메뉴 건너뛰기




Volumn 80, Issue 11, 1998, Pages 933-941

Protein thermostability in extremophiles

Author keywords

Electrostatic interactions; Extremophiles; Hydrophobic interactions; Protein thermostability

Indexed keywords

BACTERIAL PROTEIN;

EID: 0032287230     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)88890-2     Document Type: Article
Times cited : (122)

References (71)
  • 1
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • [1] Stetter K.O., Hyperthermophilic procaryotes, FEMS Microbiol. Rev. 18 (1996) 149-158.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 2
    • 0029946198 scopus 로고    scopus 로고
    • Extremophile research in European Union: From fundamental aspects to industrial expectations
    • [2] Aguilar A., Extremophile research in European Union: from fundamental aspects to industrial expectations, FEMS Microbiol. Rev. 18 (1996) 89-62.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 89-162
    • Aguilar, A.1
  • 3
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • [3] Jaenicke R., Schurig H., Beaucamp N., Ostendorp R., Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima, Adv. Prot. Chem. 48 (1996) 181-269.
    • (1996) Adv. Prot. Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 4
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • [4] Privalov P.L., Stability of proteins. Small globular proteins, Adv. Prot. Chem. 33 (1979) 167-241.
    • (1979) Adv. Prot. Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 5
    • 0027769953 scopus 로고
    • Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis
    • [5] Stillman T.J., Baker P.J., Britton K.L., Rice D.W., Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis, J. Mol. Biol. 234 (1993) 1131-1139.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1131-1139
    • Stillman, T.J.1    Baker, P.J.2    Britton, K.L.3    Rice, D.W.4
  • 6
    • 0025179832 scopus 로고
    • Protein folding
    • [6] Creighton T.E., Protein folding, Biochem. J. 270 (1990) 1-16.
    • (1990) Biochem. J. , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 7
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • [7] Sturtevant J.M., Heat capacity and entropy changes in processes involving proteins, Proc. Natl. Acad. Sci. USA 74 (1977) 2236-2240 .
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 8
    • 0023442217 scopus 로고
    • Protein stability curves
    • [8] Becktel W.J., Schellman J.A., Protein stability curves, Biopolymers 26 (1987) 1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 10
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • [10] Privalov P.L., Gill S.J., Stability of protein structure and hydrophobic interaction, Adv Prot. Chem. 39 (1988) 193-231.
    • (1988) Adv Prot. Chem. , vol.39 , pp. 193-231
    • Privalov, P.L.1    Gill, S.J.2
  • 11
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • [11] Myers J.K., Pace C.N., Scholtz J.M., Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding, Protein Sci. 4 (1995) 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 12
    • 0029018003 scopus 로고
    • Thermodynamics of the temperature-induced unfolding of globular proteins
    • [12] Khechinashvili N.N., Janin J., Rodier F., Thermodynamics of the temperature-induced unfolding of globular proteins, Protein Sci. 4 (1995) 1315-1324.
    • (1995) Protein Sci. , vol.4 , pp. 1315-1324
    • Khechinashvili, N.N.1    Janin, J.2    Rodier, F.3
  • 13
    • 0027965116 scopus 로고
    • Hydration effects in protein unfolding
    • [13] Makhadhaze G.I., Privalov P.L., Hydration effects in protein unfolding, Biophys. Chem. 51 (1994) 291-309.
    • (1994) Biophys. Chem. , vol.51 , pp. 291-309
    • Makhadhaze, G.I.1    Privalov, P.L.2
  • 14
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbons and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of non-polar and polar surfaces from water
    • [14] Spolar R.S., Livingstone J.R., Record M.T., Use of liquid hydrocarbons and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of non-polar and polar surfaces from water, Biochemistry 31 (1992) 3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record, M.T.3
  • 15
    • 0019720278 scopus 로고
    • Globular protein stability: Aspects of interest in protein turnover
    • [15] Pace C.N., Fisher L.M., Cupo J.F., Globular protein stability: aspects of interest in protein turnover, Acta Biol. Med. Ger. 40 (1981) 1385-1392.
    • (1981) Acta Biol. Med. Ger. , vol.40 , pp. 1385-1392
    • Pace, C.N.1    Fisher, L.M.2    Cupo, J.F.3
  • 17
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • [17] Spolar R.S., Record M.T., Coupling of local folding to site-specific binding of proteins to DNA, Science 263 (1994) 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 18
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • [18] Pace C.N., Shirley B.A., Mc Nutt M., Gajiwala K., Forces contributing to the conformational stability of proteins, FASEB J. 10 (1996) 75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    Mc Nutt, M.3    Gajiwala, K.4
  • 20
    • 0000484499 scopus 로고
    • Hydrophobic parameters of amino acid side chains from the partitioning of N-acetyl-amino-acid amides
    • [20] Fauchere J.L., Pliska V.E., Hydrophobic parameters of amino acid side chains from the partitioning of N-acetyl-amino-acid amides, Eur. J. Med. Chem. 18 (1983) 369-375.
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.E.2
  • 21
    • 0027362193 scopus 로고
    • Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus studies on thermal and guanidine-dependent inactivation
    • [21] Consalvi V., Chiaraluce R., Politi L., Pasquo A., DeRosa M., Scandurra R., Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus studies on thermal and guanidine-dependent inactivation, Biochim. Biophys. Acta 1202 (1993) 207-215.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 207-215
    • Consalvi, V.1    Chiaraluce, R.2    Politi, L.3    Pasquo, A.4    DeRosa, M.5    Scandurra, R.6
  • 22
    • 0029987615 scopus 로고    scopus 로고
    • Refolding pathway and association intermediates of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus
    • [22] Consalvi V., Chiaraluce R., Millevoi S., Pasquo A., Vecchini P., Chiancone E., Scandurra R., Refolding pathway and association intermediates of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus, Eur. J. Biochem. 239 (1996) 679-685.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 679-685
    • Consalvi, V.1    Chiaraluce, R.2    Millevoi, S.3    Pasquo, A.4    Vecchini, P.5    Chiancone, E.6    Scandurra, R.7
  • 23
    • 0023992328 scopus 로고
    • The unfolding and refolding of glutamate dehydrogenase from bovine liver, baker's yeast and Clostridium symbiosum
    • [23] West S.M., Price N.C., The unfolding and refolding of glutamate dehydrogenase from bovine liver, baker's yeast and Clostridium symbiosum, Biochem. J. 251 (1988) 135-139.
    • (1988) Biochem. J. , vol.251 , pp. 135-139
    • West, S.M.1    Price, N.C.2
  • 24
    • 0029549021 scopus 로고
    • Exchange of domains of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus and the mesophilic bacterium Clostridium difficile: Effects on catalysis, thermoactivity and stability
    • [24] Lebbink J.H.G., Eggen R.I.L., Geerling A.C.M., Consalvi V., Chiaraluce R., Scandurra R., DeVos W.M., Exchange of domains of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus and the mesophilic bacterium Clostridium difficile: effects on catalysis, thermoactivity and stability, Prot. Engin. 8 (1995) 1287-1994.
    • (1995) Prot. Engin. , vol.8 , pp. 1287-1994
    • Lebbink, J.H.G.1    Eggen, R.I.L.2    Geerling, A.C.M.3    Consalvi, V.4    Chiaraluce, R.5    Scandurra, R.6    DeVos, W.M.7
  • 25
    • 0028774720 scopus 로고
    • The crystal structure of citrate synthase from the thermophilic Archaeon, Thermoplasma acidophilum
    • [25] Russel R.J.M., Hough D.W., Danson M.J., Taylor G.L., The crystal structure of citrate synthase from the thermophilic Archaeon, Thermoplasma acidophilum, Structure 2 (1994) 1157-1167.
    • (1994) Structure , vol.2 , pp. 1157-1167
    • Russel, R.J.M.1    Hough, D.W.2    Danson, M.J.3    Taylor, G.L.4
  • 26
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • [26] Jaenicke R., Protein stability and molecular adaptation to extreme conditions, Eur. J. Biochem. 202 (1991) 715-728.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 29
    • 0026580536 scopus 로고
    • The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, athermoacidophilic archaebacterium. Is the presence of N-ε-methylysine related to thermostability?
    • [29] Maras B., Consalvi V., Chiaraluce R., Politi L., DeRosa M., Bossa F., Scandurra R., Barra D., The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, athermoacidophilic archaebacterium. Is the presence of N-ε-methylysine related to thermostability?, Eur. J. Biochem. 203 (1992) 81-87.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 81-87
    • Maras, B.1    Consalvi, V.2    Chiaraluce, R.3    Politi, L.4    DeRosa, M.5    Bossa, F.6    Scandurra, R.7    Barra, D.8
  • 30
    • 0023759962 scopus 로고
    • Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the archaebacterium Sulfolobus solfataricus
    • [30] Choli T., Henning P., Wittmann-Liebold B., Reinhardt R., Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the archaebacterium Sulfolobus solfataricus, Biochim. Biophys. Acta 950 (1988) 193-203.
    • (1988) Biochim. Biophys. Acta , vol.950 , pp. 193-203
    • Choli, T.1    Henning, P.2    Wittmann-Liebold, B.3    Reinhardt, R.4
  • 32
    • 0025351922 scopus 로고
    • Proteins under extreme physical conditions
    • [32] Jaenicke R., Zavodsky P., Proteins under extreme physical conditions, FEBS Lett. 268 (1990) 344-349.
    • (1990) FEBS Lett. , vol.268 , pp. 344-349
    • Jaenicke, R.1    Zavodsky, P.2
  • 33
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • [33] Matthews B., Structural and genetic analysis of protein stability, Annu. Rev. Biochem. 62 (1993) 139-160.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.1
  • 35
    • 0024974452 scopus 로고
    • Engineering protein thermal stability
    • [35] Menéndez-Arias L., Argos P., Engineering protein thermal stability, J. Mol. Biol. 206 (1988) 397-406.
    • (1988) J. Mol. Biol. , vol.206 , pp. 397-406
    • Menéndez-Arias, L.1    Argos, P.2
  • 36
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • [36] Vihinen M., Relationship of protein flexibility to thermostability, Prot. Eng. 1 (1987) 477-480.
    • (1987) Prot. Eng. , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 37
    • 0019856479 scopus 로고
    • Protein thermostability. Correlation between calculated macroscopic parameters and growth temperature for closely related thermophilic and mesophilic bacilli
    • [37] Merkler D.J., Farrington G.K., Wedler F.C., Protein thermostability. Correlation between calculated macroscopic parameters and growth temperature for closely related thermophilic and mesophilic bacilli, Int. J. Pept. Protein Res. 18 (1981) 430-442.
    • (1981) Int. J. Pept. Protein Res. , vol.18 , pp. 430-442
    • Merkler, D.J.1    Farrington, G.K.2    Wedler, F.C.3
  • 38
    • 0019776488 scopus 로고
    • Dipoles of the α-helix and β-sheet: Their role in protein folding
    • [38] Hol W.G.J., Halie L.M., Sander C., Dipoles of the α-helix and β-sheet: their role in protein folding, Nature 294 (1981) 532-536.
    • (1981) Nature , vol.294 , pp. 532-536
    • Hol, W.G.J.1    Halie, L.M.2    Sander, C.3
  • 39
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational chracteristics related to thermostability
    • [39] Querol E., Perez-Pons J.A., Mozo-Villarias A., Analysis of protein conformational chracteristics related to thermostability, Prot. Eng. 9 (1996) 265-271.
    • (1996) Prot. Eng. , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 40
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glycerladehyde-3-phosphate dehydrogenase at 2.5 Å resolution
    • [40] Tanner J.J., Hecht R.M., Krause K.L., Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glycerladehyde-3-phosphate dehydrogenase at 2.5 Å resolution, Biochemistry 35 (1996) 2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 41
    • 0029056926 scopus 로고
    • Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5 Å resolution: Structural basis for thermostability
    • [41] Korolev S., Murad N., Barnes W.M., DiCera E., Waksman G., Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5 Å resolution: structural basis for thermostability, Proc. Natl. Acad. Sci. USA 92 (1995) 9264-9268.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9264-9268
    • Korolev, S.1    Murad, N.2    Barnes, W.M.3    DiCera, E.4    Waksman, G.5
  • 42
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the enthropy of unfolding
    • [42] Matthews B.W., Nicholson H., Becktel W.J., Enhanced protein thermostability from site-directed mutations that decrease the enthropy of unfolding, Proc. Natl. Acad. Sci USA 84 (1987) 6663-6667.
    • (1987) Proc. Natl. Acad. Sci USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 43
    • 0026714968 scopus 로고
    • Role of proline residues in human lysozyme stability: A scanning cslorimetric study combined with X-ray structure analysis of proline mutants
    • [43] Herning T., Yutani K., Inaka K., Kuroki R., Matsushima M., Kikuchi M., Role of proline residues in human lysozyme stability: a scanning cslorimetric study combined with X-ray structure analysis of proline mutants, Biochemistry 31 (1992) 7077-7085.
    • (1992) Biochemistry , vol.31 , pp. 7077-7085
    • Herning, T.1    Yutani, K.2    Inaka, K.3    Kuroki, R.4    Matsushima, M.5    Kikuchi, M.6
  • 44
    • 0028147704 scopus 로고
    • Role of cysteine residues in esterase from Bacillus staerothermophilus and increasing its thermostability by the replacement of cysteines
    • [44] Amaki Y., Nakano H., Yamane T., Role of cysteine residues in esterase from Bacillus staerothermophilus and increasing its thermostability by the replacement of cysteines, Appl. Microbiol. Biotechnol. 40 (1994) 664-668.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 664-668
    • Amaki, Y.1    Nakano, H.2    Yamane, T.3
  • 45
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • [45] Kelly C., Nishiyama M., Ohnishi Y, Beppu T., Birktoft J.J., Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus, Biochemistry 32 (1993) 3913-3922.
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 46
    • 0028846686 scopus 로고
    • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in sx isomerases with known three dimensional structures points to the importance of hydrophobic ineractions
    • [46] Delboni L.F., Mande S.C., Rentier-Delrue F., Mainfroid V., Turley S., Vellieux F.M.D., Martial J.A., Hol W.G.J., Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in sx isomerases with known three dimensional structures points to the importance of hydrophobic ineractions, Protein Sci. 4 (1995) 2594-2604.
    • (1995) Protein Sci. , vol.4 , pp. 2594-2604
    • Delboni, L.F.1    Mande, S.C.2    Rentier-Delrue, F.3    Mainfroid, V.4    Turley, S.5    Vellieux, F.M.D.6    Martial, J.A.7    Hol, W.G.J.8
  • 47
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • [47] Perutz M.F., Electrostatic effects in proteins, Science 210 (1978) 1187-1191.
    • (1978) Science , vol.210 , pp. 1187-1191
    • Perutz, M.F.1
  • 48
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2
    • [48] Perutz M., Raidt H., Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2, Nature 255 (1975) 255-259.
    • (1975) Nature , vol.255 , pp. 255-259
    • Perutz, M.1    Raidt, H.2
  • 49
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • [49] Hendsch Z.S., Tidor B., Do salt bridges stabilize proteins? A continuum electrostatic analysis, Prot. Sci. 3 (1994) 211-226.
    • (1994) Prot. Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 50
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • [50] Honig B., Nicholls A., Classical electrostatics in biology and chemistry, Science 268 (1995) 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 51
    • 0026345864 scopus 로고
    • Structural and tnermodynamic consequences of burying a charged residue within the hydrophobic of T4 lysozyme
    • [51] Dao-Pin S., Anderson D.E., Baase W.A., Dahlquist F.W., Matthews B.W., Structural and tnermodynamic consequences of burying a charged residue within the hydrophobic of T4 lysozyme, Biochemistry 30 (1991) 11521-11529.
    • (1991) Biochemistry , vol.30 , pp. 11521-11529
    • Dao-Pin, S.1    Anderson, D.E.2    Baase, W.A.3    Dahlquist, F.W.4    Matthews, B.W.5
  • 52
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • [52] Waldburger C.D., Schildbach J.F., Sauer R.T., Are buried salt bridges important for protein stability and conformational specificity?, Nature Struct. Biol. 2 (1995) 122-128.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 53
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds and ion pairs
    • [53] Vogt G., Woell S., Argos P., Protein thermal stability, hydrogen bonds and ion pairs, J. Mol. Biol. 269 (1997) 631-643.
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 55
    • 0031564613 scopus 로고    scopus 로고
    • Crystal structure of glutamate dehydrogenase from hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution
    • [55] Knapp S., DeVos W., Rice D., Ladenstein R., Crystal structure of glutamate dehydrogenase from hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution, J. Mol. Biol. 267 (1997) 916-932.
    • (1997) J. Mol. Biol. , vol.267 , pp. 916-932
    • Knapp, S.1    DeVos, W.2    Rice, D.3    Ladenstein, R.4
  • 57
    • 0028961901 scopus 로고
    • Structure of hyperthermophilic tungstenopterin enzyme, aldehyde ferredoxin oxidoreductase
    • [57] Chan M.K., Mukund S., Kietzin A., Adams M.W.W., Rees D.C., Structure of hyperthermophilic tungstenopterin enzyme, aldehyde ferredoxin oxidoreductase, Science 267 (1995) 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kietzin, A.3    Adams, M.W.W.4    Rees, D.C.5
  • 58
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-Superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • [58] Jae-Hwan L., Yeon G.Y., Ye S.H., Seung-Je C., Byung-Yoon A., Sung-Hou K., Yunje C., The crystal structure of an Fe-Superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: structural basis for thermostability, J. Mol. Biol. 270 (1997) 259-274.
    • (1997) J. Mol. Biol. , vol.270 , pp. 259-274
    • Jae-Hwan, L.1    Yeon, G.Y.2    Ye, S.H.3    Seung-Je, C.4    Byung-Yoon, A.5    Sung-Hou, K.6    Yunje, C.7
  • 59
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • [59] Dill K., Dominant forces in protein folding, Biochemistry 29 (1990) 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.1
  • 60
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • [60] Tsai C.J., Lin S.L., Wolfson H.J., Nussinov R., Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect, Protein Sci. 6 (1997) 53-64.
    • (1997) Protein Sci. , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 61
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distribution and packing density
    • [61] Richards F.M., The interpretation of protein structures: total volume, group volume distribution and packing density, J. Mol. Biol. 82 (1974) 1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 62
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • [62] Richards F.M., Areas, volumes, packing and protein structure, Annu. Rev. Biophys. Bioeng. 6 (1977) 151-175.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-175
    • Richards, F.M.1
  • 63
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • [63] Korndörfer I., Steipe B., Huber R., Tomschy A., Jaenicke R., The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution, J. Mol. Biol. 246 (1995) 511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 65
    • 0030970741 scopus 로고    scopus 로고
    • Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus
    • [65] Haney P., Konisky K.K., Luthey-Schulten Wolynes P.G., Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus, Proteins 28 (1997) 117-130.
    • (1997) Proteins , vol.28 , pp. 117-130
    • Haney, P.1    Konisky, K.K.2    Luthey-Schulten Wolynes, P.G.3
  • 68
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • [68] Hennig M., Darimont B., Sterner R., Kirschner K., Jansonius J.N., 2.0 Å structure of indole-3-glycerol phosphate synthase from hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability, Structure 3 (1995) 1295-1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 69
    • 0030568997 scopus 로고    scopus 로고
    • The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: Effects of ionic strength
    • [69] Knöchel T.R., Hennig M., Merz A., Darimont B., Kirschner K., Jansonius J.N., The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effects of ionic strength, J. Mol. Biol. 262 (1996) 502-515.
    • (1996) J. Mol. Biol. , vol.262 , pp. 502-515
    • Knöchel, T.R.1    Hennig, M.2    Merz, A.3    Darimont, B.4    Kirschner, K.5    Jansonius, J.N.6
  • 71
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the β-glycosidase from the hyperthermophiilic archaeon Sulfolobus solfataricus: Resilience as a key factor in thermostability
    • [71] Aguilar C., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., Pearl L.H., Crystal structure of the β-glycosidase from the hyperthermophiilic archaeon Sulfolobus solfataricus: resilience as a key factor in thermostability, J. Mol. Biol. 271 (1997) 789-80.
    • (1997) J. Mol. Biol. , vol.271 , pp. 789-880
    • Aguilar, C.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6    Pearl, L.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.