메뉴 건너뛰기




Volumn 288, Issue 3, 1999, Pages 461-475

Pressure-jump studies of the folding/unfolding of trp repressor

Author keywords

Activation volume; Fluorescence; FTIR; High pressure; Protein folding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BACTERIAL PROTEIN; GUANIDINE;

EID: 0033531967     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2692     Document Type: Article
Times cited : (86)

References (57)
  • 1
    • 0000335117 scopus 로고
    • The global analysis of fluorescence intensity and anisotropy decay data: Second generation theory and programs
    • J. R. Lakowicz. Plenum Publishing Corp. New York
    • Beechem J. M., Gratton E., Ameloot M., Knutson J. R., Brand L. The global analysis of fluorescence intensity and anisotropy decay data: second generation theory and programs. Lakowicz J. R. Topics in Fluorescence Spectroscopy Principles. 1992;241-305 Plenum Publishing Corp. New York.
    • (1992) Topics in Fluorescence Spectroscopy Principles , pp. 241-305
    • Beechem, J.M.1    Gratton, E.2    Ameloot, M.3    Knutson, J.R.4    Brand, L.5
  • 2
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvoluted FTIR spectra
    • Byler D. M., Susi H. Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers. 25:1986;469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 3
    • 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. Kinetic analysis of the acid and alkaline unfolded states of staphylococcal nuclease. J. Mol. Biol. 220:1991;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
  • 4
    • 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. pH-induced folding/unfolding of staphylococcal nuclease: determination of kinetic parameters by the sequential-jump method. Biochemistry. 31:1992;1483-1491.
    • (1992) Biochemistry , vol.31 , pp. 1483-1491
    • Chen, H.M.1    Markin, V.S.2    Tsong, T.Y.3
  • 5
    • 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. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers. 14:1975;679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Federov, O.V.2    Trushina, N.P.3
  • 6
    • 0026259378 scopus 로고
    • Segmental differences in the stability of the trp repressor peptide backbone
    • Czapliki J., Arrowsmith C., Jardetsky O. Segmental differences in the stability of the trp repressor peptide backbone. J. Biomol. NMR. 1:1991;349-361.
    • (1991) J. Biomol. NMR , vol.1 , pp. 349-361
    • Czapliki, J.1    Arrowsmith, C.2    Jardetsky, O.3
  • 7
    • 0027998091 scopus 로고
    • Functional selection and characterization of DNA-binding sites for trp repressor of Escherichia coli
    • Czernik P. J., Shin D. S., Hurlburt B. K. Functional selection and characterization of DNA-binding sites for trp repressor of Escherichia coli. J. Biol. Chem. 269:1994;27869-27875.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27869-27875
    • Czernik, P.J.1    Shin, D.S.2    Hurlburt, B.K.3
  • 9
    • 0028103991 scopus 로고
    • The unfolding of trp aporepressor as a function of pH: Evidence for an unfolding intermediate
    • Eftink M. R., Helton K. J., Beavers A., Ramsay G. D. The unfolding of trp aporepressor as a function of pH: evidence for an unfolding intermediate. Biochemistry. 33:1994;10220-10228.
    • (1994) Biochemistry , vol.33 , pp. 10220-10228
    • Eftink, M.R.1    Helton, K.J.2    Beavers, A.3    Ramsay, G.D.4
  • 11
    • 0026569112 scopus 로고
    • The role of protein-protein interactions in the regulation of transcription by trp repressor investigated by fluorescence spectroscopy
    • Fernando T., Royer C. A. The role of protein-protein interactions in the regulation of transcription by trp repressor investigated by fluorescence spectroscopy. Biochemistry. 31:1992a;3429-3441.
    • (1992) Biochemistry , vol.31 , pp. 3429-3441
    • Fernando, T.1    Royer, C.A.2
  • 12
    • 0026763452 scopus 로고
    • Unfolding of trp repressor studied using fluorescence spectroscopic techniques
    • Fernando T., Royer C. A. Unfolding of trp repressor studied using fluorescence spectroscopic techniques. Biochemistry. 31:1992b;6683-6691.
    • (1992) Biochemistry , vol.31 , pp. 6683-6691
    • Fernando, T.1    Royer, C.A.2
  • 13
    • 0030898066 scopus 로고    scopus 로고
    • The kinetic basis for the stabilization of staphylococcal nuclease by xylose
    • Frye K. J., 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
  • 14
    • 0031789585 scopus 로고    scopus 로고
    • Probing the contribution of internal cavities to the volume change of unfolding under pressure
    • Frye K. J., Royer C. A. Probing the contribution of internal cavities to the volume change of unfolding under pressure. Protein Sci. 7:1998;2217-2222.
    • (1998) Protein Sci. , vol.7 , pp. 2217-2222
    • Frye, K.J.1    Royer, C.A.2
  • 15
    • 0029737544 scopus 로고    scopus 로고
    • Testing the correlation between Δa and Δv of protein unfolding using m- value mutants of staphylococcal nuclease
    • Frye K. J., Perman C. S., Royer C. A. Testing the correlation between ΔA and ΔV of protein unfolding using m- value mutants of staphylococcal nuclease. Biochemistry. 35:1996;10234-10239.
    • (1996) Biochemistry , vol.35 , pp. 10234-10239
    • Frye, K.J.1    Perman, C.S.2    Royer, C.A.3
  • 16
    • 0030817794 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics and structure of the I form of aponyoglooin
    • Gilmanshin R., Williams S., Callender R. H., Woodruff W. H., Dyer R. B. Fast events in protein folding: relaxation dynamics and structure of the I form of aponyoglooin. Biochemistry. 36:1997;15006-15012.
    • (1997) Biochemistry , vol.36 , pp. 15006-15012
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 17
    • 0025334690 scopus 로고
    • Folding and stability of trp aporepressor from Escherichia coli
    • Gittelman M. S., Matthews C. R. Folding and stability of trp aporepressor from Escherichia coli. Biochemistry. 29:1990;7011-7020.
    • (1990) Biochemistry , vol.29 , pp. 7011-7020
    • Gittelman, M.S.1    Matthews, C.R.2
  • 18
    • 0030925611 scopus 로고    scopus 로고
    • Urea and thermal denaturation studies on the dimerization domain of Escherichia coli trp repressor
    • Gloss L. M., Matthews C. R. Urea and thermal denaturation studies on the dimerization domain of Escherichia coli trp repressor. Biochemistry. 36:1997;5612-5623.
    • (1997) Biochemistry , vol.36 , pp. 5612-5623
    • Gloss, L.M.1    Matthews, C.R.2
  • 19
    • 0032506169 scopus 로고    scopus 로고
    • The barriers of the bimolecular folding reaction of the dimeric core domain of Escherichia coli trp repressor are dominated by enthalpic contributions
    • Gloss L. M., Matthews C. R. The barriers of the bimolecular folding reaction of the dimeric core domain of Escherichia coli trp repressor are dominated by enthalpic contributions. Biochemistry. 37:1998a;16000-16010.
    • (1998) Biochemistry , vol.37 , pp. 16000-16010
    • Gloss, L.M.1    Matthews, C.R.2
  • 20
    • 0032506048 scopus 로고    scopus 로고
    • Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: A nearly diffusion-limited reaction leads to formation of an on-pathway dimeric intermediate
    • Gloss L. M., Matthews C. R. Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to formation of an on-pathway dimeric intermediate. Biochemistry. 37:1998b;15990-15999.
    • (1998) Biochemistry , vol.37 , pp. 15990-15999
    • Gloss, L.M.1    Matthews, C.R.2
  • 21
    • 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. Pressure-tuning the 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
    • Goosens, K.1    Smeller, L.2    Frank, J.3    Heremans, K.4
  • 23
    • 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
  • 24
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G., Garde S., Garcia A. E., Pavlaitis 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    Garcia, A.E.3    Pavlaitis, M.E.4    Pratt, L.R.5
  • 27
    • 36849150819 scopus 로고
    • Protein stabilization: Thermodynamics of unfolding
    • Kauzmann W. Protein stabilization: thermodynamics of unfolding. Nature. 325:1986;763-764.
    • (1986) Nature , vol.325 , pp. 763-764
    • Kauzmann, W.1
  • 28
    • 0027190920 scopus 로고
    • Structure and stability of an early folding intermediate of Escherichia colitrp aporepressor measured by Far-UV stopped flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding
    • Mann C. J., Matthews C. R. Structure and stability of an early folding intermediate of Escherichia colitrp aporepressor measured by Far-UV stopped flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry. 32:1993;5282-5290.
    • (1993) Biochemistry , vol.32 , pp. 5282-5290
    • Mann, C.J.1    Matthews, C.R.2
  • 29
    • 0028810468 scopus 로고
    • Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase
    • Mann C. J., Shao X., Matthews C. R. Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry. 34:1995;14573-14580.
    • (1995) Biochemistry , vol.34 , pp. 14573-14580
    • Mann, C.J.1    Shao, X.2    Matthews, C.R.3
  • 30
    • 0028981210 scopus 로고
    • Negative activation enthalpies in kinetics of proteinn folding
    • Oliveberg M., Tan Y.-J., Fersht A. R. Negative activation enthalpies in kinetics of proteinn folding. Proc. Natl Acad. Sci. USA. 92:1995;8926-8929.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.-J.2    Fersht, A.R.3
  • 31
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, N.1
  • 32
    • 0019539412 scopus 로고
    • Absolute measurements of fluorescence polarization at high pressure
    • Paladini A. A., Weber G. Absolute measurements of fluorescence polarization at high pressure. Rev. Sci. Instrum. 52:1981;419-423.
    • (1981) Rev. Sci. Instrum. , vol.52 , pp. 419-423
    • Paladini, A.A.1    Weber, G.2
  • 33
    • 0023056195 scopus 로고
    • High-level production and rapid purification of the Escherichia colitrp repressor
    • Paluh J. L., Yanofsky C. High-level production and rapid purification of the Escherichia colitrp repressor. Nucl. Acids Res. 14:1986;7851-7860.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 7851-7860
    • Paluh, J.L.1    Yanofsky, C.2
  • 34
    • 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 infra-red spectroscopy
    • Panik G., Malessa R., Winter R., Rapp G., Frye K. J., 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 infra-red spectroscopy. J. Mol. Biol. 275:1998;389-402.
    • (1998) J. Mol. Biol. , vol.275 , pp. 389-402
    • Panik, G.1    Malessa, R.2    Winter, R.3    Rapp, G.4    Frye, K.J.5    Royer, C.A.6
  • 35
    • 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. Comparison of various molecular forms of bovine trypsin: correlation of infrared spectra with X-ray crystal structures. Biochemistry. 30:1991;133-143.
    • (1991) Biochemistry , vol.30 , pp. 133-143
    • Prestrelski, S.J.1    Byler, D.M.2    Liebman, M.N.3
  • 36
    • 0028882449 scopus 로고
    • Evidence for coupled folding and function in the trp repressor: Physical characterization of the superrepressor mutant AV77
    • Reedstrom R. J., Royer C. A. Evidence for coupled folding and function in the trp repressor: physical characterization of the superrepressor mutant AV77. J. Mol. Biol. 253:1995;266-276.
    • (1995) J. Mol. Biol. , vol.253 , pp. 266-276
    • Reedstrom, R.J.1    Royer, C.A.2
  • 37
    • 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. The effect of high external pressure on DPPC-cholesterol multilamellar vesicles-a pressure-tuning Fourier-transform infrared spectroscopy 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
  • 38
    • 0030062907 scopus 로고    scopus 로고
    • Infrared amide I′ band of the coiled coil
    • Reisdorf W. C. Jr, Krimm S. Infrared amide I′ band of the coiled coil. Biochemistry. 35:1996;1383-1386.
    • (1996) Biochemistry , vol.35 , pp. 1383-1386
    • Reisdorf W.C., Jr.1    Krimm, S.2
  • 39
    • 0345451829 scopus 로고
    • Interaction of the operator of the tryptophan operon with repressor
    • Rose J. K., Yanofsky C. Interaction of the operator of the tryptophan operon with repressor. Proc. Natl Acad. Sci. USA. 71:1974;3134-3138.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 3134-3138
    • Rose, J.K.1    Yanofsky, C.2
  • 40
    • 0026662984 scopus 로고
    • Reolution of the instrinsic tryptophan fluorescence of trp repressor using single tryptophan mutants
    • Royer C. A. Reolution of the instrinsic tryptophan fluorescence of trp repressor using single tryptophan mutants. Biophys. J. 63:1992;741-750.
    • (1992) Biophys. J. , vol.63 , pp. 741-750
    • Royer, C.A.1
  • 41
    • 0027310271 scopus 로고
    • Improvements in the numerical analysis of thermodynamic data from biomolecular complexes
    • Royer C. A. Improvements in the numerical analysis of thermodynamic data from biomolecular complexes. Anal. Biochem. 210:1993;91-97.
    • (1993) Anal. Biochem. , vol.210 , pp. 91-97
    • Royer, C.A.1
  • 42
    • 0026637612 scopus 로고
    • Numerical analysis of binding data: Advantages, practical aspects and implications
    • Royer C. A., Beechem J. M. Numerical analysis of binding data: advantages, practical aspects and implications. Methods Enzymol. 210:1992;481-493.
    • (1992) Methods Enzymol. , vol.210 , pp. 481-493
    • Royer, C.A.1    Beechem, J.M.2
  • 43
    • 0025696029 scopus 로고
    • Analysis of binding in macromolecular complexes: A generalized numerical approach
    • Royer C. A., Smith W. R., Beechem J. M. Analysis of binding in macromolecular complexes: a generalized numerical approach. Anal. Biochem. 191:1991;287-294.
    • (1991) Anal. Biochem. , vol.191 , pp. 287-294
    • Royer, C.A.1    Smith, W.R.2    Beechem, J.M.3
  • 44
    • 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. Effects of amino acid substitutions on the pressure denaturation of Staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry. 32:1993a;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
  • 45
    • 0027378450 scopus 로고
    • Resolution of the fluorescence unfolding profile of trp repressor using single tryptophan mutants
    • Royer C. A., Mann C. J., Matthews C. R. Resolution of the fluorescence unfolding profile of trp repressor using single tryptophan mutants. Protein Sci. 2:1993b;1844-1852.
    • (1993) Protein Sci. , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 46
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability
    • Scalley M. L., Baker D. Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc. Natl Acad. Sci USA. 94:1997;10636-10640.
    • (1997) Proc. Natl Acad. Sci USA , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 48
    • 0023657740 scopus 로고
    • Effects of cis and trans unsaturation on 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 on 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
  • 49
    • 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. Least activation path for protein folding: investigation of Staphylococcal nuclease folding by stopped-flow circular dichroism. Proc. Natl Acad. Sci. USA. 93:1996;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
  • 50
    • 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. Pressure and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy. Biochemistry. 34:1995;5980-5987.
    • (1995) Biochemistry , vol.34 , pp. 5980-5987
    • Takeda, N.1    Kato, M.2    Taniguchi, Y.3
  • 51
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber G., Drickamer H. G. The effect of high pressure upon proteins and other biomolecules. Quart. Rev. Biophys. 16:1983;89-112.
    • (1983) Quart. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 53
    • 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
  • 54
    • 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. High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. Biochemistry. 35:1996;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
  • 55
    • 0023256884 scopus 로고
    • The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity
    • Zhang R.-G., Joachimiak A., Lawson C. L., Schevitz R. W., Otwinowski Z., Sigler P. B. The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity. Nature. 327:1987;591-597.
    • (1987) Nature , vol.327 , pp. 591-597
    • Zhang, R.-G.1    Joachimiak, A.2    Lawson, C.L.3    Schevitz, R.W.4    Otwinowski, Z.5    Sigler, P.B.6
  • 57
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp A., Kauzmann W. Pressure denaturation of metmyoglobin. Biochemistry. 12:1973;4217-4228.
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.