메뉴 건너뛰기




Volumn 19, Issue 1, 1996, Pages 74-79

The upper limits of enzyme thermal stability

Author keywords

Degradation; Denaturation; Enzyme engineering; Enzymes; Stability; Thermophiles

Indexed keywords

CONFORMATIONS; DEGRADATION; GENETIC ENGINEERING; GROWTH KINETICS; PROTEINS; THERMODYNAMIC STABILITY;

EID: 0030199970     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/0141-0229(95)00174-3     Document Type: Article
Times cited : (143)

References (66)
  • 1
    • 0001872834 scopus 로고
    • Modern life at high temperatures
    • Daniel, R. M. Modern life at high temperatures. Orig. Life Evol. Biosph. 1992, 22, 33-42
    • (1992) Orig. Life Evol. Biosph. , vol.22 , pp. 33-42
    • Daniel, R.M.1
  • 2
    • 0021892611 scopus 로고
    • The mechanism of irreversible enzyme inactivation at 100°C
    • Ahern, J. J. and Klibanov, A. M. The mechanism of irreversible enzyme inactivation at 100°C. Science 1985, 228, 1280-1284
    • (1985) Science , vol.228 , pp. 1280-1284
    • Ahern, J.J.1    Klibanov, A.M.2
  • 3
    • 0026469488 scopus 로고
    • The enzymes from extreme thermophiles: Bacterial sources, thermostabilities, and industrial relevance
    • Coolbear, T., Daniel, R. M., and Morgan, H. W. The enzymes from extreme thermophiles: Bacterial sources, thermostabilities, and industrial relevance. Adv. Biochem. Eng. Biotech. 1992, 45, 57-98
    • (1992) Adv. Biochem. Eng. Biotech. , vol.45 , pp. 57-98
    • Coolbear, T.1    Daniel, R.M.2    Morgan, H.W.3
  • 4
    • 0025061657 scopus 로고
    • Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus
    • Koch, R., Zoblowski, P., Spreinat, A., and Antranikian, G. Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus. FEMS Microbiol. Lett. 1990, 71, 21-26
    • (1990) FEMS Microbiol. Lett. , vol.71 , pp. 21-26
    • Koch, R.1    Zoblowski, P.2    Spreinat, A.3    Antranikian, G.4
  • 5
    • 0025870894 scopus 로고
    • An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga Fj SS3-B1
    • Simpson, H. D., Haufler, U. R., and Daniel, R. M. An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga Fj SS3-B1. Biochem. J. 1991, 277, 413-417
    • (1991) Biochem. J. , vol.277 , pp. 413-417
    • Simpson, H.D.1    Haufler, U.R.2    Daniel, R.M.3
  • 7
    • 85025384988 scopus 로고
    • Pyrodictium gen. nov.; a new species of submarine disc-shaped sulphur-reducing Archaebacteria growing optimally at 105°C
    • Stetter, K. O., Konig, H., and Stackebrandt, E. Pyrodictium gen. nov.; A new species of submarine disc-shaped sulphur-reducing Archaebacteria growing optimally at 105°C. Syst. Appl. Microbiol. 1983, 4, 535-551
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 535-551
    • Stetter, K.O.1    Konig, H.2    Stackebrandt, E.3
  • 8
    • 0019510613 scopus 로고
    • Cloning of 3-isopropyl-malate dehydrogenase gene of an extreme thermophile and partial purification of the gene product
    • Tanaka, T., Kawano, N., and Oshima, T. Cloning of 3-isopropyl-malate dehydrogenase gene of an extreme thermophile and partial purification of the gene product. J. Biochem. 1981, 89, 677-689
    • (1981) J. Biochem. , vol.89 , pp. 677-689
    • Tanaka, T.1    Kawano, N.2    Oshima, T.3
  • 10
    • 0020479358 scopus 로고
    • Purification and some properties of an extracellular protease (Caldolysin) from an extreme thermophile
    • Cowan, D. A. and Daniel, R. M. Purification and some properties of an extracellular protease (Caldolysin) from an extreme thermophile. Biochem. Biophys. Acta 1982, 705, 293-305
    • (1982) Biochem. Biophys. Acta , vol.705 , pp. 293-305
    • Cowan, D.A.1    Daniel, R.M.2
  • 11
    • 0021763831 scopus 로고
    • Interactions of calcium and other metal ions with Caldolysin
    • Khoo, T. C., Cowan, D. A., Daniel, R. M., and Morgan, H. W. Interactions of calcium and other metal ions with Caldolysin. Biochem. J. 1984, 221, 407-413
    • (1984) Biochem. J. , vol.221 , pp. 407-413
    • Khoo, T.C.1    Cowan, D.A.2    Daniel, R.M.3    Morgan, H.W.4
  • 12
  • 13
    • 0024613893 scopus 로고
    • Nucleotide sequence of the glyceraldehyde 3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum
    • Fabry, S., Lang, J., Nierman, T., Vingron, M., and Hensel, R. Nucleotide sequence of the glyceraldehyde 3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum. Eur. J. Biochem. 1989, 179, 405-413
    • (1989) Eur. J. Biochem. , vol.179 , pp. 405-413
    • Fabry, S.1    Lang, J.2    Nierman, T.3    Vingron, M.4    Hensel, R.5
  • 14
    • 0024974452 scopus 로고
    • Engineering protein thermal stability
    • Menendez-Arias, L. and Argos, P. Engineering protein thermal stability. J. Mol. Biol. 1989, 206, 397-406
    • (1989) J. Mol. Biol. , vol.206 , pp. 397-406
    • Menendez-Arias, L.1    Argos, P.2
  • 15
    • 0028014604 scopus 로고
    • Relevance of sequence statistics for the properties of extremophilic proteins
    • Bohm, G. and Jaenicke, R. Relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Peptide Protein Res. 1994, 43, 97-106
    • (1994) Int. J. Peptide Protein Res. , vol.43 , pp. 97-106
    • Bohm, G.1    Jaenicke, R.2
  • 16
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferrodoxins and in haemoglobin
    • Perutz, M. F. and Raidt, H. Stereochemical basis of heat stability in bacterial ferrodoxins and in haemoglobin. Nature 1975, 255, 256-259
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 17
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews, B. W. Structural and genetic analysis of protein stability. Ann. Rev. Biochem. 1993, 62, 139-160
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 18
    • 0025351922 scopus 로고
    • Proteins under extreme physical conditions
    • Jaenicke, R. and Zavodszky, P. Proteins under extreme physical conditions. FEBS Lett. 1990, 268, 344-349
    • (1990) FEBS Lett. , vol.268 , pp. 344-349
    • Jaenicke, R.1    Zavodszky, P.2
  • 19
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100°C
    • Adams, M. W. W. Enzymes and proteins from organisms that grow near and above 100°C. Ann. Rev. Microbiol. 1993, 47, 627-658
    • (1993) Ann. Rev. Microbiol. , vol.47 , pp. 627-658
    • Adams, M.W.W.1
  • 20
    • 0342875456 scopus 로고
    • Proteins of extreme thermophiles
    • (Kates, M., Ed.). Elsevier, New York
    • Hensel, R. Proteins of extreme thermophiles. In: The Biochemistry of the Archaea (Kates, M., Ed.). Elsevier, New York, 1993
    • (1993) The Biochemistry of the Archaea
    • Hensel, R.1
  • 22
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C. R. Bacterial evolution. Microbiol. Rev. 1987, 51, 221-271
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 25
    • 0014349928 scopus 로고
    • Genetic and enzymatic experiments relating to the tertiary structure of β-galactosidase
    • Langridge, J. Genetic and enzymatic experiments relating to the tertiary structure of β-galactosidase. J. Bact. 1968, 96, 1711-1717
    • (1968) J. Bact. , vol.96 , pp. 1711-1717
    • Langridge, J.1
  • 26
    • 0024412497 scopus 로고
    • Mutational effects on protein stability
    • Alber, T. Mutational effects on protein stability. Ann. Rev. Biochem. 1989, 58, 765-798
    • (1989) Ann. Rev. Biochem. , vol.58 , pp. 765-798
    • Alber, T.1
  • 27
    • 0023643422 scopus 로고
    • Genetic and structural analysis of the protein stability problem
    • Matthews, B. W. Genetic and structural analysis of the protein stability problem. Biochemistry 1987, 26, 6885-6888
    • (1987) Biochemistry , vol.26 , pp. 6885-6888
    • Matthews, B.W.1
  • 28
    • 0005876924 scopus 로고
    • Bacteriophage λ cro mutations: Effects on activity and intracellular degradation
    • Pakula, A. A., Young, V. B., and Sauer, R. T. Bacteriophage λ cro mutations: Effects on activity and intracellular degradation. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 8829-8833
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8829-8833
    • Pakula, A.A.1    Young, V.B.2    Sauer, R.T.3
  • 30
    • 0344027824 scopus 로고
    • A genetic screen for mutations that increase the thermal stability of phage T4 lysozyme
    • Alber, T. and Wozniak, J. A. A genetic screen for mutations that increase the thermal stability of phage T4 lysozyme. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 747-750
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 747-750
    • Alber, T.1    Wozniak, J.A.2
  • 31
    • 0022403302 scopus 로고
    • Screening for thermostable mutant of kanamycin nucleotidyl transferase by the use of a transformation system for a thermophile Bacillus stearothermophilus
    • Matsumura, M. and Aiba, S. Screening for thermostable mutant of kanamycin nucleotidyl transferase by the use of a transformation system for a thermophile Bacillus stearothermophilus. J. Biol. Chem. 1985, 260, 15298-15303
    • (1985) J. Biol. Chem. , vol.260 , pp. 15298-15303
    • Matsumura, M.1    Aiba, S.2
  • 32
    • 0342367772 scopus 로고
    • Isolation of a thermostable enzyme variant by cloning and selection in a thermophile
    • Liao, H., Mackenzie, T., and Hageman, R. Isolation of a thermostable enzyme variant by cloning and selection in a thermophile. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 576-580
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 576-580
    • Liao, H.1    Mackenzie, T.2    Hageman, R.3
  • 34
    • 0001767586 scopus 로고
    • A strong correlation between the increase in the number of proline residues and the rise in thermostability of 5 Bacillus oligo-1-6-glucosidases
    • Suzuki, Y., Oishi, K., Nakano, H., and Nagayama, T. A strong correlation between the increase in the number of proline residues and the rise in thermostability of 5 Bacillus oligo-1-6-glucosidases. Appl. Micro. Biotech. 1987, 26, 546-551
    • (1987) Appl. Micro. Biotech. , vol.26 , pp. 546-551
    • Suzuki, Y.1    Oishi, K.2    Nakano, H.3    Nagayama, T.4
  • 35
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews, B. W., Nicholson, H., and Becktel, W. J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 6663-6667
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 36
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • Serrano, L. and Ferst, A. R. Capping and α-helix stability. Nature 1989, 342, 296-299
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Ferst, A.R.2
  • 37
    • 0026696173 scopus 로고
    • Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59
    • Bell, J. A., Bechtel, W. J., Sayer, U., Baase, W. H., and Matthews, B. W. Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. Biochemistry 1992, 31, 3590-3596
    • (1992) Biochemistry , vol.31 , pp. 3590-3596
    • Bell, J.A.1    Bechtel, W.J.2    Sayer, U.3    Baase, W.H.4    Matthews, B.W.5
  • 39
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J. A. Additivity of mutational effects in proteins. Biochemistry 1990, 29, 8509-8517
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 40
    • 85030205169 scopus 로고    scopus 로고
    • Properties and stabilisation of an extracellular α-glucosidase from the extremely thermophilic archaea, Thermococcus strain ANI: Enzyme activity at 130°C
    • in press
    • Piller, K., Daniel, R. M., and Petach, H. Properties and stabilisation of an extracellular α-glucosidase from the extremely thermophilic archaea, Thermococcus strain ANI: Enzyme activity at 130°C. Biochim. Biophys. Acta (in press)
    • Biochim. Biophys. Acta
    • Piller, K.1    Daniel, R.M.2    Petach, H.3
  • 41
    • 0001912876 scopus 로고
    • Thermoadaption of methanogenic bacteria by intracellular ion concentration
    • Hensel, R. and Konig, H. Thermoadaption of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 1988, 49, 75-79
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 75-79
    • Hensel, R.1    Konig, H.2
  • 42
    • 0023069360 scopus 로고
    • The specific activities of mesophilic and thermophilic proteinases
    • Cowan, D. A., Daniel, R. M., and Morgan, H. W. The specific activities of mesophilic and thermophilic proteinases. Int. J. Biochem. 1987, 19, 741-743
    • (1987) Int. J. Biochem. , vol.19 , pp. 741-743
    • Cowan, D.A.1    Daniel, R.M.2    Morgan, H.W.3
  • 43
    • 0018782123 scopus 로고
    • Correlation between the amide proton exchange rates and the denaturation temperature in globular proteins related to the basic pancreatic trypsin inhibitor
    • Wagner, G. and Wuthrich, K. Correlation between the amide proton exchange rates and the denaturation temperature in globular proteins related to the basic pancreatic trypsin inhibitor. J. Mol. Biol. 1979, 130, 31-37
    • (1979) J. Mol. Biol. , vol.130 , pp. 31-37
    • Wagner, G.1    Wuthrich, K.2
  • 44
    • 0025182490 scopus 로고
    • Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wrba, A., Schweiger, A., Schultes, V., Jaenicke, R., and Zavodszky, P. Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry 1990, 29, 7592-7594
    • (1990) Biochemistry , vol.29 , pp. 7592-7594
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Zavodszky, P.5
  • 45
    • 0025822794 scopus 로고
    • Relation between stability, dynamics, and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
    • Varley, P. G. and Pain, R. H. Relation between stability, dynamics, and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus. J. Mol. Biol. 1991, 220, 531-538
    • (1991) J. Mol. Biol. , vol.220 , pp. 531-538
    • Varley, P.G.1    Pain, R.H.2
  • 46
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • Vihinen, M. Relationship of protein flexibility to thermostability. Protein Eng. 1987, 1, 477-480
    • (1987) Protein Eng. , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 47
    • 0013965360 scopus 로고
    • The conversion of serine at the active site of subtilisin to cysteine: A chemical mutation
    • Neet, K. E. and Koshland, D. E. The conversion of serine at the active site of subtilisin to cysteine: A chemical mutation. Proc. Natl. Acad. Sci. U.S.A. 1966, 56, 1606-1611
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.56 , pp. 1606-1611
    • Neet, K.E.1    Koshland, D.E.2
  • 48
    • 0000662833 scopus 로고
    • The molecular basis of enzyme regulation
    • 3rd Ed. (Boyer, P. D., Ed.). Academic Press, New York
    • Koshland, D. E. The molecular basis of enzyme regulation. In: The Enzymes Vol. 1, 3rd Ed. (Boyer, P. D., Ed.). Academic Press, New York, 1970, 332
    • (1970) The Enzymes , vol.1 , pp. 332
    • Koshland, D.E.1
  • 49
    • 0018793861 scopus 로고
    • Temperature-dependent x-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder, H., Petsko, G. A., and Tsernoglou, D. Temperature-dependent x-ray diffraction as a probe of protein structural dynamics. Nature 1979, 280, 558-563
    • (1979) Nature , vol.280 , pp. 558-563
    • Frauenfelder, H.1    Petsko, G.A.2    Tsernoglou, D.3
  • 51
    • 0020647920 scopus 로고
    • Functional significance of flexibility in proteins
    • Huber, R. and Bennett, W. S. Functional significance of flexibility in proteins. Biopolymers 1983, 22, 261-279
    • (1983) Biopolymers , vol.22 , pp. 261-279
    • Huber, R.1    Bennett, W.S.2
  • 52
    • 0342875445 scopus 로고
    • The stability of proteins from extreme thermophiles
    • (Oxender, D. L., Ed.). Liss, New York
    • Daniel, R. M. The stability of proteins from extreme thermophiles. In: Protein Structure, Folding, and Design (Oxender, D. L., Ed.). Liss, New York, 1986, 291-296
    • (1986) Protein Structure, Folding, and Design , pp. 291-296
    • Daniel, R.M.1
  • 53
    • 0023043961 scopus 로고
    • The immune response to proteins from extreme thermophiles
    • Daniel, R. M. The immune response to proteins from extreme thermophiles. J. Theor. Biol. 1986, 120, 125-127
    • (1986) J. Theor. Biol. , vol.120 , pp. 125-127
    • Daniel, R.M.1
  • 54
    • 84996075885 scopus 로고
    • Relation between the stabilisation and rigidification of the 3-dimensional structure of an enzyme
    • Germain, P., Slagmolen, T., and Crighton, R. R. Relation between the stabilisation and rigidification of the 3-dimensional structure of an enzyme. Biotech. Bioeng. 1989, 33, 563-569
    • (1989) Biotech. Bioeng. , vol.33 , pp. 563-569
    • Germain, P.1    Slagmolen, T.2    Crighton, R.R.3
  • 55
    • 0020394274 scopus 로고
    • A correlation between protein thermostability and resistance to proteolysis
    • Daniel, R. M., Cowan, D. A., Morgan, H. W., and Curran, M. P. A correlation between protein thermostability and resistance to proteolysis. Biochem. J. 1982, 207, 641-644
    • (1982) Biochem. J. , vol.207 , pp. 641-644
    • Daniel, R.M.1    Cowan, D.A.2    Morgan, H.W.3    Curran, M.P.4
  • 56
    • 0022538679 scopus 로고
    • Cumulative effect of intragenic amino acid replacements on the thermostability of a protein
    • Matsumura, M., Yasumura, S., and Aiba, S. Cumulative effect of intragenic amino acid replacements on the thermostability of a protein. Nature 1986, 23, 356-358
    • (1986) Nature , vol.23 , pp. 356-358
    • Matsumura, M.1    Yasumura, S.2    Aiba, S.3
  • 57
    • 0025652792 scopus 로고
    • Characterisation of mutant glucose dehydrogenases with increasing stability
    • Yamamoto, K., Nagao, T., Makino, Y., Urabe, I., and Okada, H. Characterisation of mutant glucose dehydrogenases with increasing stability. Ann. N.Y. Acad. Sci. 1990, 613, 362-365
    • (1990) Ann. N.Y. Acad. Sci. , vol.613 , pp. 362-365
    • Yamamoto, K.1    Nagao, T.2    Makino, Y.3    Urabe, I.4    Okada, H.5
  • 59
    • 0024429207 scopus 로고
    • NMR studies of mobility within protein structure
    • Williams, R. J. P. NMR studies of mobility within protein structure. Eur. J. Biochem. 1989, 183, 479-497
    • (1989) Eur. J. Biochem. , vol.183 , pp. 479-497
    • Williams, R.J.P.1
  • 60
    • 0018802524 scopus 로고
    • Space-filling models of kinase clefts and conformation changes
    • Anderson, C. M., Zucker, F. H., and Steitz, T. A. Space-filling models of kinase clefts and conformation changes. Science 1979, 204, 375-380
    • (1979) Science , vol.204 , pp. 375-380
    • Anderson, C.M.1    Zucker, F.H.2    Steitz, T.A.3
  • 61
    • 0002954496 scopus 로고
    • Enzymes from extreme environments
    • (Abvamowicz, D. A., Ed.). Van Nostrand Reinhold, New York
    • Daniel, R. M., Bragger, J. M., and Morgan, H. W. Enzymes from extreme environments. In: Biocatalysis (Abvamowicz, D. A., Ed.). Van Nostrand Reinhold, New York, 1990, 243-254
    • (1990) Biocatalysis , pp. 243-254
    • Daniel, R.M.1    Bragger, J.M.2    Morgan, H.W.3
  • 62
    • 0023464863 scopus 로고
    • Propensity for spontaneous succinamide formation from aspartyl and asparaginyl residues in cellular proteins
    • Clarke, S. Propensity for spontaneous succinamide formation from aspartyl and asparaginyl residues in cellular proteins. Int. J. Pep. Protein Res. 1987, 30, 808-821
    • (1987) Int. J. Pep. Protein Res. , vol.30 , pp. 808-821
    • Clarke, S.1
  • 63
    • 0024516367 scopus 로고
    • Succinamide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins
    • Stephenson, R. C. and Clarke, S. Succinamide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 1989, 264, 6164-6170
    • (1989) J. Biol. Chem. , vol.264 , pp. 6164-6170
    • Stephenson, R.C.1    Clarke, S.2
  • 64
    • 0025690709 scopus 로고
    • Formation of isoaspartate in human growth hormone and bovine brain calmodulin
    • Aswad, D. Formation of isoaspartate in human growth hormone and bovine brain calmodulin. Ann. N.Y. Acad. Sci. 1990, 613, 26-36
    • (1990) Ann. N.Y. Acad. Sci. , vol.613 , pp. 26-36
    • Aswad, D.1
  • 65
    • 0026736883 scopus 로고
    • Proteins from hyperthermophilic archaea: Stability towards covalent modification of the peptide chain
    • Hensel, R., Jakob, I., Scheer, H., and Lottspeich, R. Proteins from hyperthermophilic archaea: Stability towards covalent modification of the peptide chain. Biochem. Soc. Symp. 1992, 58, 127-133
    • (1992) Biochem. Soc. Symp. , vol.58 , pp. 127-133
    • Hensel, R.1    Jakob, I.2    Scheer, H.3    Lottspeich, R.4
  • 66
    • 0021753827 scopus 로고
    • Hydrolytic stability of biomolecules at high temperatures and its implications for life at 250°C
    • White, R. H. Hydrolytic stability of biomolecules at high temperatures and its implications for life at 250°C. Nature 1984, 310, 430-432
    • (1984) Nature , vol.310 , pp. 430-432
    • White, R.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.