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Volumn 291, Issue 3, 1999, Pages 693-701

The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding

Author keywords

Guanidinium chloride; Hen egg white lysozyme; Partial specific isentropic compressibility; Partial specific volume; Pressure assisted unfolding

Indexed keywords

EGG WHITE; GLOBULAR PROTEIN; GUANIDINE; LYSOZYME;

EID: 0033588264     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2982     Document Type: Article
Times cited : (55)

References (49)
  • 1
    • 0014952474 scopus 로고
    • Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A
    • Brandts J. F., Oliveira R. J., Westort C. Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry. 9:1970;1038-1047.
    • (1970) Biochemistry , vol.9 , pp. 1038-1047
    • Brandts, J.F.1    Oliveira, R.J.2    Westort, C.3
  • 2
    • 0028349704 scopus 로고
    • Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea
    • Buck M., Radford S. E., 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
    • 0030034601 scopus 로고    scopus 로고
    • Compressibility as a means to detect and characterize globular protein states
    • Chalikian T. V., Breslauer K. J. Compressibility as a means to detect and characterize globular protein states. Proc. Natl Acad. Sci. USA. 93:1996a;1012-1014.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1012-1014
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 4
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • Chalikian T. V., Breslauer K. J. On volume changes accompanying conformational transitions of biopolymers. Biopolymers. 39:1996b;619-626.
    • (1996) Biopolymers , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 5
    • 0031790423 scopus 로고    scopus 로고
    • Thermodynamic analysis of biomolecules: A volumetric approach
    • Chalikian T. V., Breslauer K. J. Thermodynamic analysis of biomolecules: a volumetric approach. Curr. Opin. Struct. Biol. 8:1998;657-664.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 657-664
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 6
    • 0027993455 scopus 로고
    • Hydration and partial compressibility of biological compounds
    • Chalikian T. V., Sarvazyan A. P., Breslauer K. J. Hydration and partial compressibility of biological compounds. Biophys. Chem. 51:1994;89-109.
    • (1994) Biophys. Chem. , vol.51 , pp. 89-109
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 7
    • 0029011017 scopus 로고
    • Volumetric characterization of the native, molten globule and unfolded states of cytochrome c at acidic pH
    • Chalikian T. V., Gindikin V. S., Breslauer K. J. Volumetric characterization of the native, molten globule and unfolded states of cytochrome c at acidic pH. J. Mol. Biol. 250:1995;291-306.
    • (1995) J. Mol. Biol. , vol.250 , pp. 291-306
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 8
    • 0030059691 scopus 로고    scopus 로고
    • Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: Characterization of the base-induced unfolded state at 25 °c
    • Chalikian T. V., Gindikin V. S., Breslauer K. J. Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: characterization of the base-induced unfolded state at 25 °C. FASEB J. 10:1996a;164-170.
    • (1996) FASEB J. , vol.10 , pp. 164-170
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 9
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamic and structural data
    • Chalikian T. V., Totrov M., Abagyan R., Breslauer K. J. The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data. J. Mol. Biol. 260:1996b;588-603.
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 10
    • 0030572626 scopus 로고    scopus 로고
    • A lysozyme folding intermediate revealed by solution X-ray scattering
    • Chen L., Hodgson K. O., Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261:1996;658-671.
    • (1996) J. Mol. Biol. , vol.261 , pp. 658-671
    • Chen, L.1    Hodgson, K.O.2    Doniach, S.3
  • 12
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink A. L., Calciano L. J., Goto Y., Kurotsu T., Palleros D. R. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry. 33:1994;12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 13
    • 0031789585 scopus 로고    scopus 로고
    • Probing the contribution of internal cavities to the volume change of protein unfolding under pressure
    • Frye K. J., Royer C. A. Probing the contribution of internal cavities to the volume change of protein 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
  • 14
    • 0029737544 scopus 로고    scopus 로고
    • Testing the correlation between delta A and delta V of protein unfolding using m value mutants of staphylococcal nuclease
    • Frye K. J., Perman C. S., Royer C. A. Testing the correlation between delta A and delta V 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
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko K., Hasegawa Y. Compressibility-structure relationship of globular proteins. Biochemistry. 25:1986;6563-6571.
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 17
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 °c
    • Gekko K., Noguchi H. Compressibility of globular proteins in water at 25 °C. J. Phys. Chem. 83:1979;2706-2714.
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 18
    • 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
  • 19
    • 0030371848 scopus 로고    scopus 로고
    • The volume and compressibility changes associated with protein denaturation
    • Hayashi T., Sakurai M., Nitta K. The volume and compressibility changes associated with protein denaturation. Chem. Letters. 1996;723-724.
    • (1996) Chem. Letters , pp. 723-724
    • Hayashi, T.1    Sakurai, M.2    Nitta, K.3
  • 20
    • 0000413841 scopus 로고
    • Partial molar compressibilities of organic solutes in water
    • H.-J. Hinz. Heidelberg, New York, Tokyo: Springer-Verlag, Berlin
    • Høiland H. Partial molar compressibilities of organic solutes in water. Hinz H.-J. Thermodynamic Data for Biochemistry and Biotechnology. 1986;129-147 Springer-Verlag, Berlin, Heidelberg, New York, Tokyo.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 129-147
    • Høiland, H.1
  • 21
    • 0001689633 scopus 로고
    • Volumetric properties of aqueous solutions of bovine serum albumin, human serum albumin, and human hemoglobin
    • Iqbal M., Verrall R. E. Volumetric properties of aqueous solutions of bovine serum albumin, human serum albumin, and human hemoglobin. J. Phys. Chem. 91:1987;1935-1941.
    • (1987) J. Phys. Chem. , vol.91 , pp. 1935-1941
    • Iqbal, M.1    Verrall, R.E.2
  • 22
    • 21944444619 scopus 로고    scopus 로고
    • Compressibility and volume changes of lysozyme due to guanidine hydrochloride denaturation
    • Kamiyama T., Gekko K. Compressibility and volume changes of lysozyme due to guanidine hydrochloride denaturation. Chem. Letters. 1997;1063-1064.
    • (1997) Chem. Letters , pp. 1063-1064
    • Kamiyama, T.1    Gekko, K.2
  • 23
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Advan. Protein Chem. 14:1959;1-66.
    • (1959) Advan. Protein Chem. , vol.14 , pp. 1-66
    • Kauzmann, W.1
  • 24
    • 36849150819 scopus 로고
    • Thermodynamics of unfolding
    • Kauzmann W. Thermodynamics of unfolding. Nature. 325:1987;763-764.
    • (1987) Nature , vol.325 , pp. 763-764
    • Kauzmann, W.1
  • 25
    • 0030787855 scopus 로고    scopus 로고
    • Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure
    • Kharakoz D. P. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry. 36:1997;10276-10285.
    • (1997) Biochemistry , vol.36 , pp. 10276-10285
    • Kharakoz, D.P.1
  • 26
    • 0027535729 scopus 로고
    • Hydrational and intrinsic compressibilities of globular proteins
    • Kharakoz D. P., Sarvazyan A. P. Hydrational and intrinsic compressibilities of globular proteins. Biopolymers. 33:1993;11-26.
    • (1993) Biopolymers , vol.33 , pp. 11-26
    • Kharakoz, D.P.1    Sarvazyan, A.P.2
  • 27
    • 0015237085 scopus 로고
    • On the nature of the protein interior
    • Klapper M. H. On the nature of the protein interior. Biochim. Biophys. Acta. 229:1971;557-566.
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 557-566
    • Klapper, M.H.1
  • 29
    • 0026018045 scopus 로고
    • Isoenthalpic and isoentropic temperatures and the thermodynamics of protein denaturation
    • Lee B. Isoenthalpic and isoentropic temperatures and the thermodynamics of protein denaturation. Proc. Natl Acad. Sci. USA. 88:1991;5154-5158.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5154-5158
    • Lee, B.1
  • 30
    • 0015950174 scopus 로고
    • Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride
    • Lee J. C., Timasheff S. N. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry. 13:1974;257-265.
    • (1974) Biochemistry , vol.13 , pp. 257-265
    • Lee, J.C.1    Timasheff, S.N.2
  • 31
    • 0017054059 scopus 로고
    • Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme
    • Li T. M., Hook J. W., Drickamer H. G., Weber G. Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme. Biochemistry. 15:1976;5571-5580.
    • (1976) Biochemistry , vol.15 , pp. 5571-5580
    • Li, T.M.1    Hook, J.W.2    Drickamer, H.G.3    Weber, G.4
  • 32
    • 0017185649 scopus 로고
    • Partial specific volume, expansibility, compressibility, and heat capacity of aqueous lysozyme solutions
    • Millero F. J., Ward G. K., Chetirkin P. Partial specific volume, expansibility, compressibility, and heat capacity of aqueous lysozyme solutions. J. Biol. Chem. 251:1976;4001-4004.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4001-4004
    • Millero, F.J.1    Ward, G.K.2    Chetirkin, P.3
  • 33
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea-denatured protein, the 434-repressor
    • Neri D., Billeter M., Wider G., Wüthrich K. NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science. 257:1992;1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wüthrich, K.4
  • 34
    • 0027373133 scopus 로고
    • Adiabatic compressibility of molten globules
    • Nölting B., Sligar S. G. Adiabatic compressibility of molten globules. Biochemistry. 32:1993;12319-12323.
    • (1993) Biochemistry , vol.32 , pp. 12319-12323
    • Nölting, B.1    Sligar, S.G.2
  • 35
    • 0015438810 scopus 로고
    • The preparation of guanidine hydrochloride
    • Nozaki Y. The preparation of guanidine hydrochloride. Methods Enzymol. 26:1972;43-50.
    • (1972) Methods Enzymol , vol.26 , pp. 43-50
    • Nozaki, Y.1
  • 36
    • 0025271463 scopus 로고
    • PH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
    • Pace C. N., Laurents D. V., Thomson J. A. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry. 29:1990;2564-2572.
    • (1990) Biochemistry , vol.29 , pp. 2564-2572
    • Pace, C.N.1    Laurents, D.V.2    Thomson, J.A.3
  • 37
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein structure
    • Richards F. M. Areas, volumes, packing, and protein structure. Annu. Rev. Biophys. Bioeng. 6:1977;151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 38
    • 0001779639 scopus 로고
    • Partial molar volumes in aqueous mixtures of nonelectrolytes. 1. t -butyl alcohol
    • Sakurai M. Partial molar volumes in aqueous mixtures of nonelectrolytes. 1. t -butyl alcohol. Bull. Chem. Soc. Jpn. 60:1987;1-7.
    • (1987) Bull. Chem. Soc. Jpn. , vol.60 , pp. 1-7
    • Sakurai, M.1
  • 40
    • 0000303539 scopus 로고
    • Apparent molar volumes and apparent molar adiabatic compressions of water in some alcohols
    • Sakurai M., Nakamura K., Takenaka N. Apparent molar volumes and apparent molar adiabatic compressions of water in some alcohols. Bull. Chem. Soc. Jpn. 67:1994;352-359.
    • (1994) Bull. Chem. Soc. Jpn. , vol.67 , pp. 352-359
    • Sakurai, M.1    Nakamura, K.2    Takenaka, N.3
  • 41
    • 0029221283 scopus 로고
    • Sound velocities and apparent molar adiabatic compressions of alcohols in dilute aqueous solutions
    • Sakurai M., Nakamura K., Nitta K. Sound velocities and apparent molar adiabatic compressions of alcohols in dilute aqueous solutions. J. Chem. Eng. Data. 40:1995;301-310.
    • (1995) J. Chem. Eng. Data , vol.40 , pp. 301-310
    • Sakurai, M.1    Nakamura, K.2    Nitta, K.3
  • 42
    • 0026781884 scopus 로고
    • High-resolution NMR study of the pressure-induced unfolding of lysozyme
    • Samarasinghe S. D., Campbell D. M., Jonas A., Jonas J. High-resolution NMR study of the pressure-induced unfolding of lysozyme. Biochemistry. 31:1992;7773-7778.
    • (1992) Biochemistry , vol.31 , pp. 7773-7778
    • Samarasinghe, S.D.1    Campbell, D.M.2    Jonas, A.3    Jonas, J.4
  • 43
    • 84985713724 scopus 로고
    • Relaxational contributions to protein compressibility from ultrasonic data
    • Sarvazyan A. P., Hemmes P. Relaxational contributions to protein compressibility from ultrasonic data. Biopolymers. 18:1979;3015-3024.
    • (1979) Biopolymers , vol.18 , pp. 3015-3024
    • Sarvazyan, A.P.1    Hemmes, P.2
  • 44
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle D. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10:1996;27-34.
    • (1996) FASEB J. , vol.10 , pp. 27-34
    • Shortle, D.1
  • 45
    • 0015530494 scopus 로고
    • A dilatometric study of the denaturation of lysozyme by guanidine hydrochloride and hydrochloric acid
    • Skerjanc J., Lapanje S. A dilatometric study of the denaturation of lysozyme by guanidine hydrochloride and hydrochloric acid. Eur. J. Biochem. 25:1972;49-53.
    • (1972) Eur. J. Biochem. , vol.25 , pp. 49-53
    • Skerjanc, J.1    Lapanje, S.2
  • 46
    • 0026733250 scopus 로고
    • Denatured states of ribonuclease A have compact dimensions and residual secondary structure
    • Sosnick T. R., Trewhella J. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry. 31:1992;8329-8335.
    • (1992) Biochemistry , vol.31 , pp. 8329-8335
    • Sosnick, T.R.1    Trewhella, J.2
  • 47
    • 0028925816 scopus 로고
    • Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
    • Tamura Y., Gekko K. Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility. Biochemistry. 34:1995;1878-1884.
    • (1995) Biochemistry , vol.34 , pp. 1878-1884
    • Tamura, Y.1    Gekko, K.2
  • 48
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;121-282.
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 49
    • 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


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