
    • Smeller, L.1
  • 34
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures
    • Gekko K., and Timasheff S.N. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20 (1981) 4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 35
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee J.C., and Timasheff S.N. The stabilization of proteins by sucrose. J. Biol. Chem. 256 (1981) 7193-7201
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 36
    • 0027310845 scopus 로고
    • The control of protein stability and association by interactions with water: how do solvent affect these processes?
    • Timasheff S.N. The control of protein stability and association by interactions with water: how do solvent affect these processes?. Annu. Rev. Biophys. Biomol. Struct. 22 (1993) 67-97
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 37
    • 0029878188 scopus 로고    scopus 로고
    • High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants
    • Vidugiris G.J.A., Truckses D.M., Markley J., and Royer C. High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. Biochemistry 35 (1996) 3854-3857
    • (1996) Biochemistry , vol.35 , pp. 3854-3857
    • Vidugiris, G.J.A.1    Truckses, D.M.2    Markley, J.3    Royer, C.4
  • 39
    • 0030898066 scopus 로고    scopus 로고
    • The kinetic basis for the stabilization of staphylococcal nuclease by xylose
    • Frye K.J., and Royer C.A. The kinetic basis for the stabilization of staphylococcal nuclease by xylose. Protein Sci. 6 (1997) 789-793
    • (1997) Protein Sci. , vol.6 , pp. 789-793
    • Frye, K.J.1    Royer, C.A.2
  • 40
    • 0024963668 scopus 로고
    • Hysteresis and conformational drift of pressure-dissociated glyceraldehydephosphate dehydrogenase
    • Ruan K., and Weber G. Hysteresis and conformational drift of pressure-dissociated glyceraldehydephosphate dehydrogenase. Biochemistry 28 (1989) 2144-2153
    • (1989) Biochemistry , vol.28 , pp. 2144-2153
    • Ruan, K.1    Weber, G.2
  • 41
    • 0028071439 scopus 로고
    • Arc repressor will not denature under pressure in the absence of water
    • Oliveira A.C., Gaspar L.P., Da Poian A.T., and Silva J.L. Arc repressor will not denature under pressure in the absence of water. J. Mol. Biol. 240 (1994) 184-187
    • (1994) J. Mol. Biol. , vol.240 , pp. 184-187
    • Oliveira, A.C.1    Gaspar, L.P.2    Da Poian, A.T.3    Silva, J.L.4
  • 42
  • 43
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra- and intermolecular interactions within proteins
    • Boonyaratanakornkit B.B., Park C.B., and Clark D.S. Pressure effects on intra- and intermolecular interactions within proteins. Biochim. Biophys. Acta 1595 (2002) 235-249
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 235-249
    • Boonyaratanakornkit, B.B.1    Park, C.B.2    Clark, D.S.3
  • 44
    • 0030028764 scopus 로고    scopus 로고
    • Glycerol decreases the volume and compressibility of protein interior
    • Priev A., Almagor A., Yedgar S., and Gavish B. Glycerol decreases the volume and compressibility of protein interior. Biochemistry 35 (1996) 2061-2066
    • (1996) Biochemistry , vol.35 , pp. 2061-2066
    • Priev, A.1    Almagor, A.2    Yedgar, S.3    Gavish, B.4
  • 45
    • 0029130871 scopus 로고
    • Macromolecules and water: probing with osmotic stress
    • Parsegian V.A., Rand R.P., and Rau D. Macromolecules and water: probing with osmotic stress. Methods Enzymol. 259 (1995) 43-94
    • (1995) Methods Enzymol. , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.3
  • 46
    • 0037171146 scopus 로고    scopus 로고
    • The effects of osmotic and hydrostatic pressures on macromolecular systems
    • Kornblatt J.A., and Kornblatt M.J. The effects of osmotic and hydrostatic pressures on macromolecular systems. Biochim. Biophys. Acta 1595 (2002) 30-47
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 30-47
    • Kornblatt, J.A.1    Kornblatt, M.J.2
  • 47
    • 0028210538 scopus 로고
    • Hydrostatic pressure reverses osmotic pressure effect on the specificity of EcoRI-DNA interactions
    • Robinson C.R., and Sligar S.G. Hydrostatic pressure reverses osmotic pressure effect on the specificity of EcoRI-DNA interactions. Biochemistry 33 (1994) 3787-3793
    • (1994) Biochemistry , vol.33 , pp. 3787-3793
    • Robinson, C.R.1    Sligar, S.G.2
  • 48
    • 0029144073 scopus 로고
    • Hydrostatic pressure and osmotic pressure as tools to study macromolecular recognition
    • Robinson C.R., and Sligar S.G. Hydrostatic pressure and osmotic pressure as tools to study macromolecular recognition. Methods Enzymol. 259 (1995) 359-427
    • (1995) Methods Enzymol. , vol.259 , pp. 359-427
    • Robinson, C.R.1    Sligar, S.G.2
  • 49
    • 0034700971 scopus 로고    scopus 로고
    • Pressure induced unfolding/refolding of ribonuclease A: static and kinetic Fourier transform infrared spectroscopy study
    • Panick G., and 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
  • 50
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding dynamics and structure
    • Silva J.L., Fouguel D., and Royer C.A. Pressure provides new insights into protein folding dynamics and structure. Trends Biochem. Sci. 26 (2001) 612-618
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Fouguel, D.2    Royer, C.A.3


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