메뉴 건너뛰기




Volumn 14, Issue 4, 2003, Pages 360-365

New understandings of thermostable and peizostable enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; ENZYME;

EID: 0042433116     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(03)00075-2     Document Type: Review
Times cited : (88)

References (49)
  • 2
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Comprehensive review on hyperthermophiles with special emphasis on mechanisms of thermostabilization and the commercial application of thermostable enzymes.
    • Vieille C., Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65:2001;1-43 Comprehensive review on hyperthermophiles with special emphasis on mechanisms of thermostabilization and the commercial application of thermostable enzymes.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 3
    • 0035214616 scopus 로고    scopus 로고
    • Bivalent cations and amino-acid composition contribute to the thermostability of Bacillus licheniformis xylose isomerase
    • Vieille C., Epting K.L., Kelly R.M., Zeikus J.G. Bivalent cations and amino-acid composition contribute to the thermostability of Bacillus licheniformis xylose isomerase. Eur. J. Biochem. 268:2001;6291-6301.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6291-6301
    • Vieille, C.1    Epting, K.L.2    Kelly, R.M.3    Zeikus, J.G.4
  • 4
    • 0035283618 scopus 로고    scopus 로고
    • The biotechnological potential of piezophiles
    • One of the few reviews on pressure-stable enzymes, discusses the commercial application of piezostable enzymes.
    • Abe F., Horikoshi K. The biotechnological potential of piezophiles. Trends Biotechnol. 19:2001;102-108 One of the few reviews on pressure-stable enzymes, discusses the commercial application of piezostable enzymes.
    • (2001) Trends Biotechnol. , vol.19 , pp. 102-108
    • Abe, F.1    Horikoshi, K.2
  • 5
    • 0036425552 scopus 로고    scopus 로고
    • Role of cation-pi interactions to the stability of thermophilic proteins
    • Gromiha M.M., Thomas S., Santhosh C. Role of cation-pi interactions to the stability of thermophilic proteins. Prep. Biochem. Biotechnol. 32:2002;355-362.
    • (2002) Prep. Biochem. Biotechnol. , vol.32 , pp. 355-362
    • Gromiha, M.M.1    Thomas, S.2    Santhosh, C.3
  • 6
    • 0037172796 scopus 로고    scopus 로고
    • Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study
    • Chakravarty S., Varadarajan R. Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study. Biochemistry. 41:2002;8152-8161.
    • (2002) Biochemistry , vol.41 , pp. 8152-8161
    • Chakravarty, S.1    Varadarajan, R.2
  • 7
    • 0034624393 scopus 로고    scopus 로고
    • A computational study of cation-π interactions vs salt bridges in aqueous media: Implications for protein engineering
    • Gallivan J.P., Dougherty D.A. A computational study of cation-π interactions vs salt bridges in aqueous media: implications for protein engineering. J. Am. Chem. Soc. 122:2000;870-874.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 870-874
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 8
    • 0035827175 scopus 로고    scopus 로고
    • In-vitro selection of highly stabilized protein variants with optimized surface
    • Elegant study demonstrating the Proside selection method. Proside links the increased protease resistance of stabilized protein variants with the infectivity of the phage. This study demonstrated the importance of the protein surface in thermal adaptation and showed that there may be multiple pathways to increasing stability.
    • Martin A., Sieber V., Schmid F.X. In-vitro selection of highly stabilized protein variants with optimized surface. J. Mol. Biol. 309:2001;717-726 Elegant study demonstrating the Proside selection method. Proside links the increased protease resistance of stabilized protein variants with the infectivity of the phage. This study demonstrated the importance of the protein surface in thermal adaptation and showed that there may be multiple pathways to increasing stability.
    • (2001) J. Mol. Biol. , vol.309 , pp. 717-726
    • Martin, A.1    Sieber, V.2    Schmid, F.X.3
  • 9
    • 0036310988 scopus 로고    scopus 로고
    • Origins of the high stability of an in vitro-selected cold-shock protein
    • Martin A., Kather I., Schmid F.X. Origins of the high stability of an in vitro-selected cold-shock protein. J. Mol. Biol. 318:2002;1341-1349.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1341-1349
    • Martin, A.1    Kather, I.2    Schmid, F.X.3
  • 10
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber V., Pluckthun A., Schmid F.X. Selecting proteins with improved stability by a phage-based method. Nat. Biotechnol. 16:1998;955-960.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 955-960
    • Sieber, V.1    Pluckthun, A.2    Schmid, F.X.3
  • 11
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D., Mueller U., Heinemann U., Schmid F.X. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat. Struct. Biol. 7:2000;380-383.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 12
    • 0035914477 scopus 로고    scopus 로고
    • Electrostatic stabilization of a thermophilic cold shock protein
    • Perl D., Schmid F.X. Electrostatic stabilization of a thermophilic cold shock protein. J. Mol. Biol. 313:2001;343-357.
    • (2001) J. Mol. Biol. , vol.313 , pp. 343-357
    • Perl, D.1    Schmid, F.X.2
  • 13
    • 0035840105 scopus 로고    scopus 로고
    • Patterns of adaptation in a laboratory evolved thermophilic enzyme
    • Wintrode P.L., Miyazaki K., Arnold F.H. Patterns of adaptation in a laboratory evolved thermophilic enzyme. Biochim. Biophys. Acta. 1549:2001;1-8.
    • (2001) Biochim. Biophys. Acta , vol.1549 , pp. 1-8
    • Wintrode, P.L.1    Miyazaki, K.2    Arnold, F.H.3
  • 14
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger C.D., Schildbach J.F., Sauer R.T. Are buried salt bridges important for protein stability and conformational specificity? Nat. Struct. Biol. 2:1995;122-128.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 15
    • 0347927627 scopus 로고    scopus 로고
    • Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus
    • Yano J.K., Blasco F., Li H., Schmid R.D., Henne A., Poulos T.L. Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus. J. Biol. Chem. 278:2003;608-616.
    • (2003) J. Biol. Chem. , vol.278 , pp. 608-616
    • Yano, J.K.1    Blasco, F.2    Li, H.3    Schmid, R.D.4    Henne, A.5    Poulos, T.L.6
  • 16
    • 0035427308 scopus 로고    scopus 로고
    • Cooperative helix stabilization by complex Arg-Glu salt bridges
    • This study demonstrates the importance of salt-link networks over isolated charge-charge interactions. It estimates that triads of charged sidechains spaced at i,i + 4 or i,i + 3 intervals in a helical peptide increase stability >1 kcal/mol more than the sum of the individual pairs.
    • Olson C.A., Spek E.J., Shi Z., Vologodskii A., Kallenbach N.R. Cooperative helix stabilization by complex Arg-Glu salt bridges. Proteins. 44:2001;123-132 This study demonstrates the importance of salt-link networks over isolated charge-charge interactions. It estimates that triads of charged sidechains spaced at i,i + 4 or i,i + 3 intervals in a helical peptide increase stability >1 kcal/mol more than the sum of the individual pairs.
    • (2001) Proteins , vol.44 , pp. 123-132
    • Olson, C.A.1    Spek, E.J.2    Shi, Z.3    Vologodskii, A.4    Kallenbach, N.R.5
  • 17
    • 0034633994 scopus 로고    scopus 로고
    • Contribution of salt bridges near the surface of a protein to the conformational stability
    • Takano K., Tsuchimori K., Yamagata Y., Yutani K. Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry. 39:2000;12375-12381.
    • (2000) Biochemistry , vol.39 , pp. 12375-12381
    • Takano, K.1    Tsuchimori, K.2    Yamagata, Y.3    Yutani, K.4
  • 18
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analsyis
    • Hendsch Z.S., Tidor B. Do salt bridges stabilize proteins? A continuum electrostatic analsyis. Protein Sci. 3:1994;211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 19
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar S., Nussinov R. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83:2002;1595-1612.
    • (2002) Biophys. J. , vol.83 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 20
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock A.D. The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J. Mol. Biol. 284:1998;489-502.
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.D.1
  • 21
    • 0027959168 scopus 로고
    • Pressure effects on enzyme reactions in mainly organic media: Α-chymotrypsin in reversed micelles of Aerosol OT in octane
    • Mozhaev V.V., Bec N., Balny C. Pressure effects on enzyme reactions in mainly organic media: α-chymotrypsin in reversed micelles of Aerosol OT in octane. Biochem. Mol. Biol. Int. 34:1994;191-199.
    • (1994) Biochem. Mol. Biol. Int. , vol.34 , pp. 191-199
    • Mozhaev, V.V.1    Bec, N.2    Balny, C.3
  • 22
    • 0029041846 scopus 로고
    • Pressure stabilization is not a general property of thermophilic enzymes: The adenylate kinases of Methanococcus voltae, Methanococcus maripaludis, Methanococcus thermolithotrophicus, and Methanococcus jannaschii
    • Konisky J., Michels P.C., Clark D.S. Pressure stabilization is not a general property of thermophilic enzymes: the adenylate kinases of Methanococcus voltae, Methanococcus maripaludis, Methanococcus thermolithotrophicus, and Methanococcus jannaschii. Appl. Environ. Microbiol. 61:1995;2762-2764.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2762-2764
    • Konisky, J.1    Michels, P.C.2    Clark, D.S.3
  • 23
    • 0034823445 scopus 로고    scopus 로고
    • Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants
    • Tschirret-Guth R.A., Koo L.S., Hoa G.H., Ortiz De Montellano P.R. Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants. J. Am. Chem. Soc. 123:2001;3412-3417.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3412-3417
    • Tschirret-Guth, R.A.1    Koo, L.S.2    Hoa, G.H.3    Ortiz De Montellano, P.R.4
  • 24
    • 0035100923 scopus 로고    scopus 로고
    • Understanding thermostability in cytochrome P450 by combinatorial mutagenesis
    • Maves S.A., Sligar S.G. Understanding thermostability in cytochrome P450 by combinatorial mutagenesis. Protein Sci. 10:2001;161-168.
    • (2001) Protein Sci. , vol.10 , pp. 161-168
    • Maves, S.A.1    Sligar, S.G.2
  • 25
    • 0037223885 scopus 로고    scopus 로고
    • Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus
    • Puchkaev A.V., Koo L.S., Ortiz de Montellano P.R. Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus. Arch. Biochem. Biophys. 409:2003;52-58.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 52-58
    • Puchkaev, A.V.1    Koo, L.S.2    Ortiz de Montellano, P.R.3
  • 26
    • 0037145075 scopus 로고    scopus 로고
    • Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High-resolution structure and functional properties
    • Park S.Y., Yamane K., Adachi S., Shiro Y., Weiss K.E., Maves S.A., Sligar S.G. Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high-resolution structure and functional properties. J. Inorg. Biochem. 91:2002;491-501.
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 491-501
    • Park, S.Y.1    Yamane, K.2    Adachi, S.3    Shiro, Y.4    Weiss, K.E.5    Maves, S.A.6    Sligar, S.G.7
  • 27
    • 0030781508 scopus 로고    scopus 로고
    • Extreme heat- and pressure-resistant 7-kDa protein P2 from the archaeon Sulfolobus solfataricus is dramatically destabilized by a single-point amino acid substitution
    • Fusi P., Goossens K., Consonni R., Grisa M., Puricelli P., Vecchio G., Vanoni M., Zetta L., Heremans K., Tortora P. Extreme heat- and pressure-resistant 7-kDa protein P2 from the archaeon Sulfolobus solfataricus is dramatically destabilized by a single-point amino acid substitution. Proteins. 29:1997;381-390.
    • (1997) Proteins , vol.29 , pp. 381-390
    • Fusi, P.1    Goossens, K.2    Consonni, R.3    Grisa, M.4    Puricelli, P.5    Vecchio, G.6    Vanoni, M.7    Zetta, L.8    Heremans, K.9    Tortora, P.10
  • 28
    • 0035960641 scopus 로고    scopus 로고
    • Thermodynamic differences among homologous thermophilic and mesophilic proteins
    • Kumar S., Tsai C.J., Nussinov R. Thermodynamic differences among homologous thermophilic and mesophilic proteins. Biochemistry. 40:2001;14152-14165.
    • (2001) Biochemistry , vol.40 , pp. 14152-14165
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 29
    • 0035876479 scopus 로고    scopus 로고
    • Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria
    • Fukuchi S., Nishikawa K. Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. J. Mol. Biol. 309:2001;835-843.
    • (2001) J. Mol. Biol. , vol.309 , pp. 835-843
    • Fukuchi, S.1    Nishikawa, K.2
  • 30
    • 0037236096 scopus 로고    scopus 로고
    • Structural plasticity of thermophilic serine hydroxymethyltransferases
    • Paiardini A., Gianese G., Bossa F., Pascarella S. Structural plasticity of thermophilic serine hydroxymethyltransferases. Proteins. 50:2003;122-134.
    • (2003) Proteins , vol.50 , pp. 122-134
    • Paiardini, A.1    Gianese, G.2    Bossa, F.3    Pascarella, S.4
  • 31
    • 0035259956 scopus 로고    scopus 로고
    • Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus
    • Tamakoshi M., Nakano Y., Kakizawa S., Yamagishi A., Oshima T. Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus. Extremophiles. 5:2001;17-22.
    • (2001) Extremophiles , vol.5 , pp. 17-22
    • Tamakoshi, M.1    Nakano, Y.2    Kakizawa, S.3    Yamagishi, A.4    Oshima, T.5
  • 32
    • 0036699655 scopus 로고    scopus 로고
    • Improvement of oxidative and thermostability of N-carbamyl-D-amino acid amidohydrolase by directed evolution
    • Oh K.H., Nam S.H., Kim H.S. Improvement of oxidative and thermostability of N-carbamyl-D-amino acid amidohydrolase by directed evolution. Protein Eng. 15:2002;689-695.
    • (2002) Protein Eng. , vol.15 , pp. 689-695
    • Oh, K.H.1    Nam, S.H.2    Kim, H.S.3
  • 33
    • 0035988011 scopus 로고    scopus 로고
    • Directed evolution of N-carbamyl-D-amino acid amidohydrolase for simultaneous improvement of oxidative and thermal stability
    • Oh K.H., Nam S.H., Kim H.S. Directed evolution of N-carbamyl-D-amino acid amidohydrolase for simultaneous improvement of oxidative and thermal stability. Biotechnol. Prog. 18:2002;413-417.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 413-417
    • Oh, K.H.1    Nam, S.H.2    Kim, H.S.3
  • 34
    • 0036372478 scopus 로고    scopus 로고
    • Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD
    • Murashima K., Kosugi A., Doi R.H. Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD. Mol. Microbiol. 45:2002;617-626.
    • (2002) Mol. Microbiol. , vol.45 , pp. 617-626
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 35
    • 0036303387 scopus 로고    scopus 로고
    • Increasing the thermal stability of an oligomeric protein, β-glucuronidase
    • Flores H., Ellington A.D., Murashima K., Kosugi A., Doi R.H. Increasing the thermal stability of an oligomeric protein, β-glucuronidase. J. Mol. Biol. 315:2002;325-337.
    • (2002) J. Mol. Biol. , vol.315 , pp. 325-337
    • Flores, H.1    Ellington, A.D.2    Murashima, K.3    Kosugi, A.4    Doi, R.H.5
  • 36
  • 37
    • 0035914470 scopus 로고    scopus 로고
    • Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability
    • Delbruck H., Mueller U., Perl D., Schmid F.X., Heinemann U. Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability. J. Mol. Biol. 313:2001;359-369.
    • (2001) J. Mol. Biol. , vol.313 , pp. 359-369
    • Delbruck, H.1    Mueller, U.2    Perl, D.3    Schmid, F.X.4    Heinemann, U.5
  • 38
    • 0034790185 scopus 로고    scopus 로고
    • New insights into the thermostability of bacterial ferredoxins: High-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus
    • Macedo-Ribeiro S., Martins B.M., Pereira P.J., Buse G., Huber R., Soulimane T. New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus. J. Biol. Inorg. Chem. 6:2001;663-674.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 663-674
    • Macedo-Ribeiro, S.1    Martins, B.M.2    Pereira, P.J.3    Buse, G.4    Huber, R.5    Soulimane, T.6
  • 39
    • 0035830969 scopus 로고    scopus 로고
    • X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 Å resolution: Determinants of thermostability revealed from structural comparisons
    • Zhang X., Meining W., Fischer M., Bacher A., Ladenstein R. X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6. Å resolution: determinants of thermostability revealed from structural comparisons J. Mol. Biol. 306:2001;1099-1114.
    • (2001) J. Mol. Biol. , vol.306 , pp. 1099-1114
    • Zhang, X.1    Meining, W.2    Fischer, M.3    Bacher, A.4    Ladenstein, R.5
  • 42
    • 0036643503 scopus 로고    scopus 로고
    • Ionic network at the C-terminus of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization
    • Cobucci-Ponzano B., Moracci M., Di Lauro B., Ciaramella M., D'Avino R., Rossi M. Ionic network at the C-terminus of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: functional role in the quaternary structure thermal stabilization. Proteins. 48:2002;98-106.
    • (2002) Proteins , vol.48 , pp. 98-106
    • Cobucci-Ponzano, B.1    Moracci, M.2    Di Lauro, B.3    Ciaramella, M.4    D'Avino, R.5    Rossi, M.6
  • 43
    • 0037207103 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on a salt-bridge triad in the NADP-binding domain of glutamate dehydrogenase from Thermotoga maritima: Cooperativity and electrostatic contribution to stability
    • Lebbink J.H., Consalvi V., Chiaraluce R., Berndt K.D., Ladenstein R. Structural and thermodynamic studies on a salt-bridge triad in the NADP-binding domain of glutamate dehydrogenase from Thermotoga maritima: cooperativity and electrostatic contribution to stability. Biochemistry. 41:2002;15524-15535.
    • (2002) Biochemistry , vol.41 , pp. 15524-15535
    • Lebbink, J.H.1    Consalvi, V.2    Chiaraluce, R.3    Berndt, K.D.4    Ladenstein, R.5
  • 44
    • 0036838706 scopus 로고    scopus 로고
    • Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: Contribution of salt bridging
    • Bogin O., Levin I., Hacham Y., Tel-Or S., Peretz M., Frolow F., Burstein Y. Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging. Protein Sci. 11:2002;2561-2574.
    • (2002) Protein Sci. , vol.11 , pp. 2561-2574
    • Bogin, O.1    Levin, I.2    Hacham, Y.3    Tel-Or, S.4    Peretz, M.5    Frolow, F.6    Burstein, Y.7
  • 46
    • 0037423708 scopus 로고    scopus 로고
    • Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: Thermostability and 1.8 Å resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate
    • Van Boxstael S., Cunin R., Khan S., Maes D. Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8. Å resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate J. Mol. Biol. 326:2003;203-216.
    • (2003) J. Mol. Biol. , vol.326 , pp. 203-216
    • Van Boxstael, S.1    Cunin, R.2    Khan, S.3    Maes, D.4
  • 47
    • 0037474542 scopus 로고    scopus 로고
    • Structure-based hyperthermostability of archaeal histone HPhA from Pyrococcus horikoshii
    • Li T., Sun F., Ji X., Feng Y., Rao Z. Structure-based hyperthermostability of archaeal histone HPhA from Pyrococcus horikoshii. J. Mol. Biol. 325:2003;1031-1037.
    • (2003) J. Mol. Biol. , vol.325 , pp. 1031-1037
    • Li, T.1    Sun, F.2    Ji, X.3    Feng, Y.4    Rao, Z.5
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 49
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., David J. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    David, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.