메뉴 건너뛰기




Volumn 274, Issue 2, 1997, Pages 237-252

The native and the heat-induced denatured states of α-Chymotrypsinogen A: Thermodynamic and spectroscopic studies

Author keywords

Molten globule; Partial adiabatic compressibility; Partial volume; Protein folding; chymotrypsinogen A

Indexed keywords

CHYMOTRYPSINOGEN;

EID: 0343247668     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1394     Document Type: Article
Times cited : (76)

References (57)
  • 1
    • 0001384941 scopus 로고
    • The velocity of sound in electrolytic solutions
    • Barnartt S. The velocity of sound in electrolytic solutions. J. Chem. Phys. 20:1952;278-279.
    • (1952) J. Chem. Phys. , vol.20 , pp. 278-279
    • Barnartt, S.1
  • 2
    • 33947481462 scopus 로고
    • The thermodynamics of protein denaturation. I. The denaturation of chymo trypsinogen
    • Brandts J. F. The thermodynamics of protein denaturation. I. The denaturation of chymo trypsinogen. J. Am. Chem. Soc. 86:1964a;4291-4301.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 4291-4301
    • Brandts, J.F.1
  • 3
    • 0001059847 scopus 로고
    • The thermodynamics of protein denaturation. II. A model of reversible denaturation and interpretations regarding the stability of chymotrypsinogen
    • Brandts J. F. The thermodynamics of protein denaturation. II. A model of reversible denaturation and interpretations regarding the stability of chymotrypsinogen. J. Am. Chem. Soc. 86:1964b;4302-4314.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 4302-4314
    • Brandts, J.F.1
  • 4
    • 0343115278 scopus 로고
    • The reversible thermal denaturation of chymotrypsinogen, I. Experimental characterization
    • Brandts J., Lumry R. The reversible thermal denaturation of chymotrypsinogen, I. Experimental characterization. J. Phys. Chem. 67:1963;1484-1494.
    • (1963) J. Phys. Chem. , vol.67 , pp. 1484-1494
    • Brandts, J.1    Lumry, R.2
  • 5
    • 0002659517 scopus 로고
    • Methods for obtaining thermodynamic data on oligonucleotide transitions
    • Heidelberg, New York, Tokyo: Springer-Verlag, Berlin
    • Breslauer K. J. Methods for obtaining thermodynamic data on oligonucleotide transitions. Thermodynamic Data for Biochemistry and Biotechnology. 1986;Springer-Verlag, Berlin, Heidelberg, New York, Tokyo.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology
    • Breslauer, K.J.1
  • 6
    • 0343115280 scopus 로고
    • Extracting thermodynamic data from equilibrium melting curves for oligonucleotide order-disorder transitions
    • S. Agrawal. Totowa: Humana Press Inc.
    • Breslauer K. J. Extracting thermodynamic data from equilibrium melting curves for oligonucleotide order-disorder transitions. Agrawal S. Methods in Molecular Biology, vol. 26: Protocols for Oligonucleotide Conjugates. 1994;Humana Press Inc. Totowa.
    • (1994) Methods in Molecular Biology, Vol. 26: Protocols for Oligonucleotide Conjugates
    • Breslauer, K.J.1
  • 7
    • 0015713752 scopus 로고
    • Temperature dependence of partial volumes of proteins
    • Bull H. B., Breese K. Temperature dependence of partial volumes of proteins. Biopolymers. 12:1973;2351-2358.
    • (1973) Biopolymers , vol.12 , pp. 2351-2358
    • Bull, H.B.1    Breese, K.2
  • 8
    • 0030034601 scopus 로고    scopus 로고
    • Compressibility as a unique means to detect and characterize globular protein states
    • Chalikian T. V., Breslauer K. J. Compressibility as a unique 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
  • 9
    • 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
  • 11
    • 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. 51:1994a;89-109.
    • (1994) Biophys. Chem. , vol.51 , pp. 89-109
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 13
    • 0029011017 scopus 로고
    • Volumetric characterizations of the native, molten globule, and unfolded states of cytochrome c at acidic pH
    • Chalikian T. V., Gindikin V. S., Breslauer K. J. Volumetric characterizations 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
  • 14
    • 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
  • 15
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility: 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: 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
  • 16
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • H.-J. Hinz. Heidelberg, New York, Tokyo: Springer-Verlag, Berlin
    • Durchschlag H. Specific volumes of biological macromolecules and some other molecules of biological interest. Hinz H.-J. Thermodynamic Data for Biochemistry and Biotechnology. 1986;Springer-Verlag, Berlin, Heidelberg, New York, Tokyo.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology
    • Durchschlag, H.1
  • 17
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink A. L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 18
    • 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
  • 20
    • 0029132790 scopus 로고
    • Thermodynamics of partly folded intermediates in proteins
    • Freire E. Thermodynamics of partly folded intermediates in proteins. Annu. Rev. Biophys. Biomol. Struct. 24:1995;141-165.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 141-165
    • Freire, E.1
  • 21
    • 0014965896 scopus 로고
    • Chymotrypsinogen: 2.5-Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation
    • Freer S. T., Kraut J., Robertus J. D., Wright H. T., Xuong Ng. H. Chymotrypsinogen: 2.5-Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation. Biochemistry. 9:1970;1997-2009.
    • (1970) Biochemistry , vol.9 , pp. 1997-2009
    • Freer, S.T.1    Kraut, J.2    Robertus, J.D.3    Wright, H.T.4    Xuong Ng., H.5
  • 22
    • 0026315736 scopus 로고
    • Effect of reductive alkylation on thermal stability of ribonuclease A and chymotrypsinogen A
    • Fujita Y., Noda Y. Effect of reductive alkylation on thermal stability of ribonuclease A and chymotrypsinogen A. Int. J. Pept. Protein Res. 38:1991;445-452.
    • (1991) Int. J. Pept. Protein Res. , vol.38 , pp. 445-452
    • Fujita, Y.1    Noda, Y.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0028174361 scopus 로고
    • Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study
    • Griko Yu. V., Freire E., Privalov P. L. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry. 33:1994;1889-1899.
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko Yu., V.1    Freire, E.2    Privalov, P.L.3
  • 27
    • 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
  • 28
    • 0001202494 scopus 로고
    • Amino acid sequence of bovine chymotrypsinogen-A
    • Hartley B. S. Amino acid sequence of bovine chymotrypsinogen-A. Nature. 201:1964;1284-1287.
    • (1964) Nature , vol.201 , pp. 1284-1287
    • Hartley, B.S.1
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0014963345 scopus 로고
    • Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation
    • Jackson W. A., Brandts J. F. Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation. Biochemistry. 9:1970;2294-2301.
    • (1970) Biochemistry , vol.9 , pp. 2294-2301
    • Jackson, W.A.1    Brandts, J.F.2
  • 32
    • 0018339835 scopus 로고
    • The interpretation of near-ultraviolet circular dichroism
    • Kahn P. C. The interpretation of near-ultraviolet circular dichroism. Methods Enzymol. 61:1979;339-378.
    • (1979) Methods Enzymol. , vol.61 , pp. 339-378
    • Kahn, P.C.1
  • 33
    • 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;1-63.
    • (1959) Advan. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 34
    • 0024438754 scopus 로고
    • Volumetric properties of proteins and their analogs in diluted water solutions. 1. Partial volumes of amino acids at 15-55°C
    • Kharakoz D. P. Volumetric properties of proteins and their analogs in diluted water solutions. 1. Partial volumes of amino acids at 15-55°C. Biophys. Chem. 34:1989;115-125.
    • (1989) Biophys. Chem. , vol.34 , pp. 115-125
    • Kharakoz, D.P.1
  • 35
    • 0342578230 scopus 로고
    • Hydration and adiabatic compressibility changes of α-chymotrypsinogen denaturation
    • Kharakoz D. P., Sarvazyan A. P. Hydration and adiabatic compressibility changes of α-chymotrypsinogen denaturation. Studia Biophys. 79:1980;179-180.
    • (1980) Studia Biophys. , vol.79 , pp. 179-180
    • Kharakoz, D.P.1    Sarvazyan, A.P.2
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • Marky L. A., Breslauer K. J. Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers. 26:1987;1601-1620.
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Breslauer, K.J.2
  • 40
    • 0001054914 scopus 로고
    • Standard partial molal compressibilities by ultrasonics. 1. Sodium chloride and potassium chloride at 25°C
    • Owen B. B., Simons H. L. Standard partial molal compressibilities by ultrasonics. 1. Sodium chloride and potassium chloride at 25°C. J. Phys. Chem. 61:1957;479-482.
    • (1957) J. Phys. Chem. , vol.61 , pp. 479-482
    • Owen, B.B.1    Simons, H.L.2
  • 41
    • 0028180536 scopus 로고
    • Denaturation behavior of α-chymotrypsinogen A in urea and alkylurea solutions: Fluorescence studies
    • Poklar N., Vesnaver G., Lapanje S. Denaturation behavior of α-chymotrypsinogen A in urea and alkylurea solutions: fluorescence studies. J. Protein Chem. 13:1994;323-331.
    • (1994) J. Protein Chem. , vol.13 , pp. 323-331
    • Poklar, N.1    Vesnaver, G.2    Lapanje, S.3
  • 42
    • 0029417045 scopus 로고
    • Thermodynamics of denaturation of α-chymotrypsinogen A in aqueous urea and alkylurea solutions
    • Poklar N., Vesnaver G., Lapanje S. Thermodynamics of denaturation of α-chymotrypsinogen A in aqueous urea and alkylurea solutions. J. Protein Chem. 14:1995;709-719.
    • (1995) J. Protein Chem. , vol.14 , pp. 709-719
    • Poklar, N.1    Vesnaver, G.2    Lapanje, S.3
  • 43
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • Privalov P. L. Stability of proteins. Small globular proteins. Advan. Protein Chem. 33:1979;167-241.
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 44
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease, and myoglobin
    • Privalov P. L., Khechinashvili N. N., Atanasov B. P. Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease, and myoglobin. Biopolymers. 10:1971;1865-1890.
    • (1971) Biopolymers , vol.10 , pp. 1865-1890
    • Privalov, P.L.1    Khechinashvili, N.N.2    Atanasov, B.P.3
  • 45
    • 0028227065 scopus 로고
    • Kinetic and equilibrium intermediates in protein folding
    • Ptitsyn O. B. Kinetic and equilibrium intermediates in protein folding. Protein Eng. 7:1994;593-596.
    • (1994) Protein Eng. , vol.7 , pp. 593-596
    • Ptitsyn, O.B.1
  • 46
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O. B. Molten globule and protein folding. Advan. Protein Chem. 47:1995a;83-229.
    • (1995) Advan. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 47
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn O. B. Structures of folding intermediates. Curr. Opin. Struct. Biol. 5:1995b;74-78.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 48
    • 0028222021 scopus 로고
    • The molten globule is a third thermodynamical state of protein molecules
    • Ptitsyn O. B., Uversky V. N. The molten globule is a third thermodynamical state of protein molecules. FEBS Letters. 341:1994;15-18.
    • (1994) FEBS Letters , vol.341 , pp. 15-18
    • Ptitsyn, O.B.1    Uversky, V.N.2
  • 49
    • 0025855018 scopus 로고
    • Ultrasonic velocimetry of biological compounds
    • Sarvazyan A. P. Ultrasonic velocimetry of biological compounds. Annu. Rev. Biophys. Biophys. Chem. 20:1991;321-342.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 321-342
    • Sarvazyan, A.P.1
  • 50
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R. S., Record M. T. Jr. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:1994;777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record M.T., Jr.2
  • 51
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant J. M. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38:1987;463-488.
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 53
    • 0000697562 scopus 로고
    • Proteins as random coils. I Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
    • Tanford C., Kawahara K., Lapanje S. Proteins as random coils. I Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. J. Am. Chem. Soc. 89:1967;729-736.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 729-736
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 56
    • 0021930156 scopus 로고
    • Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution
    • Wang D., Bode W., Huber R. Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution. J. Mol. Biol. 185:1985;595-624.
    • (1985) J. Mol. Biol. , vol.185 , pp. 595-624
    • Wang, D.1    Bode, W.2    Huber, R.3
  • 57
    • 0021195067 scopus 로고
    • Amino acid, peptide, and protein volume in solution
    • Zamyatnin A. A. Amino acid, peptide, and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13:1984;145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.