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Volumn 275, Issue 2, 1998, Pages 389-402

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

Author keywords

FT IR; High pressure; Protein folding; SAXS; Staphylococcal nuclease

Indexed keywords

NUCLEASE;

EID: 0032536156     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1454     Document Type: Article
Times cited : (238)

References (77)
  • 1
    • 0024965948 scopus 로고
    • Hydrogen NMR evidence for three interconverting forms of staphylococcal nuclease: Effects of mutations and solution conditions on their distribution
    • Alexandrescu, A. T., Ulrich, E. L. & Markley, J. L. (1989). Hydrogen NMR evidence for three interconverting forms of staphylococcal nuclease: effects of mutations and solution conditions on their distribution. Biochemistry, 28, 204-211.
    • (1989) Biochemistry , vol.28 , pp. 204-211
    • Alexandrescu, A.T.1    Ulrich, E.L.2    Markley, J.L.3
  • 2
    • 0025366064 scopus 로고
    • Coupling between local structure and global stability of a protein: Mutants of staphylococcal nuclease
    • Alexandrescu, A. T., Hinck, A. P. & Markley, J. L. (1990). Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. Biochemistry, 29, 4516-4525.
    • (1990) Biochemistry , vol.29 , pp. 4516-4525
    • Alexandrescu, A.T.1    Hinck, A.P.2    Markley, J.L.3
  • 3
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew, R. M., Sabelko, J. & Gruebele, M. (1996). Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl Acad. Sci. USA, 93, 5759-5764.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 4
    • 0014952474 scopus 로고
    • Thermodynamics of protein denaturation: Effect of pressure on the denaturation of ribonuclease A
    • Brandts, J. F., Oliveira, R. J. & Westort, C. (1970). Thermodynamics of protein denaturation: effect of pressure on the denaturation of ribonuclease A. Biochemistry, 9, 1038-1047.
    • (1970) Biochemistry , vol.9 , pp. 1038-1047
    • Brandts, J.F.1    Oliveira, R.J.2    Westort, C.3
  • 5
    • 0001435569 scopus 로고
    • The coagulation of albumen by pressure
    • Bridgman, P. W. (1914). The coagulation of albumen by pressure. J. Biol. Chem. 19, 511-512.
    • (1914) J. Biol. Chem. , vol.19 , pp. 511-512
    • Bridgman, P.W.1
  • 8
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvoluted FTIR spectra
    • Byler, D. M. & Susi, H. (1986). Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers, 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 9
    • 0028968250 scopus 로고
    • Energetics of denaturation and m values of staphylococcal nuclease mutants
    • Carra, J. H. & Privalov, P. L. (1995). Energetics of denaturation and m values of staphylococcal nuclease mutants. Biochemistry, 34, 2034-2041.
    • (1995) Biochemistry , vol.34 , pp. 2034-2041
    • Carra, J.H.1    Privalov, P.L.2
  • 11
    • 0025834146 scopus 로고
    • Kinetic analysis of the acid and alkaline unfolded states of staphylococcal nuclease
    • Chen, H. M., You, J. L., Markin, V. S. & Tsong, T. Y. (1991). Kinetic analysis of the acid and alkaline unfolded states of staphylococcal nuclease. J. Mol. Biol. 220, 771-778.
    • (1991) J. Mol. Biol. , vol.220 , pp. 771-778
    • Chen, H.M.1    You, J.L.2    Markin, V.S.3    Tsong, T.Y.4
  • 12
    • 0026534194 scopus 로고
    • PH-induced folding/unfolding of staphylococcal nuclease: Determination of kinetic parameters by the sequential-jump method
    • Chen, H. M., Markin, V. S. & Tsong, T. Y. (1992). pH-induced folding/unfolding of staphylococcal nuclease: determination of kinetic parameters by the sequential-jump method. Biochemistry, 31, 1483-1491.
    • (1992) Biochemistry , vol.31 , pp. 1483-1491
    • Chen, H.M.1    Markin, V.S.2    Tsong, T.Y.3
  • 13
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgadze, Y. N., Federov, O. V. & Trushina, N. P. (1975). Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers, 14, 679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Federov, O.V.2    Trushina, N.P.3
  • 14
    • 0024040279 scopus 로고
    • Toward a better understanding of protein folding pathways
    • Creighton, T. E. (1988). Toward a better understanding of protein folding pathways. Proc. Natl Acad. Sci. USA, 85, 5082-5086.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 5082-5086
    • Creighton, T.E.1
  • 15
    • 0001401624 scopus 로고    scopus 로고
    • High-pressure synchrotron X-ray diffraction studies of biological molecules using the diamond anvil technique
    • Czeslik, C., Malessa, R., Winter, R. & Rapp, G. (1996). High-pressure synchrotron X-ray diffraction studies of biological molecules using the diamond anvil technique. Nucl. Instr. Methods A, 368, 847-851.
    • (1996) Nucl. Instr. Methods A , vol.368 , pp. 847-851
    • Czeslik, C.1    Malessa, R.2    Winter, R.3    Rapp, G.4
  • 16
    • 0028966781 scopus 로고
    • Modeling protein stability as heteropolymer collapse
    • Dill, K. A. & Stitger, D. (1995). Modeling protein stability as heteropolymer collapse. Advan. Protein Chem. 46, 59-104.
    • (1995) Advan. Protein Chem. , vol.46 , pp. 59-104
    • Dill, K.A.1    Stitger, D.2
  • 17
    • 0025897132 scopus 로고
    • Fluorescence and conformational stability studies of staphylococcal nuclease and its mutants, including the less stable nuclease-concanavalin a hybrids
    • Eftink, M. R., Ghiron, C. A., Kautz, R. A. & Fox, O. R. (1991a). Fluorescence and conformational stability studies of staphylococcal nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids. Biochemistry, 30, 1193-1199.
    • (1991) Biochemistry , vol.30 , pp. 1193-1199
    • Eftink, M.R.1    Ghiron, C.A.2    Kautz, R.A.3    Fox, O.R.4
  • 18
    • 0025945777 scopus 로고
    • Effects of temperature on the fluorescence intensity and anisotropy decays of staphylococcal nuclease and the less stable nuclease-conA-SG28 mutant
    • Eftink, M. R., Gryczynski, I., Wiczk, W., Laczko, G. & Lakowicz, J. R. (1991b). Effects of temperature on the fluorescence intensity and anisotropy decays of staphylococcal nuclease and the less stable nuclease-conA-SG28 mutant. Biochemistry, 30, 8945-8953.
    • (1991) Biochemistry , vol.30 , pp. 8945-8953
    • Eftink, M.R.1    Gryczynski, I.2    Wiczk, W.3    Laczko, G.4    Lakowicz, J.R.5
  • 19
    • 0000125188 scopus 로고
    • Relaxation methods
    • (Weissberger, A., ed.), Wiley, New York
    • Eigen, M. & De Maeyer, L. (1963). Relaxation methods. In Techniques in Organic Chemistry (Weissberger, A., ed.), pp. 895-1054, Wiley, New York.
    • (1963) Techniques in Organic Chemistry , pp. 895-1054
    • Eigen, M.1    De Maeyer, L.2
  • 20
    • 0028884580 scopus 로고
    • The radius of gyration of an apomyoglobin folding intermediate
    • Eliezer, D., Jennings, P. A. & Wright, P. E. (1995). The radius of gyration of an apomyoglobin folding intermediate. Science, 270, 487-488.
    • (1995) Science , vol.270 , pp. 487-488
    • Eliezer, D.1    Jennings, P.A.2    Wright, P.E.3
  • 21
    • 0024965951 scopus 로고
    • A magnetization transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease
    • Evans, P. A., Kautz, R. A., Fox, R. O. & Dobson, C. M. (1989). A magnetization transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease. Biochemistry, 28, 362-370.
    • (1989) Biochemistry , vol.28 , pp. 362-370
    • Evans, P.A.1    Kautz, R.A.2    Fox, R.O.3    Dobson, C.M.4
  • 22
    • 0000736085 scopus 로고
    • Preparation, crystalline structure, and spectral properties of the fluorescent probe 4,4′-bis-1-phenylamino-8-naphthalenesulfonate
    • Farris, F. J., Weber, G., Chiang, C. & Paul, I. C. (1978). Preparation, crystalline structure, and spectral properties of the fluorescent probe 4,4′-bis-1-phenylamino-8-naphthalenesulfonate. J. Am. Chem. Soc. 100, 4469-4478.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 4469-4478
    • Farris, F.J.1    Weber, G.2    Chiang, C.3    Paul, I.C.4
  • 24
    • 0030898066 scopus 로고    scopus 로고
    • The kinetic basis for the stabilization of staphylococcal nuclease by xylose
    • Frye, K. J. & Royer, C. A. (1997). The kinetic basis for the stabilization of staphylococcal nuclease by xylose. Protein Sci. 6, 789-793.
    • (1997) Protein Sci. , vol.6 , pp. 789-793
    • Frye, K.J.1    Royer, C.A.2
  • 25
    • 0029737544 scopus 로고    scopus 로고
    • Testing the correlation between AA and AV of protein unfolding using m-value mutants of staphylococcal nuclease
    • Frye, K. J., Perman, C. S. & Royer, C. A. (1996). Testing the correlation between AA and AV of protein unfolding using m-value mutants of staphylococcal nuclease. Biochemistry, 35, 10234-10239.
    • (1996) Biochemistry , vol.35 , pp. 10234-10239
    • Frye, K.J.1    Perman, C.S.2    Royer, C.A.3
  • 26
    • 0017539686 scopus 로고
    • Position sensitive X-ray detectors
    • Gabriel, A. (1977). Position sensitive X-ray detectors. Rev. Sci. Instr. 48, 1303-1305.
    • (1977) Rev. Sci. Instr. , vol.48 , pp. 1303-1305
    • Gabriel, A.1
  • 27
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin, R., Williams, S., Callender, R. H., Woodruff, W. H. & Dyer, R. B. (1997). Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl Acad. Sci. USA, 94, 3709-3713.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 28
    • 0002622807 scopus 로고
    • Data evaluation in small-angle scattering: Calculation of the radial electron density distribution by means of indirect Fourier transformation
    • Glatter, O. (1977). Data evaluation in small-angle scattering: calculation of the radial electron density distribution by means of indirect Fourier transformation. Acta Phys. Aust. 47, 83-102.
    • (1977) Acta Phys. Aust. , vol.47 , pp. 83-102
    • Glatter, O.1
  • 29
    • 0001757015 scopus 로고
    • The interpretation of real-space information from small-angle scattering experiments
    • Glatter, O. (1979). The interpretation of real-space information from small-angle scattering experiments. J. Appl. Crystallog. 12, 166-175.
    • (1979) J. Appl. Crystallog. , vol.12 , pp. 166-175
    • Glatter, O.1
  • 31
    • 0029915110 scopus 로고    scopus 로고
    • Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier-transform infrared spectroscopy
    • Goosens, K., Smeller, L., Frank, J. & Heremans, K. (1996). Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier-transform infrared spectroscopy. Eur. J. Biochem. 236, 254-262.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 254-262
    • Goosens, K.1    Smeller, L.2    Frank, J.3    Heremans, K.4
  • 33
    • 0028220701 scopus 로고
    • Proteins under pressure
    • Gross, M. & Jaenicke, R. (1994). Proteins under pressure. Eur. J. Biochem. 221, 617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 34
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley, S. A. (1971). Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry, 10, 2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 35
    • 0020017199 scopus 로고
    • High-pressure effects on proteins and other biomolecules
    • Heremans, K. (1982). High-pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11, 1-21.
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 36
    • 0025877987 scopus 로고
    • The crystal structure of staphylococcal nuclease refined at 1. 7 Å resolution
    • Hynes, T. R. & Fox, R. O. (1991). The crystal structure of staphylococcal nuclease refined at 1. 7 Å resolution. Proteins: Struct. Funct. Genet. 10, 92-105.
    • (1991) Proteins: Struct. Funct. Genet. , vol.10 , pp. 92-105
    • Hynes, T.R.1    Fox, R.O.2
  • 37
    • 0002770218 scopus 로고
    • Protein folding: Theoretical studies of thermodynamics and dynamics
    • (Creighton, T., ed.), W. H. Freeman, New York
    • Karplus, M. & Shaknovich, E. (1992). Protein folding: theoretical studies of thermodynamics and dynamics. In Protein Folding (Creighton, T., ed.), pp. 126-195, W. H. Freeman, New York.
    • (1992) Protein Folding , pp. 126-195
    • Karplus, M.1    Shaknovich, E.2
  • 38
    • 0017251893 scopus 로고
    • Protein-folding dynamics
    • Karplus, M. & Weaver, D. L. (1976). Protein-folding dynamics. Nature, 260, 404-406.
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 39
    • 0001885952 scopus 로고
    • Use of X-ray solution scattering for a protein folding study
    • (Chance, B., Deisenhofer, J., Ebashi, S., Goodhead, D. T., Helliwell, J. R., Huxley, H. E., Iizuka, T., Kirz, J., Mitsui, T., Rubenstein, E., Sakabe, N., Sasaki, T., Schmahl, G., Stuhrmann, H. B., Wüthrich, K. & Zaccai, G., eds), Calendon Press, Oxford
    • Kataoka, M., Flanagan, J. M., Tokunaga, F. & Engelman, D. M. (1994). Use of X-ray solution scattering for a protein folding study. In Synchrotron Radiation in the Biosciences (Chance, B., Deisenhofer, J., Ebashi, S., Goodhead, D. T., Helliwell, J. R., Huxley, H. E., Iizuka, T., Kirz, J., Mitsui, T., Rubenstein, E., Sakabe, N., Sasaki, T., Schmahl, G., Stuhrmann, H. B., Wüthrich, K. & Zaccai, G., eds), pp. 187-194, Calendon Press, Oxford.
    • (1994) Synchrotron Radiation in the Biosciences , pp. 187-194
    • Kataoka, M.1    Flanagan, J.M.2    Tokunaga, F.3    Engelman, D.M.4
  • 40
    • 0027413672 scopus 로고
    • NMR analysis of staphylococcal nuclease thermal quench refolding kinetics
    • Kautz, R. A. & Fox, R. O. (1993). NMR analysis of staphylococcal nuclease thermal quench refolding kinetics. Protein Sci. 2, 851-858.
    • (1993) Protein Sci. , vol.2 , pp. 851-858
    • Kautz, R.A.1    Fox, R.O.2
  • 41
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S. & Baldwin, R. L. (1982). Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 42
    • 0025345415 scopus 로고
    • Intermediates in the folding reaction of small proteins
    • Kim, P. S. & Baldwin, R. L. (1990). Intermediates in the folding reaction of small proteins. Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 43
    • 0026244229 scopus 로고
    • Molscript, a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). Molscript, a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 44
    • 0017054059 scopus 로고
    • Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme
    • Li, T. M., Hook, T. W., Drickamer, H. G. & Weber, G. (1976). Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme. Biochemistry, 15, 5572-5581.
    • (1976) Biochemistry , vol.15 , pp. 5572-5581
    • Li, T.M.1    Hook, T.W.2    Drickamer, H.G.3    Weber, G.4
  • 45
    • 0014349486 scopus 로고
    • Dimensions of protein random coils
    • Miller, W. G. & Goebel, C. V. (1968). Dimensions of protein random coils. Biochemistry, 7, 3925-3935.
    • (1968) Biochemistry , vol.7 , pp. 3925-3935
    • Miller, W.G.1    Goebel, C.V.2
  • 48
    • 0000990154 scopus 로고
    • Practical aspects in the use of indirect Fourier transformation methods
    • Müller, K. & Glatter, O. (1982). Practical aspects in the use of indirect Fourier transformation methods. Makromol. Chem. 183, 465-479.
    • (1982) Makromol. Chem. , vol.183 , pp. 465-479
    • Müller, K.1    Glatter, O.2
  • 49
    • 0028963362 scopus 로고
    • Toward an outline of the topography of a realistic protein-folding funnel
    • Onuchic, J. N., Wolynes, P. G. & Soccir, N. D. (1995). Toward an outline of the topography of a realistic protein-folding funnel. Proc. Natl Acad. Sci. USA, 92, 3626-3630.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3626-3630
    • Onuchic, J.N.1    Wolynes, P.G.2    Soccir, N.D.3
  • 50
    • 0028058671 scopus 로고
    • High-pressure NMR study of the dissociation of arc repressor
    • Peng, X., Jonas, J. & Silva, J. L. (1994). High-pressure NMR study of the dissociation of arc repressor. Biochemistry, 33, 8323-8329.
    • (1994) Biochemistry , vol.33 , pp. 8323-8329
    • Peng, X.1    Jonas, J.2    Silva, J.L.3
  • 51
    • 0026034588 scopus 로고
    • Comparison of various molecular forms of bovine trypsin: Correlation of infrared spectra with X-ray crystal structures
    • Prestrelski, S. J., Byler, D. M. & Liebman, M. N. (1991). Comparison of various molecular forms of bovine trypsin: correlation of infrared spectra with X-ray crystal structures. Biochemistry, 30, 133-143.
    • (1991) Biochemistry , vol.30 , pp. 133-143
    • Prestrelski, S.J.1    Byler, D.M.2    Liebman, M.N.3
  • 52
    • 0001369113 scopus 로고
    • Time-resolved X-ray diffraction studies on biological systems
    • Rapp, G. (1992). Time-resolved X-ray diffraction studies on biological systems. Acta Phys. Polonica A, 82, 103-120.
    • (1992) Acta Phys. Polonica A , vol.82 , pp. 103-120
    • Rapp, G.1
  • 53
    • 0030021044 scopus 로고    scopus 로고
    • The effect of high external pressure on DPPC-cholesterol multilamellar vesicles - A pressure-tuning Fourier-transform infrared spectroscopy study
    • Reis, O., Winter, R. & Zerda, T. W. (1996). The effect of high external pressure on DPPC-cholesterol multilamellar vesicles - a pressure-tuning Fourier-transform infrared spectroscopy study. Biochim. Biophys. Acta, 1279, 5-16.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 5-16
    • Reis, O.1    Winter, R.2    Zerda, T.W.3
  • 54
    • 0027815614 scopus 로고
    • An Analysis of packing in the protein folding problem
    • Richards, F. M. & Lim, W. A. (1994). An Analysis of packing in the protein folding problem. Annu. Rev. Biophys. Bioeng. 26, 423-498.
    • (1994) Annu. Rev. Biophys. Bioeng. , vol.26 , pp. 423-498
    • Richards, F.M.1    Lim, W.A.2
  • 55
    • 0025696029 scopus 로고
    • Analysis of binding in macromolecular complexes: A generalized numerical approach
    • Royer, C. A., Smith, W. R. & Beechem, J. M. (1991). Analysis of binding in macromolecular complexes: a generalized numerical approach. Anal. Biochem. 191, 287-294.
    • (1991) Anal. Biochem. , vol.191 , pp. 287-294
    • Royer, C.A.1    Smith, W.R.2    Beechem, J.M.3
  • 56
    • 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. & Markley, J. L. (1993). Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry, 32, 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
  • 57
    • 0026781884 scopus 로고
    • High-resolution NMR study of the pressure-induced unfolding of lysozyme
    • Samarasinghe, S. D., Campbell, D. M., Jonas, A. & Jonas, J. (1992). High-resolution NMR study of the pressure-induced unfolding of lysozyme. Biochemistry, 31, 7773-7778.
    • (1992) Biochemistry , vol.31 , pp. 7773-7778
    • Samarasinghe, S.D.1    Campbell, D.M.2    Jonas, A.3    Jonas, J.4
  • 59
    • 0022571680 scopus 로고
    • Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease
    • Shortle, D. (1986). Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease. J. Cell. Biochem. 30, 281-289.
    • (1986) J. Cell. Biochem. , vol.30 , pp. 281-289
    • Shortle, D.1
  • 60
    • 0021968408 scopus 로고
    • Genetic analysis of staphylococcal nuclease: Identification of three intragenic global suppressors of nuclease-minus mutations
    • Shortle, D. & Lin, B. (1985). Genetic analysis of staphylococcal nuclease: identification of three intragenic global suppressors of nuclease-minus mutations. Genetics, 110, 539-555.
    • (1985) Genetics , vol.110 , pp. 539-555
    • Shortle, D.1    Lin, B.2
  • 61
    • 0022994226 scopus 로고
    • Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation
    • Shortle, D. & Meeker, A. K. (1986). Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. Proteins: Struct. Funct. Genet. 1, 81-89.
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 81-89
    • Shortle, D.1    Meeker, A.K.2
  • 62
    • 0024298839 scopus 로고    scopus 로고
    • Stability mutants of staphylococcal nuclease: Large compensating enthalpy-entropy changes for the reversible denaturation reaction
    • Shortle, D., Meeker, A. K. & Freire, E. (1998). Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction. Biochemistry, 27, 4761-4768.
    • (1998) Biochemistry , vol.27 , pp. 4761-4768
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 63
    • 0024375552 scopus 로고
    • Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease
    • Shortle, D., Meeker, A. K. & Gerring, S. L. (1989). Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease. Arch. Biochem. Biophys. 272, 103-113.
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 103-113
    • Shortle, D.1    Meeker, A.K.2    Gerring, S.L.3
  • 64
  • 65
    • 0026541905 scopus 로고
    • Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor
    • Silva, J. L., Silveira, C. F., Correia, A., Jr & Pontes, L. (1992). Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor. J. Mol. Biol. 223, 545-555.
    • (1992) J. Mol. Biol. , vol.223 , pp. 545-555
    • Silva, J.L.1    Silveira, C.F.2    Correia A., Jr.3    Pontes, L.4
  • 66
    • 0023657740 scopus 로고
    • Effects of cis and trans unsaturation on the structure of phospholipid bilayers: A high-pressure infrared spectroscophic study
    • Siminovitch, D. J., Wong, P. T. T. & Mantsch, H. H. (1987). Effects of cis and trans unsaturation on the structure of phospholipid bilayers: a high-pressure infrared spectroscophic study. Biochemistry, 26, 3277-3287.
    • (1987) Biochemistry , vol.26 , pp. 3277-3287
    • Siminovitch, D.J.1    Wong, P.T.T.2    Mantsch, H.H.3
  • 67
    • 0029975983 scopus 로고    scopus 로고
    • Least activation path for protein folding: Investigation of staphylococcal nuclease folding by stopped-flow circular dichroism
    • Su, Z. D., Arooz, M. T., Chen, H. M., Gross, C. J. & Tsong, T. Y. (1996). Least activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow circular dichroism. Proc. Natl Acad. Sci. USA, 93, 2539-2544.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2539-2544
    • Su, Z.D.1    Arooz, M.T.2    Chen, H.M.3    Gross, C.J.4    Tsong, T.Y.5
  • 68
    • 0000357520 scopus 로고
    • Protein denaturation by high-pressure. Measurements of turbidity of isoelectric ovalbumin and horse serum albumin under high-pressure
    • Suzuki, K., Miyosawa, Y. & Suzuki, C. (1963). Protein denaturation by high-pressure. Measurements of turbidity of isoelectric ovalbumin and horse serum albumin under high-pressure. Arch. Biochem. Biophys. 101, 225-228.
    • (1963) Arch. Biochem. Biophys. , vol.101 , pp. 225-228
    • Suzuki, K.1    Miyosawa, Y.2    Suzuki, C.3
  • 69
    • 0029024519 scopus 로고
    • Pressure and thermally-induced reversible changes in the secondary structure of ribonuclease a studied by FT-IR spectroscopy
    • Takeda, N., Kato, M. & Taniguchi, Y. (1995). Pressure and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy. Biochemistry, 34, 5980-5987.
    • (1995) Biochemistry , vol.34 , pp. 5980-5987
    • Takeda, N.1    Kato, M.2    Taniguchi, Y.3
  • 70
    • 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. (1995). Evidence for a molten globule-like transition state in protein folding from determination of activation volumes. Biochemistry, 34, 4909-4912.
    • (1995) Biochemistry , vol.34 , pp. 4909-4912
    • Vidugiris, G.J.A.1    Markley, J.L.2    Royer, C.A.3
  • 71
    • 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. L. & Royer, C. A. (1996). High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. Biochemistry, 35, 3857-3864.
    • (1996) Biochemistry , vol.35 , pp. 3857-3864
    • Vidugiris, G.J.A.1    Truckses, D.M.2    Markley, J.L.3    Royer, C.A.4
  • 72
    • 0026565338 scopus 로고
    • 15N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopy
    • 15N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopy. Biochemistry, 31, 911-920.
    • (1992) Biochemistry , vol.31 , pp. 911-920
    • Wang, J.F.1    Mooberry, E.S.2    Walkenhorst, W.F.3    Markley, J.L.4
  • 73
    • 0026584349 scopus 로고
    • 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3′,5′-biphosphate-calcium ternary complex
    • 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3′,5′-biphosphate-calcium ternary complex. Biochemistry, 31, 921-936.
    • (1992) Biochemistry , vol.31 , pp. 921-936
    • Wang, J.F.1    Hinck, A.P.2    Loh, S.N.3    LeMaster, D.M.4    Markley, J.L.5
  • 74
    • 0020712468 scopus 로고
    • The effect of high-pressure upon proteins and other biomolecules
    • Weber, G. & Drickamer, H. G. (1983). The effect of high-pressure upon proteins and other biomolecules. Quart. Rev. Biophys. 16, 89-112.
    • (1983) Quart. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 75
    • 0023727267 scopus 로고
    • Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: A Fourier transform infrared spectroscopy study
    • Wong, P. T. T. & Heremans, K. (1988). Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopy study. Biochim. Biophys. Acta, 965, 1-9.
    • (1988) Biochim. Biophys. Acta , vol.965 , pp. 1-9
    • Wong, P.T.T.1    Heremans, K.2
  • 76
    • 0029869230 scopus 로고    scopus 로고
    • Reversible thermal denaturation of staphylococcal nuclease: A Fourier transformed infrared spectrum study
    • Xie, L., Jing, G.-Z. & Zhou, J.-M. (1996). Reversible thermal denaturation of staphylococcal nuclease: a Fourier transformed infrared spectrum study. Arch. Biochem. Biophys. 328, 122-128.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 122-128
    • Xie, L.1    Jing, G.-Z.2    Zhou, J.-M.3
  • 77
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp, A. & Kauzmann, W. (1973). Pressure denaturation of metmyoglobin. Biochemistry, 12, 4217-4228.
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2


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