메뉴 건너뛰기




Volumn 79, Issue 3, 2000, Pages 269-280

Interpretation of DSC data on protein denaturation complicated by kinetic and irreversible effects

Author keywords

Kinetics and thermodynamics of denaturation; pH dependences; Scanning calorimetry

Indexed keywords

RIBULOSEBISPHOSPHATE CARBOXYLASE; SOYBEAN TRYPSIN INHIBITOR;

EID: 0034717059     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(00)00243-1     Document Type: Conference Paper
Times cited : (39)

References (44)
  • 1
    • 0026766543 scopus 로고
    • Differential scanning calorimetric study of the thermal unfolding of β-lactamase I from Bacillus cereus
    • Arriaga P., Menendez M., Villacorta J.M., Laynez J. Differential scanning calorimetric study of the thermal unfolding of β-lactamase I from Bacillus cereus. Biochemistry. 31:1992;6603-6607.
    • (1992) Biochemistry , vol.31 , pp. 6603-6607
    • Arriaga, P.1    Menendez, M.2    Villacorta, J.M.3    Laynez, J.4
  • 2
    • 0017625157 scopus 로고
    • On the changes in α-chymotrypsin stability after its modification by polyelectrolytes
    • Bessmertnaya L.Y., Kozlov L.V., Antonov V.K. On the changes in α-chymotrypsin stability after its modification by polyelectrolytes. Biokhimia (Moscow). 42:1977;1825-1833.
    • (1977) Biokhimia (Moscow) , vol.42 , pp. 1825-1833
    • Bessmertnaya, L.Y.1    Kozlov, L.V.2    Antonov, V.K.3
  • 3
    • 0343179529 scopus 로고
    • Conformation stability of ribulosediphosphate carboxylase of alfalfa green leafs according to the data of differential scanning microcalorimetry
    • Burova T.V., Soshinsky A.A., Danilenko A.N., Antonov Y.A., Grinberg V.Y., Tolstoguzov V.B. Conformation stability of ribulosediphosphate carboxylase of alfalfa green leafs according to the data of differential scanning microcalorimetry. Biofizika (Moscow). 34:1989;545-549.
    • (1989) Biofizika (Moscow) , vol.34 , pp. 545-549
    • Burova, T.V.1    Soshinsky, A.A.2    Danilenko, A.N.3    Antonov, Y.A.4    Grinberg, V.Y.5    Tolstoguzov, V.B.6
  • 5
    • 0026516732 scopus 로고
    • Study of the conformational stability of 7S globulin from French beans (phaseolin) using high-sensitivity differential scanning microcalorimetry
    • Burova T.V., Grinberg N.V., Grinberg V.Y., Tolstoguzov V.B., Schlesier B., Müntz K. Study of the conformational stability of 7S globulin from French beans (phaseolin) using high-sensitivity differential scanning microcalorimetry. Int. J. Biol. Macromol. 14:1992;2-8.
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 2-8
    • Burova, T.V.1    Grinberg, N.V.2    Grinberg, V.Y.3    Tolstoguzov, V.B.4    Schlesier, B.5    Müntz, K.6
  • 7
    • 0343179528 scopus 로고
    • Effect of pH on conformational stability of 11S globulin from Glycine max seeds according to differential scanning microcalorimetry
    • Danilenko A.N., Bikbov T.M., Grinberg V.Y., Leontyev A.L., Burova T.V., Surikov V.V. et al. Effect of pH on conformational stability of 11S globulin from Glycine max seeds according to differential scanning microcalorimetry. Biofizika (Moscow). 32:1987;402-406.
    • (1987) Biofizika (Moscow) , vol.32 , pp. 402-406
    • Danilenko, A.N.1    Bikbov, T.M.2    Grinberg, V.Y.3    Leontyev, A.L.4    Burova, T.V.5    Surikov, V.V.6
  • 8
    • 0019331938 scopus 로고
    • A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoglobulin. Thermal behaviour at temperatures up to 100°C
    • de Wit J.N., Swinkels G.A. A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoglobulin. Thermal behaviour at temperatures up to 100°C. Biochim. Biophys. Acta. 624:1980;40-50.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 40-50
    • De Wit, J.N.1    Swinkels, G.A.2
  • 10
    • 0039209990 scopus 로고
    • Thermotropic gelation of ovalbumin. 2. Boundary conditions on the formation and the concentration dependence of equilibrium elastic modulus for thermotropic ovalbumin gels
    • Grinberg N., Bikbov T., Grinberg V., Chaika T., Vaintraub I., Tolstoguzov V. Thermotropic gelation of ovalbumin. 2. Boundary conditions on the formation and the concentration dependence of equilibrium elastic modulus for thermotropic ovalbumin gels. Int. J. Biol. Macromol. 1:1985;152-160.
    • (1985) Int. J. Biol. Macromol. , vol.1 , pp. 152-160
    • Grinberg, N.1    Bikbov, T.2    Grinberg, V.3    Chaika, T.4    Vaintraub, I.5    Tolstoguzov, V.6
  • 12
    • 0019542905 scopus 로고
    • 2S globulins of soybean seeds. 2. Physicochemical and biological properties of protease inhibitors in 2S globulins
    • Koshiyama I., Kikuchi M., Fukushima D. 2S globulins of soybean seeds. 2. Physicochemical and biological properties of protease inhibitors in 2S globulins. J. Agric. Food Chem. 29:1981;340-343.
    • (1981) J. Agric. Food Chem. , vol.29 , pp. 340-343
    • Koshiyama, I.1    Kikuchi, M.2    Fukushima, D.3
  • 14
    • 0016267373 scopus 로고
    • Multiple peptide composition of the large and small subunits of Nicotiana tabacum fraction I protein ascertained by fingerprinting and electrofocusing
    • Kung S.D., Sakano K., Wildman S.G. Multiple peptide composition of the large and small subunits of Nicotiana tabacum fraction I protein ascertained by fingerprinting and electrofocusing. Biochim. Biophys. Acta. 365:1974;138-147.
    • (1974) Biochim. Biophys. Acta , vol.365 , pp. 138-147
    • Kung, S.D.1    Sakano, K.2    Wildman, S.G.3
  • 15
    • 0000795704 scopus 로고
    • Crystalline soybean trypsin inhibitor. II. General properties
    • Kunitz M. Crystalline soybean trypsin inhibitor. II. General properties. J. Gen. Physiol. 30:1947;291-310.
    • (1947) J. Gen. Physiol. , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 16
    • 84932031374 scopus 로고
    • The kinetics and thermodynamics of reversible denaturation of crystalline soybean trypsin inhibitor
    • Kunitz M. The kinetics and thermodynamics of reversible denaturation of crystalline soybean trypsin inhibitor. J. Gen. Physiol. 32:1948;241-263.
    • (1948) J. Gen. Physiol. , vol.32 , pp. 241-263
    • Kunitz, M.1
  • 17
    • 33947455928 scopus 로고
    • Thermodynamic considerations of protein reactions. 1. Modified reactivity of polar groups
    • Laskowski M., Scheraga H.A. Thermodynamic considerations of protein reactions. 1. Modified reactivity of polar groups. J. Am. Chem. Soc. 76:1954;6305-6319.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 6305-6319
    • Laskowski, M.1    Scheraga, H.A.2
  • 18
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • Lepock J.R., Ritchie K.P., Kolios M.C., Rodahl M., Heinz K.A., Kruuv J. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry. 31:1992;12706-12712.
    • (1992) Biochemistry , vol.31 , pp. 12706-12712
    • Lepock, J.R.1    Ritchie, K.P.2    Kolios, M.C.3    Rodahl, M.4    Heinz, K.A.5    Kruuv, J.6
  • 20
    • 0003635465 scopus 로고
    • Thermodynamic and kinetic aspects of protein conformations in relation to the physiological functions
    • S.N. Timasheff, & G.D. Fasman. Moscow: Mir
    • Lumry R., Biltonen R. Thermodynamic and kinetic aspects of protein conformations in relation to the physiological functions. Timasheff S.N., Fasman G.D. Structure and Stability of Biological Macromolecules. 1973;7-173 Mir, Moscow.
    • (1973) Structure and Stability of Biological Macromolecules , pp. 7-173
    • Lumry, R.1    Biltonen, R.2
  • 21
    • 0014722597 scopus 로고
    • Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water
    • Lumry R., Rajender S. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers. 9:1970;1125-1227.
    • (1970) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 22
    • 0032045188 scopus 로고    scopus 로고
    • Modelling of irreversible thermal protein denaturation under variable temperatures. 1. The model involving two consecutive irreversible steps
    • Lyubarev A.E., Kurganov B.I. Modelling of irreversible thermal protein denaturation under variable temperatures. 1. The model involving two consecutive irreversible steps. Biokhimia (Moscow). 63:1998;516-523.
    • (1998) Biokhimia (Moscow) , vol.63 , pp. 516-523
    • Lyubarev, A.E.1    Kurganov, B.I.2
  • 23
    • 0020670459 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase-oxygenase
    • Miziorko H.M., Lorimer G.H. Ribulose-1,5-bisphosphate carboxylase-oxygenase. Ann. Rev. Biochem. 52:1983;507-535.
    • (1983) Ann. Rev. Biochem. , vol.52 , pp. 507-535
    • Miziorko, H.M.1    Lorimer, G.H.2
  • 24
    • 0021095863 scopus 로고
    • Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters
    • Moses E., Hinz H.J. Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters. J. Mol. Biol. 170:1983;765-776.
    • (1983) J. Mol. Biol. , vol.170 , pp. 765-776
    • Moses, E.1    Hinz, H.J.2
  • 25
    • 0342698229 scopus 로고
    • Thermodynamic study of shrinkage in fibers made from insulin
    • Nakajima A., Scheraga H.A. Thermodynamic study of shrinkage in fibers made from insulin. J. Am. Chem. Soc. 83:1961;1585-1589.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 1585-1589
    • Nakajima, A.1    Scheraga, H.A.2
  • 26
    • 0017042362 scopus 로고
    • Study of thermal denaturation of lysozyme and other globular proteins by light-scattering spectroscopy
    • Nicoli D.F., Benedek G.B. Study of thermal denaturation of lysozyme and other globular proteins by light-scattering spectroscopy. Biopolymers. 15:1976;2421-2437.
    • (1976) Biopolymers , vol.15 , pp. 2421-2437
    • Nicoli, D.F.1    Benedek, G.B.2
  • 27
    • 0343012481 scopus 로고
    • Conformational changes in proteins
    • M.M. Jones. Moscow: Mir
    • Pfeil W., Privalov P.L. Conformational changes in proteins. Jones M.M. Biochemical Thermodynamics. 1982;5-139 Mir, Moscow.
    • (1982) Biochemical Thermodynamics , pp. 5-139
    • Pfeil, W.1    Privalov, P.L.2
  • 28
    • 0014378401 scopus 로고
    • Kinetics of reversible denaturation of trypsin in water and water-ethanol mixtures
    • Pohl F.M. Kinetics of reversible denaturation of trypsin in water and water-ethanol mixtures. Eur. J. Biochem. 7:1968;146-152.
    • (1968) Eur. J. Biochem. , vol.7 , pp. 146-152
    • Pohl, F.M.1
  • 29
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • Privalov P.L. Stability of proteins. Small globular proteins. Adv. Protein Chem. 33:1979;167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 30
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov P.L. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35:1982;1-104.
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 31
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov P.L., Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86:1974;665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 32
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61:1992;921-935.
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 33
    • 0005319527 scopus 로고
    • Intramolecular bonds in proteins. 2. Noncovalent bonds
    • H. Neurath. New York: Academic Press
    • Scheraga H.A. Intramolecular bonds in proteins. 2. Noncovalent bonds. Neurath H. The Proteins. 1963;477-593 Academic Press, New York.
    • (1963) The Proteins , pp. 477-593
    • Scheraga, H.A.1
  • 35
    • 0016174105 scopus 로고
    • Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 A resolution
    • Sweet R.M., Wright H.T., Janin J., Chothia C.H., Blow D.M. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 A resolution. Biochemistry. 13:1974;4212-4228.
    • (1974) Biochemistry , vol.13 , pp. 4212-4228
    • Sweet, R.M.1    Wright, H.T.2    Janin, J.3    Chothia, C.H.4    Blow, D.M.5
  • 36
    • 0019840442 scopus 로고
    • Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex
    • Takahashi K., Sturtevant J.M. Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex. Biochemistry. 20:1981;6185-6190.
    • (1981) Biochemistry , vol.20 , pp. 6185-6190
    • Takahashi, K.1    Sturtevant, J.M.2
  • 37
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Adv. Protein Chem. 23:1968;121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 38
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24:1970;1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 39
    • 0028871971 scopus 로고
    • Effect of irreversibility on the thermodynamic characterization of the thermal denaturation of Aspergillus saitoi acid proteinase
    • Tello Solis S.R., Hernandez Arana A. Effect of irreversibility on the thermodynamic characterization of the thermal denaturation of Aspergillus saitoi acid proteinase. Biochem. J. 311:1995;969-974.
    • (1995) Biochem. J. , vol.311 , pp. 969-974
    • Tello Solis, S.R.1    Hernandez Arana, A.2
  • 40
    • 0343568457 scopus 로고
    • Kinetic study of conformational transitions of bovine liver catalase
    • Troshkina T.V., Lichtenstein G.I. Kinetic study of conformational transitions of bovine liver catalase. Mol. Biol. (in Russian). 2:1968;663-670.
    • (1968) Mol. Biol. (In Russian) , vol.2 , pp. 663-670
    • Troshkina, T.V.1    Lichtenstein, G.I.2
  • 41
    • 0032496332 scopus 로고    scopus 로고
    • Irreversible phase transition of firefly luciferase: Contrasting effects of volatile anesthetics and myristic acid
    • Ueda I., Suzuki A. Irreversible phase transition of firefly luciferase: contrasting effects of volatile anesthetics and myristic acid. Biochim. Biophys. Acta. 1380:1998;313-319.
    • (1998) Biochim. Biophys. Acta , vol.1380 , pp. 313-319
    • Ueda, I.1    Suzuki, A.2
  • 42
    • 0024723571 scopus 로고
    • Thermodynamic and kinetic study of thermal denaturation of Kunitz soybean trypsin inhibitor by differential scanning microcalorimetry
    • Varfolomeeva E.P., Burova T.V., Grinberg V.Y., Tolstoguzov V.B. Thermodynamic and kinetic study of thermal denaturation of Kunitz soybean trypsin inhibitor by differential scanning microcalorimetry. Mol. Biol. (Moscow). 23:1989;1000-1008.
    • (1989) Mol. Biol. (Moscow) , vol.23 , pp. 1000-1008
    • Varfolomeeva, E.P.1    Burova, T.V.2    Grinberg, V.Y.3    Tolstoguzov, V.B.4
  • 43
    • 0000800921 scopus 로고
    • Studies of soybean trypsin inhibitor. 1. Physicochemical properties
    • Wu Y.V., Scheraga H.A. Studies of soybean trypsin inhibitor. 1. Physicochemical properties. Biochemistry. 1:1962;905-911.
    • (1962) Biochemistry , vol.1 , pp. 905-911
    • Wu, Y.V.1    Scheraga, H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.