메뉴 건너뛰기




Volumn 512, Issue 1-2, 2011, Pages 71-75

Studies of irreversible heat denaturation of green fluorescent protein by differential scanning microcalorimetry

Author keywords

Green fluorescent protein; Irreversible denaturation; Transition state

Indexed keywords

DENATURED STATE; ENERGY PARAMETERS; GREEN FLUORESCENT PROTEIN; HEAT CAPACITIES; HEAT DENATURATION; HYDROPHOBIC GROUPS; IRREVERSIBLE DENATURATION; IRREVERSIBLE HEAT; NATIVE STATE; SCANNING MICROCALORIMETRY; TRANSITION STATE; TWO STAGE;

EID: 78650263110     PISSN: 00406031     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tca.2010.09.002     Document Type: Article
Times cited : (15)

References (27)
  • 1
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • P.L. Privalov, and S.A. Potekhin Scanning microcalorimetry in studying temperature-induced changes in proteins Methods Enzymol. 131 1986 4 51
    • (1986) Methods Enzymol. , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 2
    • 0031467295 scopus 로고    scopus 로고
    • Analysis of differential scanning calorimetry data for proteins. Criteria of validity of one-step mechanism of irreversible protein denaturation
    • B.I. Kurganov, A.E. Lyubarev, J.M. Sanchez-Ruiz, and V.L. Shnyrov Analysis of differential scanning calorimetry data for proteins. Criteria of validity of one-step mechanism of irreversible protein denaturation Biophys. Chem. 69 1997 125 135
    • (1997) Biophys. Chem. , vol.69 , pp. 125-135
    • Kurganov, B.I.1    Lyubarev, A.E.2    Sanchez-Ruiz, J.M.3    Shnyrov, V.L.4
  • 3
    • 0032498925 scopus 로고    scopus 로고
    • Irreversible thermal denaturation of uridine phosphorylase from Escherichia coli K-12
    • A.E. Lyubarev, B.I. Kurganov, A.A. Burlakova, and V.N. Orlov Irreversible thermal denaturation of uridine phosphorylase from Escherichia coli K-12 Biophys. Chem. 70 1998 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
  • 4
    • 0033612542 scopus 로고    scopus 로고
    • Two-state irreversible thermal denaturation of muscle creatine kinase
    • A.E. Lyubarev, B.I. Kurganov, V.N. Orlov, and H.M. Zhou Two-state irreversible thermal denaturation of muscle creatine kinase Biophys. Chem. 79 1999 199 204
    • (1999) Biophys. Chem. , vol.79 , pp. 199-204
    • Lyubarev, A.E.1    Kurganov, B.I.2    Orlov, V.N.3    Zhou, H.M.4
  • 5
    • 0032018830 scopus 로고    scopus 로고
    • Influence of kinetic factors on heat denaturation and renaturation of biopolymers
    • S.A. Potekhin, and E.L. Kovrigin Influence of kinetic factors on heat denaturation and renaturation of biopolymers Biofizika 43 1998 223 232
    • (1998) Biofizika , vol.43 , pp. 223-232
    • Potekhin, S.A.1    Kovrigin, E.L.2
  • 6
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • J.M. Sanchez-Ruiz, J.L. Lopez-Lacomba, M. Cortijo, and P.L. Mateo Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin Biochemistry 27 1988 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
  • 7
    • 0034562065 scopus 로고    scopus 로고
    • Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein
    • R. Battistutta, A. Negro, and G. Zanotti Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein Proteins 41 2000 429 437
    • (2000) Proteins , vol.41 , pp. 429-437
    • Battistutta, R.1    Negro, A.2    Zanotti, G.3
  • 10
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • R.Y. Tsien The green fluorescent protein Annu. Rev. Biochem. 67 1998 509 544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 11
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • H. Fukuda, M. Arai, and K. Kuwajima Folding of green fluorescent protein and the cycle3 mutant Biochemistry 39 2000 12025 12032
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 12
    • 70450265297 scopus 로고    scopus 로고
    • Can the fluorescence of green fluorescent protein chromophore be related directly to the nativity of protein structure?
    • B.S. Melnik, T.V. Povarnitsyna, and T.N. Melnik Can the fluorescence of green fluorescent protein chromophore be related directly to the nativity of protein structure? Biochem. Biophys. Res. Commun. 390 2009 1167 1170
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1167-1170
    • Melnik, B.S.1    Povarnitsyna, T.V.2    Melnik, T.N.3
  • 13
    • 34548816178 scopus 로고    scopus 로고
    • The rough energy landscape of superfolder GFP is linked to the chromophore
    • B.T. Andrews, A.R. Schoenfish, M. Roy, G. Waldo, and P.A. Jennings The rough energy landscape of superfolder GFP is linked to the chromophore J. Mol. Biol. 373 2007 476 490
    • (2007) J. Mol. Biol. , vol.373 , pp. 476-490
    • Andrews, B.T.1    Schoenfish, A.R.2    Roy, M.3    Waldo, G.4    Jennings, P.A.5
  • 14
    • 8344290520 scopus 로고    scopus 로고
    • Acid denaturation and refolding of green fluorescent protein
    • S. Enoki, K. Saeki, K. Maki, and K. Kuwajima Acid denaturation and refolding of green fluorescent protein Biochemistry 43 2004 14238 14248
    • (2004) Biochemistry , vol.43 , pp. 14238-14248
    • Enoki, S.1    Saeki, K.2    Maki, K.3    Kuwajima, K.4
  • 16
    • 0020482348 scopus 로고
    • Reversible denaturation of Aequorea green-fluorescent protein: Physical separation and characterization of the renatured protein
    • W.W. Ward, and S.H. Bokman Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein Biochemistry 21 1982 4535 4540
    • (1982) Biochemistry , vol.21 , pp. 4535-4540
    • Ward, W.W.1    Bokman, S.H.2
  • 18
    • 0027938174 scopus 로고
    • Extended theoretical analysis of irreversible protein thermal unfolding
    • D. Milardi, R.C. La, and D. Grasso Extended theoretical analysis of irreversible protein thermal unfolding Biophys. Chem. 52 1994 183 189
    • (1994) Biophys. Chem. , vol.52 , pp. 183-189
    • Milardi, D.1    La, R.C.2    Grasso, D.3
  • 19
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • J.R. Lepock, K.P. Ritchie, M.C. Kolios, A.M. Rodahl, K.A. Heinz, and J. Kruuv 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, A.M.4    Heinz, K.A.5    Kruuv, J.6
  • 20
    • 0032572516 scopus 로고    scopus 로고
    • Folding under inequilibrium conditions as a possible reason for partial irreversibility of heat-denatured proteins: Computer simulation study
    • S.A. Potekhin, and E.L. Kovrigin Folding under inequilibrium conditions as a possible reason for partial irreversibility of heat-denatured proteins: computer simulation study Biophys. Chem. 73 1998 241 248
    • (1998) Biophys. Chem. , vol.73 , pp. 241-248
    • Potekhin, S.A.1    Kovrigin, E.L.2
  • 21
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • P.L. Privalov 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
  • 22
    • 0025867101 scopus 로고
    • Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase
    • B. Chen, and J. King Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase Biochemistry 30 1991 6260 6269
    • (1991) Biochemistry , vol.30 , pp. 6260-6269
    • Chen, B.1    King, J.2
  • 23
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • B.L. Chen, W.A. Baase, and J.A. Schellman Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations Biochemistry 28 1989 691 699
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.L.1    Baase, W.A.2    Schellman, J.A.3
  • 24
    • 0021525532 scopus 로고
    • Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state
    • S. Segawa, and M. Sugihara Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state Biopolymers 23 1984 2473 2488
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.1    Sugihara, M.2
  • 25
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • P.L. Privalov, and N.N. Khechinashvili 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
  • 26
    • 9744263152 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of the unfolding and refolding of the three-stranded alpha-helical coiled coil, Lpp-56
    • A.I. Dragan, S.A. Potekhin, A. Sivolob, M. Lu, and P.L. Privalov Kinetics and thermodynamics of the unfolding and refolding of the three-stranded alpha-helical coiled coil, Lpp-56 Biochemistry 43 2004 14891 14900
    • (2004) Biochemistry , vol.43 , pp. 14891-14900
    • Dragan, A.I.1    Potekhin, S.A.2    Sivolob, A.3    Lu, M.4    Privalov, P.L.5
  • 27
    • 0032040048 scopus 로고    scopus 로고
    • Modeling of irreversible thermal protein denaturation at varying temperature. I. The model involving two consecutive irreversible steps
    • A.E. Lyubarev, and B.I. Kurganov Modeling of irreversible thermal protein denaturation at varying temperature. I. The model involving two consecutive irreversible steps Biochemistry (Mosc.) 63 1998 434 440
    • (1998) Biochemistry (Mosc.) , vol.63 , pp. 434-440
    • Lyubarev, A.E.1    Kurganov, B.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.