메뉴 건너뛰기




Volumn 264, Issue 4, 1996, Pages 784-805

Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d

Author keywords

Chemical denaturation; Differential scanning calorimetry; Hyperthermophile; Protein folding; Stability

Indexed keywords

GUANIDINE; LYSINE; RECOMBINANT PROTEIN; UREA;

EID: 0030582620     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0677     Document Type: Article
Times cited : (137)

References (121)
  • 1
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100°C
    • Adams, M. W. W. (1993). Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47, 627-658.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 627-658
    • Adams, M.W.W.1
  • 2
    • 0028947236 scopus 로고
    • Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride
    • Agashe, V. R. & Udgaonkar, J. B. (1995). Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry, 34, 3286-3299.
    • (1995) Biochemistry , vol.34 , pp. 3286-3299
    • Agashe, V.R.1    Udgaonkar, J.B.2
  • 3
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2. Why small proteins tend to have high denaturation temperatures
    • Alexander, P., Fahnestock, S., Lee, T., Orban, J. & Bryan, P. (1992). Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2. Why small proteins tend to have high denaturation temperatures. Biochemistry, 31, 3597-3603.
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 4
    • 0025822867 scopus 로고
    • Solvent denaturation and stabilization of globular proteins
    • Alonso, D. O. V. & Dill, K. (1991). Solvent denaturation and stabilization of globular proteins. Biochemistry, 30, 5974-5985.
    • (1991) Biochemistry , vol.30 , pp. 5974-5985
    • Alonso, D.O.V.1    Dill, K.2
  • 5
    • 0026969319 scopus 로고
    • +-dependent alcohol dehydrogenase from Sulfolobus solfataricus: Gene and protein sequence determination and relationship to other alcohol dehydrogenases
    • +-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases. Biochemistry, 31, 12514-12523.
    • (1992) Biochemistry , vol.31 , pp. 12514-12523
    • Ammendola, S.1    Raia, C.2    Caruso, C.3    Camardella, L.4    D'Auria, S.5    DeRosa, M.6    Rossi, M.7
  • 7
    • 0028978967 scopus 로고
    • Thermodynamics of the thermal unfolding of eglin c in the presence and absence of guanidinium chloride
    • Bae, S.-J. & Sturtevant, J. M. (1995). Thermodynamics of the thermal unfolding of eglin c in the presence and absence of guanidinium chloride. Biophys. Chem. 55, 247-252.
    • (1995) Biophys. Chem. , vol.55 , pp. 247-252
    • Bae, S.-J.1    Sturtevant, J.M.2
  • 8
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin, R. (1986). Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl Acad. Sci. USA, 83, 8069-8072.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.1
  • 10
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Baumann, H., Knapp, S., Lundback, T., Ladenstein, R. & Härd, T. (1994). Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Struct. Biol. 1, 808-819.
    • (1994) Struct. Biol. , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundback, T.3    Ladenstein, R.4    Härd, T.5
  • 11
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. & Schellman, J. (1987). Protein stability curves. Biopolymers, 26, 1862-1877.
    • (1987) Biopolymers , vol.26 , pp. 1862-1877
    • Becktel, W.1    Schellman, J.2
  • 13
    • 0026347331 scopus 로고
    • Determinants of protein hyperthermostability. 1. Purification, amino acid sequence, and secondary structure from NMR of the rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Blake, P., Park, J., Bryant, F., Aono, A., Magnuson, J. K., Eccleston, E., Howard, J., Summers, M. & Adams, M. W. W. (1991). Determinants of protein hyperthermostability. 1. Purification, amino acid sequence, and secondary structure from NMR of the rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus. Biochemistry, 30, 10885-10891.
    • (1991) Biochemistry , vol.30 , pp. 10885-10891
    • Blake, P.1    Park, J.2    Bryant, F.3    Aono, A.4    Magnuson, J.K.5    Eccleston, E.6    Howard, J.7    Summers, M.8    Adams, M.W.W.9
  • 14
    • 0027053859 scopus 로고
    • Solutions state structure by NMR of zinc-substituted rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus
    • Blake, P., Park, J.-B., Zhou, Z., Hare, D., Adams, M. W. W. & Summers, M. (1992a). Solutions state structure by NMR of zinc-substituted rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. Protein Sci. 1, 1508-1521.
    • (1992) Protein Sci. , vol.1 , pp. 1508-1521
    • Blake, P.1    Park, J.-B.2    Zhou, Z.3    Hare, D.4    Adams, M.W.W.5    Summers, M.6
  • 15
    • 0027082207 scopus 로고
    • Comparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with the NMR structure of the zinc-substituted protein
    • Blake, P., Day, M., Hsu, B., Joshua-Tor, L., Park, J.-B., Hare, D., Adams, M., Rees, D. & Summers, M. (1992b). Comparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with the NMR structure of the zinc-substituted protein. Protein Sci. 1, 1522-1525.
    • (1992) Protein Sci. , vol.1 , pp. 1522-1525
    • Blake, P.1    Day, M.2    Hsu, B.3    Joshua-Tor, L.4    Park, J.-B.5    Hare, D.6    Adams, M.7    Rees, D.8    Summers, M.9
  • 16
    • 0028014604 scopus 로고
    • Relevance of sequence statistics for the properties of extremophilic proteins
    • Böhm, G. & Jaenicke, R. (1994). Relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Pept. Protein Res. 43, 97-106.
    • (1994) Int. J. Pept. Protein Res. , vol.43 , pp. 97-106
    • Böhm, G.1    Jaenicke, R.2
  • 19
    • 0027992738 scopus 로고
    • Purification and characterization of extremely thermophilic and thermostable 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus
    • Cacciapuoti, G., Porcelli, M., Bertoldo, C., De Rosa, M. & Zappia, V. (1994). Purification and characterization of extremely thermophilic and thermostable 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. J. Biol. Chem. 269, 24762-24769.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24762-24769
    • Cacciapuoti, G.1    Porcelli, M.2    Bertoldo, C.3    De Rosa, M.4    Zappia, V.5
  • 20
    • 0029090926 scopus 로고
    • Response of rubredoxin from Pyrococcus furiosus to environmental changes: Implications for the origin of hyperthermostability
    • Cavagnero, S., Zhou, Z. H., Adams, M. W. W. & Chan, S. I. (1995). Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostability. Biochemistry, 34, 9865-9873.
    • (1995) Biochemistry , vol.34 , pp. 9865-9873
    • Cavagnero, S.1    Zhou, Z.H.2    Adams, M.W.W.3    Chan, S.I.4
  • 21
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungsopterin enzyme, aldehyde ferredoxin oxido-reductase
    • Chan, M. K., Mukund, S., Kletzin, A., Adams, M. W. W. & Rees, D. (1995). Structure of a hyperthermophilic tungsopterin enzyme, aldehyde ferredoxin oxido-reductase. Science, 267 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.W.4    Rees, D.5
  • 22
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke, J. & Fersht, A. R. (1993). Engineered 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
  • 23
    • 0003082897 scopus 로고
    • The structure of DNA-binding proteins from eu-and archaebacteria
    • Gualerzi, C. O. & Pon, C. O., eds, Springer-Verlag, Berlin
    • Dijk, J. & Reinhardt, R. (1986). The structure of DNA-binding proteins from eu-and archaebacteria. In Bacterial Chromatin (Gualerzi, C. O. & Pon, C. O., eds), pp. 185-218, Springer-Verlag, Berlin.
    • (1986) Bacterial Chromatin , pp. 185-218
    • Dijk, J.1    Reinhardt, R.2
  • 24
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K. (1985). Theory for the folding and stability of globular proteins. Biochemistry, 24, 1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.1
  • 25
    • 0028958071 scopus 로고
    • Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium
    • Dym, O., Mevarech, M. & Sussman, J. L. (1995). Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science, 267, 1344-1346.
    • (1995) Science , vol.267 , pp. 1344-1346
    • Dym, O.1    Mevarech, M.2    Sussman, J.L.3
  • 26
    • 0016909627 scopus 로고
    • The thermodynamic basis of the stability of proteins, nucleic acids, and membranes
    • Edelhoch, H. & Osborne, J. C., Jr (1976). The thermodynamic basis of the stability of proteins, nucleic acids, and membranes. Advan. Protein Chem. 30, 183-250.
    • (1976) Advan. Protein Chem. , vol.30 , pp. 183-250
    • Edelhoch, H.1    Osborne J.C., Jr.2
  • 27
    • 0028839434 scopus 로고
    • Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius
    • Edmondson, S. P., Qiu, L. & Shriver, J. W. (1995). Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry, 34, 13289-13304.
    • (1995) Biochemistry , vol.34 , pp. 13289-13304
    • Edmondson, S.P.1    Qiu, L.2    Shriver, J.W.3
  • 28
    • 0021093448 scopus 로고
    • Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • Eftink, M. R., Anusiem, A. C. & Biltonen, R. L. (1983). Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A. Biochemistry, 22, 3884-3896.
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 29
    • 0028933771 scopus 로고
    • Life in unusual environments: Progress in understanding the structure and function of enzymes from extreme halophilic bacteria
    • Eisenberg, H. (1995). Life in unusual environments: progress in understanding the structure and function of enzymes from extreme halophilic bacteria. Arch. Biochem. Biophys. 318, 1-5.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 1-5
    • Eisenberg, H.1
  • 30
    • 0028071996 scopus 로고
    • Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates
    • Ferrari, M. & Lohman, T. M. (1994). Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates. Biochemistry, 33, 12896-12910.
    • (1994) Biochemistry , vol.33 , pp. 12896-12910
    • Ferrari, M.1    Lohman, T.M.2
  • 32
    • 0028929048 scopus 로고
    • Convergent evolution of amino acid usage in archaebacterial and eubacterial lineages adapted to high salt
    • Gandbhir, M., Rasched, I., Marliere, P. & Mutzel, R. (1995). Convergent evolution of amino acid usage in archaebacterial and eubacterial lineages adapted to high salt. Res. Microbiol. 146, 113-120.
    • (1995) Res. Microbiol. , vol.146 , pp. 113-120
    • Gandbhir, M.1    Rasched, I.2    Marliere, P.3    Mutzel, R.4
  • 33
    • 0029176320 scopus 로고
    • How to make my blood boil
    • Goldman, A. (1995). How to make my blood boil. Structure, 3, 1277-1279.
    • (1995) Structure , vol.3 , pp. 1277-1279
    • Goldman, A.1
  • 34
    • 0029006334 scopus 로고
    • Structure and stability of histone HMf from the hyperthermophic archaeon Methanothermus fervidus
    • Grayling, R. A., Becktel, W. J. & Reeve, J. N. (1995). Structure and stability of histone HMf from the hyperthermophic archaeon Methanothermus fervidus. Biochemistry, 34, 8441-8448.
    • (1995) Biochemistry , vol.34 , pp. 8441-8448
    • Grayling, R.A.1    Becktel, W.J.2    Reeve, J.N.3
  • 36
    • 0028143596 scopus 로고
    • Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
    • Hamada, D., Kidokoro, S.-I., Fukada, H., Takahashi, K. & Goto, Y. (1994). Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl Acad. Sci. USA, 91, 10325-10329.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10325-10329
    • Hamada, D.1    Kidokoro, S.-I.2    Fukada, H.3    Takahashi, K.4    Goto, Y.5
  • 37
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z. & Tidor, B. (1994). Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3, 211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.1    Tidor, B.2
  • 38
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Henning, M., Darimont, B., Sterner, R., Kirschner, K. & Jansonius, J. N. (1995). 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure, 3, 1295-1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Henning, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 39
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel, R. & König, H. (1988). Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Letters, 49, 75-79.
    • (1988) FEMS Microbiol. Letters , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 40
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz, A., Serrano, L., Avron, B., Bycroft, M. & Fersht, A. (1990). Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216, 1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.5
  • 41
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor
    • Jackson, S. E., Moracci, M., elMasry, N., Johnson, C. M. & Fersht, A. R. (1993). Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor. Biochemistry, 32, 11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    ElMasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 42
    • 0025351922 scopus 로고
    • Proteins under extreme physical conditions
    • Jaenicke, R. & Zavodszky, P. (1990). Proteins under extreme physical conditions. FEBS Letters, 268 344-349.
    • (1990) FEBS Letters , vol.268 , pp. 344-349
    • Jaenicke, R.1    Zavodszky, P.2
  • 43
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • Johnson, C. M. & Fersht, A. R. (1995). Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea. Biochemistry, 34, 6795-6804.
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 44
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9 Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • Kelly, C., Nishiyama, M., Ohnishi, Y., Beppu, T. & Birktoft, J. (1993). Determinants of protein thermostability observed in the 1.9 Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry, 32, 3913-3922.
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.5
  • 45
    • 0028686645 scopus 로고
    • Extremely thermophilic microorganisms: Metabolic strategies, genetic characteristics, and biotechnological potential
    • Kelly, R. M., Peeples, T. L., Halio, S. B., Rinker, K. D. & Duffaud, G. D. (1994). Extremely thermophilic microorganisms: metabolic strategies, genetic characteristics, and biotechnological potential. Ann. N.Y. Acad. Sci. 745, 409-425.
    • (1994) Ann. N.Y. Acad. Sci. , vol.745 , pp. 409-425
    • Kelly, R.M.1    Peeples, T.L.2    Halio, S.B.3    Rinker, K.D.4    Duffaud, G.D.5
  • 46
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan-containing mutant of ubiquitin
    • Khorasanizadeh, S., Peters, I. D., Butt, T. & Roder, H. (1993). Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry, 32, 7054-7063.
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.3    Roder, H.4
  • 47
    • 0026566944 scopus 로고
    • Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus
    • Klump, H., Ruggiero, J., Kessel, M., Park, J.-B., Adams, M. W. W. & Robb, F. (1992). Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. J. Biol. Chem. 267, 22681-22685.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22681-22685
    • Klump, H.1    Ruggiero, J.2    Kessel, M.3    Park, J.-B.4    Adams, M.W.W.5    Robb, F.6
  • 48
    • 0000225523 scopus 로고
    • Life in the pressure cooker: The thermal unfolding of proteins from hyperthermophiles
    • Klump, H. H., Adams, M. W. W. & Robb, F. T. (1994). Life in the pressure cooker: the thermal unfolding of proteins from hyperthermophiles. Pure Appl. Chem. 66, 485-489.
    • (1994) Pure Appl. Chem. , vol.66 , pp. 485-489
    • Klump, H.H.1    Adams, M.W.W.2    Robb, F.T.3
  • 49
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer, L, Steipe, B., Huber, R., Tomschy, A. & Jaenicke, R. (1995). The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246, 511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, L.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 50
    • 0029056926 scopus 로고
    • Crystal structure of the large fragment of Thermus aquaticus DNA polymerase 1 at 2.5 Å resolution: Structural basis for thermostability
    • Korolev, S., Nayal, M., Barnes, W., Di Cera, E. & Waksman, G. (1995). Crystal structure of the large fragment of Thermus aquaticus DNA polymerase 1 at 2.5 Å resolution: structural basis for thermostability. Proc. Natl. Acad. Sci. USA, 92, 9264-9268.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9264-9268
    • Korolev, S.1    Nayal, M.2    Barnes, W.3    Di Cera, E.4    Waksman, G.5
  • 51
    • 0027496724 scopus 로고
    • The purification and characterization of an extremely thermostable α-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Laderman, K., Davis, B., Krutzsch, H., Lewis, M., Griko, Y., Privalov, P. & Anfinsen, C. (1993). The purification and characterization of an extremely thermostable α-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. J. Biol. Chem. 268, 24394-24401.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24394-24401
    • Laderman, K.1    Davis, B.2    Krutzsch, H.3    Lewis, M.4    Griko, Y.5    Privalov, P.6    Anfinsen, C.7
  • 52
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 54
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu, Y. & Bolen, D. W. (1995). The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry, 34, 12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 55
    • 0029917969 scopus 로고    scopus 로고
    • The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding
    • Liu, Y. & Sturtevant, J. M. (1996). The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding. Biochemistry, 35, 3059-3062.
    • (1996) Biochemistry , vol.35 , pp. 3059-3062
    • Liu, Y.1    Sturtevant, J.M.2
  • 56
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area
    • Livingstone, J., Spolar, R. & Record, T. (1991). Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry, 30, 4237-4244.
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.1    Spolar, R.2    Record, T.3
  • 57
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidine hydrochloride: A calorimetric study
    • Makhatadze, G. I. & Privalov, P. (1992). Protein interactions with urea and guanidine hydrochloride: a calorimetric study. J. Mol. Biol. 226, 491-505.
    • (1992) J. Mol. Biol. , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.2
  • 58
    • 0028297113 scopus 로고
    • A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP
    • Martinez, J. C., El Harrous, M., Filimonov, V., Mateo, P. L. & Fersht, A. (1994). A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. Biochemistry, 33, 3919-3926.
    • (1994) Biochemistry , vol.33 , pp. 3919-3926
    • Martinez, J.C.1    El Harrous, M.2    Filimonov, V.3    Mateo, P.L.4    Fersht, A.5
  • 59
    • 0027328752 scopus 로고
    • Structural and genetic analysis of protein folding and stability
    • Matthews, B. (1993). Structural and genetic analysis of protein folding and stability. Curr. Opin. Struct. Biol. 3, 589-593.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 589-593
    • Matthews, B.1
  • 60
    • 0029156641 scopus 로고
    • Gene cloning, sequencing, expression, and biophysical characterization of the Sac7 DNA-binding proteins from the hyperthermophile Sulfolobus acidocaldarius
    • McAfee, J. G., Edmondson, S. P., Datta, P. K., Shriver, J. W. & Gupta, R. (1995). Gene cloning, sequencing, expression, and biophysical characterization of the Sac7 DNA-binding proteins from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry, 34, 10063-10077.
    • (1995) Biochemistry , vol.34 , pp. 10063-10077
    • McAfee, J.G.1    Edmondson, S.P.2    Datta, P.K.3    Shriver, J.W.4    Gupta, R.5
  • 61
    • 0029883976 scopus 로고    scopus 로고
    • Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: Fluorescence and circular dichroism studies
    • McAfee, J. G., Edmondson, S., Zegar, I. & Shriver, J. W. (1996). Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: fluorescence and circular dichroism studies. Biochemistry, 35, 4034-4045.
    • (1996) Biochemistry , vol.35 , pp. 4034-4045
    • McAfee, J.G.1    Edmondson, S.2    Zegar, I.3    Shriver, J.W.4
  • 62
    • 0024974452 scopus 로고
    • Engineering protein thermal stability. Sequence statistics point to residue substitutions in α-helices
    • Menendez-Arias, L. & Argos, P. (1989). Engineering protein thermal stability. Sequence statistics point to residue substitutions in α-helices. J. Mol. Biol. 206, 397-406.
    • (1989) J. Mol. Biol. , vol.206 , pp. 397-406
    • Menendez-Arias, L.1    Argos, P.2
  • 63
    • 0021908789 scopus 로고
    • Amino acid sequence of a ferredoxin from thermoacidophilic Archaebacterium, Sulfolobus acidocaldarius. Presence of N6-monomethyllysine and phyletic consideration of Archaebacteria
    • Minami, Y., Wakabayashi, S., Wada, K., Matsubara, H., Kerscher, L. & Oesterhelt, D. (1985). Amino acid sequence of a ferredoxin from thermoacidophilic Archaebacterium, Sulfolobus acidocaldarius. Presence of N6-monomethyllysine and phyletic consideration of Archaebacteria. J. Biochem. 97, 745-753.
    • (1985) J. Biochem. , vol.97 , pp. 745-753
    • Minami, Y.1    Wakabayashi, S.2    Wada, K.3    Matsubara, H.4    Kerscher, L.5    Oesterhelt, D.6
  • 64
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera, O., Kay, C. & Hodges, R. (1994). Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3, 1984-1991.
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.1    Kay, C.2    Hodges, R.3
  • 65
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy, K. P. & Freire, E. (1992). Thermodynamics of structural stability and cooperative folding behavior in proteins. Advan. Protein Chem. 43, 313-361.
    • (1992) Advan. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 66
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy, K. P., Privalov, P. & Gill, S. J. (1990). Common features of protein unfolding and dissolution of hydrophobic compounds. Science, 247, 559-561.
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.2    Gill, S.J.3
  • 67
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J., Pace, C. N. & Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.1    Pace, C.N.2    Scholtz, J.M.3
  • 68
    • 0017706821 scopus 로고
    • Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change
    • Nojima, H., Ikai, A., Oshima, T. & Noda, H. (1977). Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change. J. Mol. Biol. 116, 429-442.
    • (1977) J. Mol. Biol. , vol.116 , pp. 429-442
    • Nojima, H.1    Ikai, A.2    Oshima, T.3    Noda, H.4
  • 69
    • 0011304639 scopus 로고
    • Thermodynamic studies on reversible denaturation of thermostable proteins from an extreme thermophile
    • Friedman, S. M., ed., Academic Press, New York
    • Nojima, H., Ikai, A., Noda, H., Hon-nami, K. & Oshima, T. (1978). Thermodynamic studies on reversible denaturation of thermostable proteins from an extreme thermophile. In Biochemistry of Thermophily (Friedman, S. M., ed.), pp. 305-323, Academic Press, New York.
    • (1978) Biochemistry of Thermophily , pp. 305-323
    • Nojima, H.1    Ikai, A.2    Noda, H.3    Hon-Nami, K.4    Oshima, T.5
  • 70
    • 0028821194 scopus 로고
    • Thermodynamic genetics of the folding of the B1 immunoglobin-binding domain from Streptococcal protein G
    • O'Neil, K. T., Hoess, R. H., Raleigh, D. P. & DeGrado, W. F. (1995). Thermodynamic genetics of the folding of the B1 immunoglobin-binding domain from Streptococcal protein G. Proteins: Struct. Funct. Genet. 21, 11-21.
    • (1995) Proteins: Struct. Funct. Genet. , vol.21 , pp. 11-21
    • O'Neil, K.T.1    Hoess, R.H.2    Raleigh, D.P.3    DeGrado, W.F.4
  • 71
    • 0028983182 scopus 로고
    • a values of the denatured state are on average 0.4 units lower than those of model compounds
    • a values of the denatured state are on average 0.4 units lower than those of model compounds. Biochemistry, 34, 9424-9433.
    • (1995) Biochemistry , vol.34 , pp. 9424-9433
    • Oliveberg, M.1    Arcus, V.2    Fersht, A.R.3
  • 72
    • 0002686828 scopus 로고
    • Polyamines in thermophiles
    • Bachrach, U. & Heimer, Y., eds, Chemical Rubber Company, Boca Raton, FA
    • Oshima, T. (1989). Polyamines in thermophiles. In The Physiology of Polyamines (Bachrach, U. & Heimer, Y., eds), pp. 35-46, Chemical Rubber Company, Boca Raton, FA.
    • (1989) The Physiology of Polyamines , pp. 35-46
    • Oshima, T.1
  • 73
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • Pace, C. N. (1975). The stability of globular proteins. CRC Crit. Rev. Biochem. 3, 1-43.
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 1-43
    • Pace, C.N.1
  • 74
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 75
    • 0024276805 scopus 로고
    • 1 is stabilized by cation and anion binding
    • 1 is stabilized by cation and anion binding. Biochemistry, 27, 3242-3246.
    • (1988) Biochemistry , vol.27 , pp. 3242-3246
    • Pace, C.N.1    Grimsley, G.R.2
  • 76
    • 0024498471 scopus 로고
    • A new method for determining the heat capacity change for protein folding
    • Pace, C. N. & Laurents, D. (1989). A new method for determining the heat capacity change for protein folding. Biochemistry, 28, 2520-2525.
    • (1989) Biochemistry , vol.28 , pp. 2520-2525
    • Pace, C.N.1    Laurents, D.2
  • 77
    • 0018798895 scopus 로고
    • Determining globular protein stability: Guanidine hydrochloride denaturation of myoglobin
    • Pace, C. N. & Vanderburg, K. E. (1979). Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin. Biochemistry, 18, 288-292.
    • (1979) Biochemistry , vol.18 , pp. 288-292
    • Pace, C.N.1    Vanderburg, K.E.2
  • 78
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton, T. E., ed., IRL Press, New York
    • Pace, C. N., Shirley, B. & Thomson, J. A. (1989). Measuring the conformational stability of a protein. In Protein Structure: A Practical Approach (Creighton, T. E., ed.), pp. 311-330, IRL Press, New York.
    • (1989) Protein Structure: A Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.2    Thomson, J.A.3
  • 80
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • Perutz, M. F. (1978). Electrostatic effects in proteins. Science, 201, 1187-1191.
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 81
    • 0017295455 scopus 로고
    • Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride
    • Pfiel, W. & Privalov, P. (1976). Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride. Biophys. Chem. 4, 33-40.
    • (1976) Biophys. Chem. , vol.4 , pp. 33-40
    • Pfiel, W.1    Privalov, P.2
  • 83
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • Privalov, P. (1979). Stability of proteins. Small globular proteins. Advan. Protein. Chem. 33, 167-241.
    • (1979) Advan. Protein. Chem. , vol.33 , pp. 167-241
    • Privalov, P.1
  • 84
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P. & Gill, S. (1988). Stability of protein structure and hydrophobic interaction. Advan. Protein Chem. 39, 191-234.
    • (1988) Advan. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.1    Gill, S.2
  • 85
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov, P. & Khechinashvili, N. (1974). A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86, 665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.1    Khechinashvili, N.2
  • 86
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov, P. & Potekin, S. (1986). Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131, 4-51.
    • (1986) Methods Enzymol. , vol.131 , pp. 4-51
    • Privalov, P.1    Potekin, S.2
  • 87
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myglobin
    • Privalov, P., Khechinashvili, N. N. & Atanosov, B. P. (1971). Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myglobin. Biopolymers, 10, 1865-1890.
    • (1971) Biopolymers , vol.10 , pp. 1865-1890
    • Privalov, P.1    Khechinashvili, N.N.2    Atanosov, B.P.3
  • 89
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees, D. C. & Adams, M. W. W. (1995). Hyperthermophiles: taking the heat and loving it. Structure, 3, 251-254.
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 90
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards, F. M. (1974). The interpretation of protein structures: total volume, group volume distributions and packing density. J. Mol. Biol. 82, 1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 91
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. & Bolen, D. (1988). Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry, 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.1    Bolen, D.2
  • 92
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro, M. & Bolen, D. W. (1992). A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry, 31, 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.1    Bolen, D.W.2
  • 93
    • 0026631716 scopus 로고
    • Increased thermal stability of proteins in the presence of naturally occurring osmolytes
    • Santoro, M., Liu, Y., Khan, S. M. A., Hou, L.-X. & Bolen, D. W. (1992). Increased thermal stability of proteins in the presence of naturally occurring osmolytes. Biochemistry, 31, 5278-5283.
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.1    Liu, Y.2    Khan, S.M.A.3    Hou, L.-X.4    Bolen, D.W.5
  • 94
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman, J. A. (1978). Solvent denaturation. Biopolymers, 17, 1305-1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 95
    • 0028966932 scopus 로고
    • Conformational stability of HPr: The histidine-containing phosphocarrier protein from Bacillus subtilis
    • Scholtz, J. M. (1995). Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilis. Protein Sci. 4, 35-43.
    • (1995) Protein Sci. , vol.4 , pp. 35-43
    • Scholtz, J.M.1
  • 96
    • 0026766429 scopus 로고
    • Di-myo-inositol-1,1′-phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz, S., Sonnenbichler, J., Schäfer, W. & Hensel, R. (1992). Di-myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Letters, 306, 239-242.
    • (1992) FEBS Letters , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schäfer, W.3    Hensel, R.4
  • 97
    • 0025879614 scopus 로고
    • Folding intermediate of hyperthermophilic d-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima are trapped at low temperature
    • Schultes, V. & Jaenicke, R. (1991). Folding intermediate of hyperthermophilic d-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima are trapped at low temperature. FEBS Letters, 290, 235-238.
    • (1991) FEBS Letters , vol.290 , pp. 235-238
    • Schultes, V.1    Jaenicke, R.2
  • 98
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
    • Serrano, L., Horovitz, A., Avron, B., Bycroft, M. & Fersht, A. (1990). Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry, 29, 9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.5
  • 100
    • 0029115963 scopus 로고
    • The optimization of protein-solvent interactions: Thermostability and the role of hydrophobic and electrostatic interactions
    • Spassov, V., Karshikoff, A. D. & Ladenstein, R. (1995). The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions. Protein Sci. 4, 1516-1527.
    • (1995) Protein Sci. , vol.4 , pp. 1516-1527
    • Spassov, V.1    Karshikoff, A.D.2    Ladenstein, R.3
  • 101
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar, R. S., Livingstone, J. R. & Record, M. T. (1992). Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry, 31, 3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record, M.T.3
  • 102
    • 0029924193 scopus 로고    scopus 로고
    • NMR structure of HMfB from the hyperthermophile Methanothermus fervidus, confirms that this archaeal protein is a histone
    • Starich, M. R., Sandman, K., Reeve, J. N. & Summers, M. F. (1996). NMR structure of HMfB from the hyperthermophile Methanothermus fervidus, confirms that this archaeal protein is a histone. J. Mol. Biol. 255, 187-203.
    • (1996) J. Mol. Biol. , vol.255 , pp. 187-203
    • Starich, M.R.1    Sandman, K.2    Reeve, J.N.3    Summers, M.F.4
  • 104
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant, J. (1987). Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38, 463-488.
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.1
  • 105
    • 0027489832 scopus 로고
    • Thermodynamics of unfolding for turkey ovomucoid third domain: Thermal and chemical denaturation
    • Swint, L. & Robertson, A. D. (1993). Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation. Protein Sci. 2, 2037-2049.
    • (1993) Protein Sci. , vol.2 , pp. 2037-2049
    • Swint, L.1    Robertson, A.D.2
  • 106
    • 0028904906 scopus 로고
    • Hydrogen bonds and the pH dependence of ovomucoid third domain stability
    • Swint-Kruse, L. & Robertson, A. D. (1995). Hydrogen bonds and the pH dependence of ovomucoid third domain stability. Biochemistry, 34, 4724-4732.
    • (1995) Biochemistry , vol.34 , pp. 4724-4732
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 107
    • 0028790684 scopus 로고
    • Structural basis for the extreme thermostability of d-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: Analysis based on homology modelling
    • Szilagyi, A. & Zavodszky, P. (1995). Structural basis for the extreme thermostability of d-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: analysis based on homology modelling. Protein Eng. 8, 779-789.
    • (1995) Protein Eng. , vol.8 , pp. 779-789
    • Szilagyi, A.1    Zavodszky, P.2
  • 108
    • 0014718113 scopus 로고
    • Protein denaturation part C: Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970). Protein denaturation part C: theoretical models for the mechanism of denaturation. Advan. Protein Chem. 24, 1-95.
    • (1970) Advan. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 109
    • 0016220258 scopus 로고
    • Heat denaturation of ribonuclease
    • Tiktopulo, E. & Privalov, P. (1974). Heat denaturation of ribonuclease. Biophys. Chem. 1, 349-357.
    • (1974) Biophys. Chem. , vol.1 , pp. 349-357
    • Tiktopulo, E.1    Privalov, P.2
  • 110
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
    • Viguera, A. R., Martinez, J. C., Filimonov, V. V., Mateo, P. L. & Serrano, L. (1994). Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry, 33, 2142-2150.
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 111
    • 0023644668 scopus 로고
    • Thermal destruction processes in proteins involving cystine residues
    • Volkin, D. & Klibanov, A. (1987). Thermal destruction processes in proteins involving cystine residues. J. Biol. Chem. 262, 2945-2950.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2945-2950
    • Volkin, D.1    Klibanov, A.2
  • 112
    • 0028787409 scopus 로고
    • Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A
    • Wang, A., Robertson, A. D. & Bolen, D. W. (1995). Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A. Biochemistry, 34, 15096-15104.
    • (1995) Biochemistry , vol.34 , pp. 15096-15104
    • Wang, A.1    Robertson, A.D.2    Bolen, D.W.3
  • 113
    • 0026484252 scopus 로고
    • Amino acid preferences of small proteins: Implications for protein stability and evolution
    • White, S. H. (1992). Amino acid preferences of small proteins: implications for protein stability and evolution. J. Mol. Biol. 227, 991-995.
    • (1992) J. Mol. Biol. , vol.227 , pp. 991-995
    • White, S.H.1
  • 115
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., Kandler, O. & Wheelis, M. L. (1990). Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl Acad. Sci. USA, 87, 4576-4579.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 116
    • 0025182490 scopus 로고
    • Extremely thermostable d-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wrba, A., Schweiger, A., Schultes, V., Jaenicke, R. & Zavodszky, P. (1990). Extremely thermostable d-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry, 29, 7584-7592.
    • (1990) Biochemistry , vol.29 , pp. 7584-7592
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Zavodszky, P.5
  • 117
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • Yang, A.-S. & Honig, B. (1993). On the pH dependence of protein stability. J. Mol. Biol. 231, 459-474.
    • (1993) J. Mol. Biol. , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 118
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • Yao, M. & Bolen, D. W. (1995). How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry, 34, 3771-3781.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 121
    • 0028271001 scopus 로고
    • Post-translational modifications in aspartate aminotransferase from Sulfolobus solfataricus. Detection of N-c-methyllysines by mass spectrometry
    • Zappacosta, F., Sannia, G., Savoy, L.-A., Marino, G. & Pucci, P. (1994). Post-translational modifications in aspartate aminotransferase from Sulfolobus solfataricus. Detection of N-c-methyllysines by mass spectrometry. Eur. J. Biochem. 222, 761-767.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 761-767
    • Zappacosta, F.1    Sannia, G.2    Savoy, L.-A.3    Marino, G.4    Pucci, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.