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Volumn 412, Issue 2, 2011, Pages 212-225

Phylogeny-based design of a B-subunit of DNA gyrase and its ATPase domain using a small set of homologous amino acid sequences

Author keywords

ATP hydrolysis; consensus design; DNA gyrase; phylogenetic tree; temperature induced unfolding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA TOPOISOMERASE; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE VI; UNCLASSIFIED DRUG;

EID: 80052024237     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.042     Document Type: Article
Times cited : (25)

References (63)
  • 1
    • 0020694602 scopus 로고
    • Protein engineering
    • Ulmer K.M. Protein engineering Science 219 1983 666 671
    • (1983) Science , vol.219 , pp. 666-671
    • Ulmer, K.M.1
  • 3
    • 0031686238 scopus 로고    scopus 로고
    • Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study
    • Facchiano A.M., Colonna G., and Ragone R. Helix stabilizing factors and stabilization of thermophilic proteins, an X-ray based study Protein Eng. 11 1998 753 760 (Pubitemid 28434484)
    • (1998) Protein Engineering , vol.11 , Issue.9 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 4
    • 0030781507 scopus 로고    scopus 로고
    • Insights into thermal resistance of proteins from the intrinsic stability of their α-helices
    • DOI 10.1002/(SICI)1097-0134(199711)29:3<309::AID-PROT5>3.0.CO;2-5
    • Petukhov M., Kil Y., Kuramitsu S., and Lanzov V. Insights into thermal resistance of proteins from the intrinsic stability of their α-helices Proteins 29 1997 309 320 (Pubitemid 27484222)
    • (1997) Proteins: Structure, Function and Genetics , vol.29 , Issue.3 , pp. 309-320
    • Petukhov, M.1    Kil, Y.2    Kuramitsu, S.3    Lanzov, V.4
  • 5
    • 41149102801 scopus 로고    scopus 로고
    • Hydrophobic effect on the stability and folding of a hyperthermophilic protein
    • Dong H., Mukaiyama A., Tadokoro T., Koga Y., Takano K., and Kanaya S. Hydrophobic effect on the stability and folding of a hyperthermophilic protein J. Mol. Biol. 378 2008 264 272
    • (2008) J. Mol. Biol. , vol.378 , pp. 264-272
    • Dong, H.1    Mukaiyama, A.2    Tadokoro, T.3    Koga, Y.4    Takano, K.5    Kanaya, S.6
  • 6
    • 1542267781 scopus 로고    scopus 로고
    • Thermodynamics of Core Hydrophobicity and Packing in the Hyperthermophile Proteins Sac7d and Sso7d
    • DOI 10.1021/bi0358263
    • Clark A.T., McCrary B.S., Edmondson S.P., and Shriver J.W. Thermodynamics of core hydrophobicity and packing in the hyperthermophile proteins Sac7d and Sso7d Biochemistry 43 2004 2840 2853 (Pubitemid 38327815)
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2840-2853
    • Clark, A.T.1    McCrary, B.S.2    Edmondson, S.P.3    Shriver, J.W.4
  • 8
    • 0041821240 scopus 로고    scopus 로고
    • High-resolution X-ray structure of the DMA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability
    • DOI 10.1007/s00792-002-0302-7
    • Christodoulou E., Rypniewski W.R., and Vorgias C.R. High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability Extremophiles 7 2003 111 122 (Pubitemid 40924480)
    • (2003) Extremophiles , vol.7 , Issue.2 , pp. 111-122
    • Christodoulou, E.1    Rypniewski, W.R.2    Vorgias, C.E.3
  • 9
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • DOI 10.1128/MMBR.65.1.1-43.2001
    • Vieille C., and Zeikus G.J. Hyperthermophilic enzymes, sources, uses, and molecular mechanisms for thermostability Microbiol. Mol. Biol. Rev. 65 2001 1 43 (Pubitemid 32204286)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 11
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • DOI 10.1016/S0959-440X(98)80094-8
    • Jaenicke R., and Bohm G. The stability of proteins in extreme environments Curr. Opin. Struct. Biol. 8 1998 738 748 (Pubitemid 29004672)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.6 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 12
    • 15444372698 scopus 로고    scopus 로고
    • Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii - Structural insights into enzymatic catalysis, thermostability, and dimerization
    • DOI 10.1021/bi047832k
    • Cheung Y.Y., Lam S.Y., Chu W.K., Allen M.D., Bycroft M., and Wong K.B. Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii - structural insights into enzymatic catalysis, thermostability, and dimerization Biochemistry 44 2005 4601 4611 (Pubitemid 40396739)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4601-4611
    • Cheung, Y.-Y.1    Lam, S.Y.2    Chu, W.-K.3    Allen, M.D.4    Bycroft, M.5    Wong, K.-B.6
  • 13
    • 0034623981 scopus 로고    scopus 로고
    • Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic archaea, thermoplasma acidophilum and pyrococcus furiosus
    • DOI 10.1006/jmbi.2000.4240
    • Arnott M.A., Michael R.A., Thompson C.R., Hough D.W., and Danson M.J. Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic archaea, Thermoplasma acidophilum and Pyrococcus furiosus J. Mol. Biol. 304 2000 657 668 (Pubitemid 32006197)
    • (2000) Journal of Molecular Biology , vol.304 , Issue.4 , pp. 657-668
    • Arnott, M.A.1    Michael, R.A.2    Thompson, C.R.3    Hough, D.W.4    Danson, M.J.5
  • 15
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino H., Aoki M., Aoshima M., Hayashi Y., Ohba M., and Yamagishi A. Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus Eur. J. Biochem. 220 1994 275 281 (Pubitemid 24067578)
    • (1994) European Journal of Biochemistry , vol.220 , Issue.1 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 18
    • 0035252648 scopus 로고    scopus 로고
    • How enzymes adapt: Lessons from directed evolution
    • DOI 10.1016/S0968-0004(00)01755-2, PII S0968000400017552
    • Arnold F.H., Wintrode P.L., Miyazaki K., and Gershenson A. How enzymes adapt, lessons from directed evolution Trends Biochem. Sci. 26 2001 100 106 (Pubitemid 32144744)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.2 , pp. 100-106
    • Arnold, F.H.1    Wintrode, P.L.2    Miyazaki, K.3    Gershenson, A.4
  • 19
    • 34248562516 scopus 로고    scopus 로고
    • Extremely Thermophilic Translation System in the Common Ancestor Commonote: Ancestral Mutants of Glycyl-tRNA Synthetase from the Extreme Thermophile Thermus thermophilus
    • DOI 10.1016/j.jmb.2007.04.001, PII S0022283607004548
    • Shimizu H., Yokobori S., Ohkuri T., Yokogawa T., Nishikawa K., and Yamagishi A. Extremely thermophilic translation system in the common ancestor commonote, ancestral mutants of glycyl-tRNA synthetase from the extreme thermophile Thermus thermophilus J. Mol. Biol. 369 2007 1060 1069 (Pubitemid 46754068)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.4 , pp. 1060-1069
    • Shimizu, H.1    Yokobori, S.-i.2    Ohkuri, T.3    Yokogawa, T.4    Nishikawa, K.5    Yamagishi, A.6
  • 20
    • 29144522906 scopus 로고    scopus 로고
    • Designing thermostable proteins: Ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree
    • DOI 10.1016/j.jmb.2005.10.011, PII S0022283605012416
    • Watanabe K., Ohkuri T., Yokobori S., and Yamagishi A. Designing thermostable proteins, ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree J. Mol. Biol. 355 2006 664 674 (Pubitemid 41817627)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 664-674
    • Watanabe, K.1    Ohkuri, T.2    Yokobori, S.-I.3    Yamagishi, A.4
  • 21
    • 15944381217 scopus 로고    scopus 로고
    • Thermostability of ancestral mutants of Caldococcus noboribetus isocitrate dehydrogenase
    • DOI 10.1016/j.femsle.2004.12.030
    • Iwabata H., Watanabe K., Ohkuri T., Yokobori S., and Yamagishi A. Thermostability of ancestral mutants of Caldococcus noboribetus isocitrate dehydrogenase FEMS Microbiol. Lett. 243 2005 393 398 (Pubitemid 40431205)
    • (2005) FEMS Microbiology Letters , vol.243 , Issue.2 , pp. 393-398
    • Iwabata, H.1    Watanabe, K.2    Ohkuri, T.3    Yokobori, S.-I.4    Yamagishi, A.5
  • 22
    • 0034986432 scopus 로고    scopus 로고
    • Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile: Experimental evidence supporting the thermophilic common ancestor hypothesis
    • Miyazaki J., Nakaya S., Suzuki T., Tamakoshi M., Oshima T., and Yamagishi A. Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile, experimental evidence supporting the thermophilic common ancestor hypothesis J. Biochem. 129 2001 777 782 (Pubitemid 32499791)
    • (2001) Journal of Biochemistry , vol.129 , Issue.5 , pp. 777-782
    • Miyazaki, J.1    Nakaya, S.2    Suzuki, T.3    Tamakoshi, M.4    Oshima, T.5    Yamagishi, A.6
  • 23
    • 77955959569 scopus 로고    scopus 로고
    • Improvement of Bacillus circulans β-amylase activity attained using the ancestral mutation method
    • Yamashiro K., Yokobori S., Koikeda S., and Yamagishi A. Improvement of Bacillus circulans β-amylase activity attained using the ancestral mutation method Protein Eng. Des. Sel. 23 2010 519 528
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 519-528
    • Yamashiro, K.1    Yokobori, S.2    Koikeda, S.3    Yamagishi, A.4
  • 24
    • 1942531303 scopus 로고    scopus 로고
    • Resurrecting ancient genes: Experimental analysis of extinct molecules
    • DOI 10.1038/nrg1324
    • Thornton J.W. Resurrecting ancient genes, experimental analysis of extinct molecules Nat. Rev. Genet. 5 2004 366 375 (Pubitemid 38529408)
    • (2004) Nature Reviews Genetics , vol.5 , Issue.5 , pp. 366-375
    • Thornton, J.W.1
  • 26
    • 34548040966 scopus 로고    scopus 로고
    • Crystal structure of an ancient protein: Evolution by conformational epistasis
    • DOI 10.1126/science.1142819
    • Ortlund E.A., Bridgham J.T., Redinbo M.R., and Thornton J.W. Crystal structure of an ancient protein, evolution by conformational epistasis Science 317 2007 1544 1548 (Pubitemid 47417432)
    • (2007) Science , vol.317 , Issue.5844 , pp. 1544-1548
    • Ortlund, E.A.1    Bridgham, J.T.2    Redinbo, M.R.3    Thornton, J.W.4
  • 27
    • 33645691679 scopus 로고    scopus 로고
    • Evolution of hormone-receptor complexity by molecular exploitation
    • Bridgham J.T., Carroll S.M., and Thornton J.W. Evolution of hormone-receptor complexity by molecular exploitation Science 312 2006 97 101
    • (2006) Science , vol.312 , pp. 97-101
    • Bridgham, J.T.1    Carroll, S.M.2    Thornton, J.W.3
  • 29
    • 38949093003 scopus 로고    scopus 로고
    • Palaeotemperature trend for Precambrian life inferred from resurrected proteins
    • DOI 10.1038/nature06510, PII NATURE06510
    • Gaucher E.A., Govindarajan S., and Ganesh O.K. Palaeotemperature trend for Precambrian life inferred from resurrected proteins Nature 451 2008 704 707 (Pubitemid 351220563)
    • (2008) Nature , vol.451 , Issue.7179 , pp. 704-707
    • Gaucher, E.A.1    Govindarajan, S.2    Ganesh, O.K.3
  • 30
    • 0141828152 scopus 로고    scopus 로고
    • Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins
    • DOI 10.1038/nature01977
    • Gaucher E.A., Thomson J.M., Burgan M.F., and Benner S.A. Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins Nature 425 2003 285 288 (Pubitemid 37158402)
    • (2003) Nature , vol.425 , Issue.6955 , pp. 285-288
    • Gaucher, E.A.1    Thomson, J.M.2    Burgan, M.F.3    Benner, S.A.4
  • 31
    • 33644859575 scopus 로고    scopus 로고
    • Three RNA cells for ribosomal lineages and three DNA viruses to replicate their genomes: A hypothesis for the origin of cellular domain
    • DOI 10.1073/pnas.0510333103
    • Forterre P. Three RNA cells for ribosomal lineages and three DNA viruses to replicate their genomes: a hypothesis for the origin of cellular domain Proc. Natl Acad. Sci. USA 103 2006 3669 3674 (Pubitemid 43376613)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.10 , pp. 3669-3674
    • Forterre, P.1
  • 33
    • 0022988840 scopus 로고
    • Mechanistic aspects of DNA topoisomerases
    • Maxwell A., and Gellert M. Mechanistic aspects of DNA topoisomerases Adv. Protein Chem. 38 1986 69 107
    • (1986) Adv. Protein Chem. , vol.38 , pp. 69-107
    • Maxwell, A.1    Gellert, M.2
  • 34
    • 0034737716 scopus 로고    scopus 로고
    • Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center
    • DOI 10.1074/jbc.275.13.9468
    • Brino L., Urzhumtsev A., Mousli M., Bronner C., Mitschler A., Oudet P., and Moras D. Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center J. Biol. Chem. 275 2000 9468 9475 (Pubitemid 30185175)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9468-9475
    • Brino, L.1    Urzhumtsev, A.2    Mousli, M.3    Bronner, C.4    Mitschler, A.5    Oudet, P.6    Moras, D.7
  • 35
    • 0029166885 scopus 로고
    • Nucleotide binding to the 43-kilodalton N-terminal fragment of the DNA gyrase B protein
    • Ali J.A., Orphanides G., and Maxwell A. Nucleotide binding to the 43-kilodalton N-terminal fragment of the DNA gyrase B protein Biochemistry 34 1995 9801 9808
    • (1995) Biochemistry , vol.34 , pp. 9801-9808
    • Ali, J.A.1    Orphanides, G.2    Maxwell, A.3
  • 37
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt H.A., Strimmer K., Vingron M., and von Haeseler A. TREE-PUZZLE, maximum likelihood phylogenetic analysis using quartets and parallel computing Bioinformatics 18 2002 502 504 (Pubitemid 34284960)
    • (2002) Bioinformatics , vol.18 , Issue.3 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 39
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang Z. PAML, a program package for phylogenetic analysis by maximum likelihood Comput. Appl. Biosci. 13 1997 555 556 (Pubitemid 27480216)
    • (1997) Computer Applications in the Biosciences , vol.13 , Issue.5 , pp. 555-556
    • Yang, Z.1
  • 40
    • 0028820333 scopus 로고
    • A new method of inference of ancestral nucleotide and amino acid sequences
    • Yang Z., Kumar S., and Nei M. A new method of inference of ancestral nucleotide and amino acid sequences Genetics 141 1995 1641 1650
    • (1995) Genetics , vol.141 , pp. 1641-1650
    • Yang, Z.1    Kumar, S.2    Nei, M.3
  • 41
    • 78650653937 scopus 로고    scopus 로고
    • A naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogs
    • Tretter E.M., Lerman J.C., and Berger J.M. A naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogs Proc. Natl Acad. Sci. USA 107 2010 22055 22059
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 22055-22059
    • Tretter, E.M.1    Lerman, J.C.2    Berger, J.M.3
  • 42
    • 34247496263 scopus 로고    scopus 로고
    • Origin and evolution of DNA topoisomerases
    • DOI 10.1016/j.biochi.2006.12.009, PII S0300908407000041, DNA Topology DNA, more than just a ladder: A tribute to Michel Duguet
    • Forterre P., Gribaldo S., Gadelle D., and Serre M.C. Origin and evolution of DNA topoisomerases Biochimie 89 2007 427 446 (Pubitemid 46656307)
    • (2007) Biochimie , vol.89 , Issue.4 , pp. 427-446
    • Forterre, P.1    Gribaldo, S.2    Gadelle, D.3    Serre, M.-C.4
  • 43
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface, flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL-X windows interface, flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 44
    • 27144482726 scopus 로고    scopus 로고
    • The effects of metal ions on the structure and stability of the DNA gyrase B protein
    • DOI 10.1016/j.jmb.2005.09.043, PII S0022283605011095
    • Sissi C., Marangon E., Chemello A., Noble C.G., Maxwell A., and Palumbo M. The effects of metal ions on the structure and stability of the DNA gyrase B protein J. Mol. Biol. 353 2005 1152 1160 (Pubitemid 41503279)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.5 , pp. 1152-1160
    • Sissi, C.1    Marangon, E.2    Chemello, A.3    Noble, C.G.4    Maxwell, A.5    Palumbo, M.6
  • 45
    • 78649879246 scopus 로고    scopus 로고
    • A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function
    • Schoeffler A.J., May A.P., and Berger J.M. A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function Nucleic Acids Res. 38 2010 7830 7844
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7830-7844
    • Schoeffler, A.J.1    May, A.P.2    Berger, J.M.3
  • 46
    • 0037166285 scopus 로고    scopus 로고
    • An open conformation of the Thermus thermophilus gyrase B ATP-binding domain
    • DOI 10.1074/jbc.M111740200
    • Lamour V., Hoermann L., Jeltsch J.M., Oudet P., and Moras D. An open conformation of the Thermus thermophilus gyrase B ATP-binding domain J. Biol. Chem. 277 2002 18947 18953 (Pubitemid 34952456)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18947-18953
    • Lamour, V.1    Hoermann, L.2    Jeltsch, J.-M.3    Oudet, P.4    Moras, D.5
  • 47
    • 0027419771 scopus 로고
    • The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs
    • Ali J.A., Jackson A.P., Howells A.J., and Maxwell A. The 43 kDa N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs Biochemistry 32 1993 2717 2724 (Pubitemid 23090662)
    • (1993) Biochemistry , vol.32 , Issue.10 , pp. 2717-2724
    • Ali, J.A.1    Jackson, A.P.2    Howells, A.J.3    Maxwell, A.4
  • 48
    • 0032493388 scopus 로고    scopus 로고
    • Identification of a residue involved in transition-state stabilization in the ATPase reaction of DNA gyrase
    • DOI 10.1021/bi9801309
    • Smith C.V., and Maxwell A. Identification of a residue involved in transition-state stabilization in the ATPase reaction of DNA gyrase Biochemistry 37 1998 9658 9667 (Pubitemid 28319610)
    • (1998) Biochemistry , vol.37 , Issue.27 , pp. 9658-9667
    • Smith, C.V.1    Maxwell, A.2
  • 49
    • 0028111743 scopus 로고
    • Sequence statistics reliably predict stabilizing mutations in a protein domain
    • DOI 10.1006/jmbi.1994.1434
    • Steipe B., Schiller B., Pluckthun A., and Steinbacher S. Sequence statistics reliably predict stabilizing mutations in a protein domain J. Mol. Biol. 240 1994 188 192 (Pubitemid 24238735)
    • (1994) Journal of Molecular Biology , vol.240 , Issue.3 , pp. 188-192
    • Steipe, B.1    Schiller, B.2    Pluckthun, A.3    Steinbacher, S.4
  • 51
    • 33748101201 scopus 로고    scopus 로고
    • Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output
    • DOI 10.1093/protein/gzl023
    • Loening A.M., Fenn T.D., Wu A.M., and Gambhir S.S. Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output Protein Eng. Des. Sel. 19 2006 391 400 (Pubitemid 44306057)
    • (2006) Protein Engineering, Design and Selection , vol.19 , Issue.9 , pp. 391-400
    • Loening, A.M.1    Fenn, T.D.2    Wu, A.M.3    Gambhir, S.S.4
  • 52
    • 0034495088 scopus 로고    scopus 로고
    • The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis
    • Rath A., and Davidson A.R. The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis Protein Sci. 9 2000 2457 2469 (Pubitemid 32105728)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2457-2469
    • Rath, A.1    Davidson, A.R.2
  • 54
    • 0033963277 scopus 로고    scopus 로고
    • From DNA sequence to improved functionality: Using protein sequence comparisons to rapidly design a thermostable consensus phytase
    • Lehmann M., Kostrewa D., Wyss M., Brugger R., D'Arcy A., Pasamontes L., and van Loon A.P. From DNA sequence to improved functionality, using protein sequence comparisons to rapidly design a thermostable consensus phytase Protein Eng. 13 2000 49 57 (Pubitemid 30105578)
    • (2000) Protein Engineering , vol.13 , Issue.1 , pp. 49-57
    • Lehmann, M.1    Kostrewa, D.2    Wyss, M.3    Brugger, R.4    D'Arcy, A.5    Pasamontes, L.6    Van Loon, A.P.G.M.7
  • 56
    • 66249122803 scopus 로고    scopus 로고
    • Inferring stabilizing mutations from protein phylogenies: Application to influenza hemagglutinin
    • Bloom J.D., and Glassman M.J. Inferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin PLoS Comput. Biol. 5 2009 e1000349
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000349
    • Bloom, J.D.1    Glassman, M.J.2
  • 57
    • 0031022599 scopus 로고    scopus 로고
    • β-Turn propensities as paradigms for the analysis of structural motifs to engineer protein stability
    • Ohage E.C., Graml W., Walter M.M., Steinbacher S., and Steipe B. Beta-turn propensities as paradigms for the analysis of structural motifs to engineer protein stability Protein Sci. 6 1997 233 241 (Pubitemid 27045261)
    • (1997) Protein Science , vol.6 , Issue.1 , pp. 233-241
    • Ohage, E.C.1    Graml, W.2    Walter, M.M.3    Steinbacher, S.4    Steipe, B.5
  • 58
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 4 1987 406 425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 59
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis Mol. Biol. Evol. 17 2000 540 552 (Pubitemid 30210700)
    • (2000) Molecular Biology and Evolution , vol.17 , Issue.4 , pp. 540-552
    • Castresana, J.1
  • 60
    • 13244278007 scopus 로고    scopus 로고
    • GASP, Gapped Ancestral Sequence Prediction for proteins
    • Edwards R.J., and Shields D.C. GASP, Gapped Ancestral Sequence Prediction for proteins BMC Bioinf. 5 2004 123
    • (2004) BMC Bioinf. , vol.5 , pp. 123
    • Edwards, R.J.1    Shields, D.C.2
  • 62
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 63
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2


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