메뉴 건너뛰기




Volumn 77, Issue 2, 1999, Pages 1052-1063

A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant

Author keywords

[No Author keywords available]

Indexed keywords

AZURIN; MUTANT PROTEIN;

EID: 0032773241     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76955-9     Document Type: Article
Times cited : (49)

References (51)
  • 1
    • 0000408369 scopus 로고
    • Correlated distribution in g and A tensors at a biologically active low-symmetry cupric site
    • Aqualino, A., A. S. Brill, G. F. Bryce, and B. S. Gerstman. 1991. Correlated distribution in g and A tensors at a biologically active low-symmetry cupric site. Phys. Rev. A. 44:5257-5271.
    • (1991) Phys. Rev. A , vol.44 , pp. 5257-5271
    • Aqualino, A.1    Brill, A.S.2    Bryce, G.F.3    Gerstman, B.S.4
  • 2
    • 0029164501 scopus 로고
    • Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa
    • Bonander, N., B. G. Karlsson, and T. Vanngård. 1995. Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa. Biochim. Biophys. Acta. 1251:48-54.
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 48-54
    • Bonander, N.1    Karlsson, B.G.2    Vanngård, T.3
  • 3
    • 0023130391 scopus 로고
    • The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide
    • Canters, G. W. 1987. The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. FEBS Lett. 212:168-172.
    • (1987) FEBS Lett. , vol.212 , pp. 168-172
    • Canters, G.W.1
  • 4
    • 0027155577 scopus 로고
    • Engineering disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke, J., and A. R. Fersht. 1993. Engineering disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry. 32:4322-4329.
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 5
    • 0025801444 scopus 로고
    • A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of Phage T4 lysozyme
    • Connelly, P., L. Ghosaini, C. Q. Hu, S. Kitamura, A. Tanaka, and J. M. Sturtevant. 1991. A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of Phage T4 lysozyme. Biochemistry. 30:1887-1895.
    • (1991) Biochemistry , vol.30 , pp. 1887-1895
    • Connelly, P.1    Ghosaini, L.2    Hu, C.Q.3    Kitamura, S.4    Tanaka, A.5    Sturtevant, J.M.6
  • 6
    • 0026659508 scopus 로고
    • Thermodynamic consequences of the removal of a disulfide bridge from hen lysozyme
    • Cooper, A., S. J. Eyles, S. E. Radford, and C. M. Dobson. 1992, Thermodynamic consequences of the removal of a disulfide bridge from hen lysozyme. J. Mol. Biol. 225:939-943.
    • (1992) J. Mol. Biol. , vol.225 , pp. 939-943
    • Cooper, A.1    Eyles, S.J.2    Radford, S.E.3    Dobson, C.M.4
  • 7
    • 0016292061 scopus 로고
    • Intermediates in the refolding of reduced bovine pancreatic trypsin inhibitor
    • Creighton, T. E. 1974. Intermediates in the refolding of reduced bovine pancreatic trypsin inhibitor. J. Mol. Biol. 87:579-602.
    • (1974) J. Mol. Biol. , vol.87 , pp. 579-602
    • Creighton, T.E.1
  • 8
    • 0000552763 scopus 로고
    • Folding pathways determined using disulfide bonds
    • T. E. Creighton, editor. W. H. Freeman and Co., New York
    • Creighton, T. E. 1992. Folding pathways determined using disulfide bonds. In Protein Folding. T. E. Creighton, editor. W. H. Freeman and Co., New York. 301-351.
    • (1992) Protein Folding , pp. 301-351
    • Creighton, T.E.1
  • 9
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig, A. J., and D. H. Williams. 1991. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 217:389-398.
    • (1991) J. Mol. Biol. , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 10
    • 0027251102 scopus 로고
    • Kinetic study into the irreversible thermal denaturation of bacteriorhodopsin
    • Galisteo, M. L., and J. M. Sanchez-Ruiz. 1993. Kinetic study into the irreversible thermal denaturation of bacteriorhodopsin. Eur. Biophys. J. 22:25-30.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 25-30
    • Galisteo, M.L.1    Sanchez-Ruiz, J.M.2
  • 11
    • 0028064007 scopus 로고
    • Thermal stabilization of thymidylate synthase by engineering two disulfide bridges across the dimer interface
    • Gokhale, R. S., S. Agarwalla, V. S. Francis, D. V. Santi, and P. Balaram. 1994. Thermal stabilization of thymidylate synthase by engineering two disulfide bridges across the dimer interface. J. Mol. Biol. 235:89-94.
    • (1994) J. Mol. Biol. , vol.235 , pp. 89-94
    • Gokhale, R.S.1    Agarwalla, S.2    Francis, V.S.3    Santi, D.V.4    Balaram, P.5
  • 12
    • 0011978454 scopus 로고
    • Effect of scan rate and protein concentration on DSC thermograms of bovine superoxide dismutase
    • Grasso, D., C. La Rosa, D. Milardi, and S. Fasone. 1995. Effect of scan rate and protein concentration on DSC thermograms of bovine superoxide dismutase. Thermochim. Acta. 265:163-175.
    • (1995) Thermochim. Acta , vol.265 , pp. 163-175
    • Grasso, D.1    La Rosa, C.2    Milardi, D.3    Fasone, S.4
  • 13
    • 0030905218 scopus 로고    scopus 로고
    • Resolving multiple protein conformers in equilibrium unfolding reactions: A time-resolved emission spectroscopic (TRES) study of Azurin
    • Guptasarma, P. 1997. Resolving multiple protein conformers in equilibrium unfolding reactions: a time-resolved emission spectroscopic (TRES) study of Azurin. Biophys. Chem. 65:221-228.
    • (1997) Biophys. Chem. , vol.65 , pp. 221-228
    • Guptasarma, P.1
  • 14
    • 0000580222 scopus 로고
    • Accuracy and precision in protein structure analysis: Restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 Å resolution
    • Guss, J. M., H. D. Bartunik, and H. C. Freeman. 1992. Accuracy and precision in protein structure analysis: restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 Å resolution. Acta Cryst. B48:790-811.
    • (1992) Acta Cryst. , vol.B48 , pp. 790-811
    • Guss, J.M.1    Bartunik, H.D.2    Freeman, H.C.3
  • 15
    • 0029992859 scopus 로고    scopus 로고
    • Experimental model for the thermal denaturation of azurin: A kinetic study
    • Guzzi, R., C. La Rosa, D. Grasso, D. Milardi, and L. Sportelli. 1996. Experimental model for the thermal denaturation of azurin: a kinetic study. Biophys. Chem. 60:29-38.
    • (1996) Biophys. Chem. , vol.60 , pp. 29-38
    • Guzzi, R.1    La Rosa, C.2    Grasso, D.3    Milardi, D.4    Sportelli, L.5
  • 18
    • 0025862426 scopus 로고
    • The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast
    • Inaka, K., Y. Taniyama, M. Kikuchi, K. Morikawa, and M. Matsushima. 1991. The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast. J. Biol. Chem. 266: 12599-12603.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12599-12603
    • Inaka, K.1    Taniyama, Y.2    Kikuchi, M.3    Morikawa, K.4    Matsushima, M.5
  • 20
    • 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. Cryst. 24:946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0000491889 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of globular protein thermal unfolding
    • La Rosa, C., D. Milardi, and D. Grasso. 1998. Thermodynamics and kinetics of globular protein thermal unfolding. Recent Res. Devel. Phys. Chem. 2:175-202.
    • (1998) Recent Res. Devel. Phys. Chem. , vol.2 , pp. 175-202
    • La Rosa, C.1    Milardi, D.2    Grasso, D.3
  • 24
    • 0032498925 scopus 로고    scopus 로고
    • Irreversible thermal denaturation of undine phosphorylase from Escherichia coli K-12
    • Lyubarev, A. E., B. I. Kurganov, A. A. Burlakova, and V. N. Orlov. 1998. Irreversible thermal denaturation of undine phosphorylase from Escherichia coli K-12. Biophys. Chem. 70:247-257.
    • (1998) Biophys. Chem. , vol.70 , pp. 247-257
    • Lyubarev, A.E.1    Kurganov, B.I.2    Burlakova, A.A.3    Orlov, V.N.4
  • 25
    • 0001960802 scopus 로고
    • Electron spin resonance of transition metal complexes
    • R. Carlin, editor. M. Dekker, New York
    • McGarvey, B. R. 1967. Electron spin resonance of transition metal complexes.In Transition Metal Chemistry. Vol. 3. R. Carlin, editor. M. Dekker, New York. 90-201.
    • (1967) Transition Metal Chemistry , vol.3 , pp. 90-201
    • McGarvey, B.R.1
  • 27
    • 0029833191 scopus 로고    scopus 로고
    • Probing the structure and mobility of Pseudomonas aeruginosa azurin by circular dichroism and dynamic fluorescence anisotropy
    • Mei, G., G. Gilardi, M. Venanzi, N. Rosato, G. W. Canters, and A. Finazzi Agrò. 1996. Probing the structure and mobility of Pseudomonas aeruginosa azurin by circular dichroism and dynamic fluorescence anisotropy. Protein Sci. 5:2248-2254.
    • (1996) Protein Sci. , vol.5 , pp. 2248-2254
    • Mei, G.1    Gilardi, G.2    Venanzi, M.3    Rosato, N.4    Canters, G.W.5    Finazzi Agrò, A.6
  • 28
    • 0027938174 scopus 로고
    • Extented theoretical analysis of irreversible protein thermal unfolding
    • Milardi, D., C. La Rosa, and D. Grasso. 1994. Extented theoretical analysis of irreversible protein thermal unfolding. Biophys. Chem. 52:183-189.
    • (1994) Biophys. Chem. , vol.52 , pp. 183-189
    • Milardi, D.1    La Rosa, C.2    Grasso, D.3
  • 29
    • 0008486887 scopus 로고    scopus 로고
    • Contribution of polar and apolar groups to the thermodynamic stability of azurin
    • Milardi, D., S. Fasone, C. La Rosa, and D. Grasso. 1996. Contribution of polar and apolar groups to the thermodynamic stability of azurin. Il Nuovo Cimento. 18:1347-1353
    • (1996) Il Nuovo Cimento , vol.18 , pp. 1347-1353
    • Milardi, D.1    Fasone, S.2    La Rosa, C.3    Grasso, D.4
  • 30
    • 0031434523 scopus 로고    scopus 로고
    • An alternative approach in the structure-based prediction of the thermodynamics of protein unfolding
    • Milardi, D., C. La Rosa, S. Fasone, and D. Grasso. 1997. An alternative approach in the structure-based prediction of the thermodynamics of protein unfolding. Biophys. Chem. 69:43-51.
    • (1997) Biophys. Chem. , vol.69 , pp. 43-51
    • Milardi, D.1    La Rosa, C.2    Fasone, S.3    Grasso, D.4
  • 31
    • 0026344361 scopus 로고
    • Solid model compounds and the thermodynamics of protein unfolding
    • Murphy, P. K, and S. J. Gill. 1991. Solid model compounds and the thermodynamics of protein unfolding. J. Mol. Biol. 222:699-709.
    • (1991) J. Mol. Biol. , vol.222 , pp. 699-709
    • Murphy, P.K.1    Gill, S.J.2
  • 32
    • 0025854571 scopus 로고
    • X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa
    • Nar, H., A. Messerschmidt, and R. Huber. 1991. X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa. J. Mol. Biol. 218:427-447.
    • (1991) J. Mol. Biol. , vol.218 , pp. 427-447
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3
  • 33
    • 0023783477 scopus 로고
    • Conformation stability and activity of ribonuclease T1 with zero, one and two intact disulfide bonds
    • Pace, C. N., G. R. Grimsley, J. A. Thomson, and B. J. Barnett. 1988. Conformation stability and activity of ribonuclease T1 with zero, one and two intact disulfide bonds. J. Biol. Chem. 263:11820-11825.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thomson, J.A.3    Barnett, B.J.4
  • 34
    • 0023659379 scopus 로고
    • Internal motion and electron transfer in proteins: A picosecond fluorescence study of three homologous azurin
    • Petrich, J. W., J. W. Longworth, and G. R. Fleming. 1987. Internal motion and electron transfer in proteins: a picosecond fluorescence study of three homologous azurin. Biochemistry. 26:2711-2722.
    • (1987) Biochemistry , vol.26 , pp. 2711-2722
    • Petrich, J.W.1    Longworth, J.W.2    Fleming, G.R.3
  • 35
    • 0028303486 scopus 로고
    • A rapid and efficient one tube PCR-based mutagenesis technique using Pfu DNA polymerase
    • Picard, P., E. Ersdal-Badju, A. Lu, and S. C. Clark. 1994. A rapid and efficient one tube PCR-based mutagenesis technique using Pfu DNA polymerase. Nucl. Acids Res. 22:2587-2591.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 2587-2591
    • Picard, P.1    Ersdal-Badju, E.2    Lu, A.3    Clark, S.C.4
  • 36
    • 0002693020 scopus 로고
    • Physical basis of the stability of the folded conformations of proteins
    • T. E. Creighton, editor. W. H. Freeman and Co., New York
    • Privalov, P. L. 1992. Physical basis of the stability of the folded conformations of proteins. In Protein Folding. T. E. Creighton, editor. W. H. Freeman and Co., New York. 83-126.
    • (1992) Protein Folding , pp. 83-126
    • Privalov, P.L.1
  • 37
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz J. M. 1992. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61:921-935.
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 38
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the thermal denaturation of Thermolysin
    • Sanchez-Ruiz, J. M., J. L. Lopez-Lacomba, M. Cortijo, and P. L. Mateo. 1988. Differential scanning calorimetry of the thermal denaturation of Thermolysin. Biochemistry. 27:1648-1652.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 39
    • 0023657725 scopus 로고
    • Stability studies on derivatives of the bovine pancreatic trypsin inhibitor
    • Schwarz, H., H.-J. Hinz, A. Mehlich, H. Tschesche, and H. R. Wenzel. 1987. Stability studies on derivatives of the bovine pancreatic trypsin inhibitor. Biochemistry. 26:3544-3551.
    • (1987) Biochemistry , vol.26 , pp. 3544-3551
    • Schwarz, H.1    Hinz, H.-J.2    Mehlich, A.3    Tschesche, H.4    Wenzel, H.R.5
  • 40
    • 0008098143 scopus 로고
    • Electronic structures of active site in copper proteins: Contributions to reactivity
    • Solomon, E. I., M. J. Baldwin, and M. D. Lowery. 1992. Electronic structures of active site in copper proteins: contributions to reactivity. Chem. Rev. 92:521-542.
    • (1992) Chem. Rev. , vol.92 , pp. 521-542
    • Solomon, E.I.1    Baldwin, M.J.2    Lowery, M.D.3
  • 41
    • 0028964815 scopus 로고
    • Structural and spectroscopic studies of the copper site of stellacyanin
    • Strange, R. W., B. Reinhammar, L. M. Murphy, and S. S. Hasnain. 1995. Structural and spectroscopic studies of the copper site of stellacyanin. Biochemistry. 34:220-231.
    • (1995) Biochemistry , vol.34 , pp. 220-231
    • Strange, R.W.1    Reinhammar, B.2    Murphy, L.M.3    Hasnain, S.S.4
  • 42
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant, J. M. 1987. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38:463-512.
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-512
    • Sturtevant, J.M.1
  • 43
    • 0013440731 scopus 로고
    • UV resonance Raman examination of the azurin tryptophan environment and energy relaxation patways
    • Sweeney, J. A., P. A. Harmon, S. A. Asher, C. M. Hutnik, and A. G. Szabo. 1991. UV Resonance Raman examination of the azurin tryptophan environment and energy relaxation patways. J. Am. Chem. Soc. 113: 7531-7537.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7531-7537
    • Sweeney, J.A.1    Harmon, P.A.2    Asher, S.A.3    Hutnik, C.M.4    Szabo, A.G.5
  • 44
    • 0028567225 scopus 로고
    • Effect of an intersubunit disulfide bond on the stability of streptomyces subtilisin inhibitor
    • Tamura, A., S. Kojima, K. Miura, and J. M. Sturtevant. 1994. Effect of an intersubunit disulfide bond on the stability of streptomyces subtilisin inhibitor. Biochemistry. 33:4512-4520.
    • (1994) Biochemistry , vol.33 , pp. 4512-4520
    • Tamura, A.1    Kojima, S.2    Miura, K.3    Sturtevant, J.M.4
  • 45
    • 0023896186 scopus 로고
    • Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae
    • Taniyama, Y., Y. Yamamoto, M. Kikuchi, and M. Ikehara. 1988. Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 152:962-967.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 962-967
    • Taniyama, Y.1    Yamamoto, Y.2    Kikuchi, M.3    Ikehara, M.4
  • 46
    • 0028871971 scopus 로고
    • Effect of irreversibility on the thermal denaturation of Aspergillus satoi acid proteinase
    • Tello-Solis, S. R., and A. Hernandez-Arana. 1995. Effect of irreversibility on the thermal denaturation of Aspergillus satoi acid proteinase. Biochem. J. 311:969-974.
    • (1995) Biochem. J. , vol.311 , pp. 969-974
    • Tello-Solis, S.R.1    Hernandez-Arana, A.2
  • 48
    • 0029562948 scopus 로고
    • Mechanism of protein stabilization by disulfide bridges: Calorimetric unfolding studies on disulfide-deficient mutants of the α-amylase inhibitor Tendamistat
    • Vogl, T., R. Brengelmann, H.-J. Hinz, M. Scharf, M. Lotzbeyer, and J. W. Engels. 1995. Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the α-amylase inhibitor Tendamistat. J. Mol. Biol. 254:481-496.
    • (1995) J. Mol. Biol. , vol.254 , pp. 481-496
    • Vogl, T.1    Brengelmann, R.2    Hinz, H.-J.3    Scharf, M.4    Lotzbeyer, M.5    Engels, J.W.6
  • 50
    • 0001227472 scopus 로고
    • Harnessing disulfide bonds using protein engineering
    • Wetzel, R. 1987. Harnessing disulfide bonds using protein engineering. Trends Biochem. Sci. 12:478-482.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 478-482
    • Wetzel, R.1
  • 51
    • 0020473261 scopus 로고
    • Studies on the relationship of disulfide bonds to the formation of the secondary structure in chicken egg white lysozyme
    • White, F. H., Jr. 1982. Studies on the relationship of disulfide bonds to the formation of the secondary structure in chicken egg white lysozyme. Biochemistry. 21:967-977.
    • (1982) Biochemistry , vol.21 , pp. 967-977
    • White F.H., Jr.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.