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Volumn 149, Issue 1, 1998, Pages 445-458

Assessing the impact of secondary structure and solvent accessibility on protein evolution

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; AMINO ACID; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; GLUTAMATE DEHYDROGENASE; GLYCOPROTEIN GP 120; GUANINE NUCLEOTIDE BINDING PROTEIN; MATRIX PROTEIN; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PROTEIN; SOLVENT; SUCROSE SYNTHASE; SYNTHETASE; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0031805465     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (214)

References (51)
  • 2
    • 0027174134 scopus 로고
    • Prediction of protein secondary structure by the hidden Markov model
    • ASAI, K., S. HAYAMIZU and K. HANDA, 1993 Prediction of protein secondary structure by the hidden Markov model. CABIOS 9: 141-146.
    • (1993) CABIOS , vol.9 , pp. 141-146
    • Asai, K.1    Hayamizu, S.2    Handa, K.3
  • 3
    • 0028180367 scopus 로고
    • Bona fide prediction of aspects of protein conformation: Assigning interior and surface residues from patterns of variation and conservation in homologous sequences
    • BENNER, S. A., I. BADCOE, M. A. COHEN and D. L. GERLOFF, 1994 Bona fide prediction of aspects of protein conformation: assigning interior and surface residues from patterns of variation and conservation in homologous sequences. J. Mol. Biol. 235: 926-958.
    • (1994) J. Mol. Biol. , vol.235 , pp. 926-958
    • Benner, S.A.1    Badcoe, I.2    Cohen, M.A.3    Gerloff, D.L.4
  • 4
    • 0017751668 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • BERNSTEIN, F. C., T. F. KOETZLE, G. J. B. WILLIAMS, E. F. MEYER, M. D. BRICE et al., 1977 The protein data bank: a computer-based archival file for macromolecular structures. Eur. J. Biochem. 80: 319-324.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 319-324
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.B.3    Meyer, E.F.4    Brice, M.D.5
  • 5
    • 0025234646 scopus 로고
    • Construction of validated, non-redundant composite protein sequence databases
    • BLEASBY, A. J., and J. C. WOOTTON, 1990 Construction of validated, non-redundant composite protein sequence databases. Prot. Eng. 3: 153-159.
    • (1990) Prot. Eng. , vol.3 , pp. 153-159
    • Bleasby, A.J.1    Wootton, J.C.2
  • 7
    • 0029856518 scopus 로고    scopus 로고
    • Modelling residue usage in aligned protein sequences via maximum likelihood
    • BRUNO, W. J., 1996 Modelling residue usage in aligned protein sequences via maximum likelihood. Mol. Biol. Evol. 13: 1368-1374.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 1368-1374
    • Bruno, W.J.1
  • 8
    • 0028172520 scopus 로고
    • Phylogenetic relationships among eutherian orders estimated from inferred sequences of mitochondrial, proteins: Instability of a tree based on a single gene
    • CAO, Y., J. ADACHI, A. JANKE, S. PÄÄBO and M. HASEGAWA, 1994 Phylogenetic relationships among eutherian orders estimated from inferred sequences of mitochondrial, proteins: instability of a tree based on a single gene. J. Mol. Evol. 39: 519-527.
    • (1994) J. Mol. Evol. , vol.39 , pp. 519-527
    • Cao, Y.1    Adachi, J.2    Janke, A.3    Pääbo, S.4    Hasegawa, M.5
  • 9
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • CHOTHIA, C., and A. M. LESK, 1986 The relation between the divergence of sequence and structure in proteins. EMBO J. 5: 823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 10
    • 0024557590 scopus 로고
    • Stochastic models for heterogeneous DNA sequences
    • CHURCHILL, G. A., 1989 Stochastic models for heterogeneous DNA sequences. Bull. Math. Biol. 51: 79-94.
    • (1989) Bull. Math. Biol. , vol.51 , pp. 79-94
    • Churchill, G.A.1
  • 11
    • 0002929101 scopus 로고
    • A model of evolutionary change in proteins
    • edited by M. O. DAYHOFF. National Biomedical Research Foundation, Washington, DC
    • DAYHOFF, M. O., R. V. ECK and C. M. PARK, 1972 A model of evolutionary change in proteins, pp. 89-99 in Atlas of Protein Sequence and Structure, edited by M. O. DAYHOFF. National Biomedical Research Foundation, Washington, DC.
    • (1972) Atlas of Protein Sequence and Structure , pp. 89-99
    • Dayhoff, M.O.1    Eck, R.V.2    Park, C.M.3
  • 12
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • edited by M. O. DAYHOFF. National Biomedical Research Foundation, Washington, DC
    • DAYHOFF, M. O., R. M. SCHWARTZ and B. C. ORCUTT, 1978 A model of evolutionary change in proteins, pp. 345-352 in Atlas of Protein Sequence and Structure, edited by M. O. DAYHOFF. National Biomedical Research Foundation, Washington, DC.
    • (1978) Atlas of Protein Sequence and Structure , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 14
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: A maximum likelihood approach
    • FELSENSTEIN, J., 1981 Evolutionary trees from DNA sequences: a maximum likelihood approach. J. Mol. Evol. 17: 368-376.
    • (1981) J. Mol. Evol. , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 15
    • 0022203256 scopus 로고
    • Phylogenies and the comparative method
    • FELSENSTEIN, J., 1985 Phylogenies and the comparative method. Am. Nat. 125: 1-15.
    • (1985) Am. Nat. , vol.125 , pp. 1-15
    • Felsenstein, J.1
  • 17
    • 0030034795 scopus 로고    scopus 로고
    • A hidden Markov model approach to variation among sites in rate of evolution
    • FELSENSTEIN, J., and G. A. CHURCHILL, 1996 A hidden Markov model approach to variation among sites in rate of evolution. Mol. Biol. Evol. 13: 93-104.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 93-104
    • Felsenstein, J.1    Churchill, G.A.2
  • 18
    • 0029864622 scopus 로고    scopus 로고
    • A nuclear gene for higher-level phylogenetics-phosphoenolpy-ruvate carboxykinase tracks Mesozoic-age divergences within Lepidoptera (Insecta)
    • FRIEDLANDER, T. P., J. C. REGIER, C. MITTER and D. L. WAGNER, 1996 A nuclear gene for higher-level phylogenetics-phosphoenolpy-ruvate carboxykinase tracks Mesozoic-age divergences within Lepidoptera (Insecta). Mol. Biol. Evol. 13: 594-604.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 594-604
    • Friedlander, T.P.1    Regier, J.C.2    Mitter, C.3    Wagner, D.L.4
  • 19
    • 0027526039 scopus 로고
    • Statistical tests of models of DNA substitution
    • GOLDMAN, N., 1993 Statistical tests of models of DNA substitution. J. Mol. Evol. 36: 182-198.
    • (1993) J. Mol. Evol. , vol.36 , pp. 182-198
    • Goldman, N.1
  • 20
    • 0028168856 scopus 로고
    • A codon-based model of nucleotide substitution for protein-coding DNA sequences
    • GOLDMAN, N., and Z. YANG, 1994 A codon-based model of nucleotide substitution for protein-coding DNA sequences. Mol. Biol. Evol. 11: 725-736.
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 725-736
    • Goldman, N.1    Yang, Z.2
  • 21
    • 0030601801 scopus 로고    scopus 로고
    • Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses
    • GOLDMAN, N., J. L. THORNE and D. T. JONES, 1996 Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses. J. Mol. Biol. 263: 196-208.
    • (1996) J. Mol. Biol. , vol.263 , pp. 196-208
    • Goldman, N.1    Thorne, J.L.2    Jones, D.T.3
  • 22
    • 0020484488 scopus 로고
    • An improved algorithm for matching biological sequences
    • GOTOH, O., 1982 An improved algorithm for matching biological sequences. J. Mol. Biol. 162: 705-708.
    • (1982) J. Mol. Biol. , vol.162 , pp. 705-708
    • Gotoh, O.1
  • 25
    • 0022376704 scopus 로고
    • Dating of the human-ape splitting by a molecular clock of mitochondrial DNA
    • HASEGAWA, M., H. KISHINO and T. A. YANO, 1985 Dating of the human-ape splitting by a molecular clock of mitochondrial DNA. J. Mol. Evol. 22: 160-174.
    • (1985) J. Mol. Evol. , vol.22 , pp. 160-174
    • Hasegawa, M.1    Kishino, H.2    Yano, T.A.3
  • 26
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • JONES, D. T., W. R. TAVLOR and J. M. THORNTON, 1992 The rapid generation of mutation data matrices from protein sequences. CABIOS 8: 275-282.
    • (1992) CABIOS , vol.8 , pp. 275-282
    • Jones, D.T.1    Tavlor, W.R.2    Thornton, J.M.3
  • 27
    • 0028153788 scopus 로고
    • A mutation data matrix for transmembrane proteins
    • JONES, D. T., W. R. TAYLOR and J. M. THORNTON, 1994 A mutation data matrix for transmembrane proteins. FEBS Letts. 339: 269-275.
    • (1994) FEBS Letts. , vol.339 , pp. 269-275
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 28
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • edited by H. N. MUNRO. Academic Press, New York
    • JUKES, T. H., and C. R. CANTOR, 1969 Evolution of protein molecules, pp. 21-132 in Mammalian Protein Metabolism, edited by H. N. MUNRO. Academic Press, New York.
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • KABSCH, W., and C. SANDER, 1983 Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 31
    • 0028808763 scopus 로고
    • Context-dependent optimal substitution matrices
    • KOSHI, J. M., and R. A. GOLDSTEIN, 1995 Context-dependent optimal substitution matrices. Prot. Eng. 8: 641-645.
    • (1995) Prot. Eng. , vol.8 , pp. 641-645
    • Koshi, J.M.1    Goldstein, R.A.2
  • 32
    • 0025997601 scopus 로고
    • Secondary structure-based profiles: Use of structure-conserving scoring tables in searching protein sequence databases for structural similarities
    • LÜTHY, R., A. D. MCLACHLAN and D. EISENBERG, 1991 Secondary structure-based profiles: use of structure-conserving scoring tables in searching protein sequence databases for structural similarities. Proteins 10: 229-239.
    • (1991) Proteins , vol.10 , pp. 229-239
    • Lüthy, R.1    Mclachlan, A.D.2    Eisenberg, D.3
  • 33
    • 0030762484 scopus 로고    scopus 로고
    • Structural biology and phylogeny estimation
    • NAYLOR, G. J. P., and W. M. BROWN, 1997 Structural biology and phylogeny estimation. Nature 388: 527-528.
    • (1997) Nature , vol.388 , pp. 527-528
    • Naylor, G.J.P.1    Brown, W.M.2
  • 34
    • 0025104478 scopus 로고
    • Tertiary structural constraints on protein evolutionary diversity: Templates, key residues and structure prediction
    • OVERINGTON, J., M. S. JOHNSON, A. ŠALI and T. L. BLUNDELL, 1990 Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction. Proc. R. Soc. Lond. Ser B 241: 132-145.
    • (1990) Proc. R. Soc. Lond. Ser B , vol.241 , pp. 132-145
    • Overington, J.1    Johnson, M.S.2    Šali, A.3    Blundell, T.L.4
  • 36
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation
    • RUSSELL, R. B., M. A. S. SAQI, R. A. SAYLE, P. A. BATES and M. J. E. STERNBERG, 1997 Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation. J. Mol. Biol. 269: 423-439.
    • (1997) J. Mol. Biol. , vol.269 , pp. 423-439
    • Russell, R.B.1    Saqi, M.A.S.2    Sayle, R.A.3    Bates, P.A.4    Sternberg, M.J.E.5
  • 37
    • 0001336205 scopus 로고    scopus 로고
    • Phylogenetic inference
    • Ed. 2, edited by D. M. HILLIS, C. MORTTZ and B. K. MABLE. Sinauer Associates, Sunderland, MA
    • SWOFFORD, D. L., G. J. OLSEN, P. J. WADDELL and D. M. HILLIS, 1996 Phylogenetic inference, pp. 407-514 in Molecular Systematics, Ed. 2, edited by D. M. HILLIS, C. MORTTZ and B. K. MABLE. Sinauer Associates, Sunderland, MA.
    • (1996) Molecular Systematics , pp. 407-514
    • Swofford, D.L.1    Olsen, G.J.2    Waddell, P.J.3    Hillis, D.M.4
  • 38
    • 0024245156 scopus 로고
    • A flexible method to align large numbers of biological sequences
    • TAYLOR, W. R., 1988 A flexible method to align large numbers of biological sequences. J. Mol. Evol. 28: 161-169.
    • (1988) J. Mol. Evol. , vol.28 , pp. 161-169
    • Taylor, W.R.1
  • 39
    • 0028915547 scopus 로고
    • Correlation of intron-exon organisation with the three-dimensional structure in glutamate dehydrogenase
    • TELLER, J. K., P. J. BAKER, K. L. BRITTON, P. C. ENGEL, D. W. RICE at al., 1995 Correlation of intron-exon organisation with the three-dimensional structure in glutamate dehydrogenase. Biochim. Biophys. Acta 1247: 231-238.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 231-238
    • Teller, J.K.1    Baker, P.J.2    Britton, K.L.3    Engel, P.C.4    Rice, D.W.5
  • 40
    • 0029985399 scopus 로고    scopus 로고
    • Combining protein evolution and secondary structure
    • THORNE, J. L., N. GOLDMAN and D. T. JONES, 1996 Combining protein evolution and secondary structure. Mol. Biol. Evol. 13: 666-673.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 666-673
    • Thorne, J.L.1    Goldman, N.2    Jones, D.T.3
  • 41
    • 0027439391 scopus 로고
    • Fragment ranking in modelling of protein structure: Conformationally constrained substitution tables
    • TOPHAM, C. M., A. MCLEOD, F. EISENMENGER, J. P. OVERINGTON, M. S. JOHNSON et al, 1993 Fragment ranking in modelling of protein structure: conformationally constrained substitution tables. J. Mol. Biol. 229: 194-220.
    • (1993) J. Mol. Biol. , vol.229 , pp. 194-220
    • Topham, C.M.1    Mcleod, A.2    Eisenmenger, F.3    Overington, J.P.4    Johnson, M.S.5
  • 42
    • 0028239337 scopus 로고
    • Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classes
    • WAKO, H., and T. L. BLUNDELL, 1994 Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classes. J. Mol. Biol. 238: 682-692.
    • (1994) J. Mol. Biol. , vol.238 , pp. 682-692
    • Wako, H.1    Blundell, T.L.2
  • 43
    • 0028181528 scopus 로고
    • Protein classification by stochastic modeling and optimal filtering of amino-acid sequences
    • WHITE, J. V., C. M. STULTZ and T. F. SMITH, 1994 Protein classification by stochastic modeling and optimal filtering of amino-acid sequences. Math. Biosci. 119: 35-75.
    • (1994) Math. Biosci. , vol.119 , pp. 35-75
    • White, J.V.1    Stultz, C.M.2    Smith, T.F.3
  • 44
    • 0028064845 scopus 로고
    • Maximum likelihood phylogenetic estimation from DNA sequences with variable rates over sites: Approximate methods
    • YANG, Z., 1994 Maximum likelihood phylogenetic estimation from DNA sequences with variable rates over sites: approximate methods. J. Mol. Evol. 39: 306-314.
    • (1994) J. Mol. Evol. , vol.39 , pp. 306-314
    • Yang, Z.1
  • 45
    • 0028813337 scopus 로고
    • A space-time process model for the evolution of DNA sequences
    • YANG, Z., 1995 A space-time process model for the evolution of DNA sequences. Genetics 139: 993-1005.
    • (1995) Genetics , vol.139 , pp. 993-1005
    • Yang, Z.1
  • 46
    • 0030451420 scopus 로고    scopus 로고
    • Among-site rate variation and its impact on phylogenetic analysis
    • YANG, Z., 1996 Among-site rate variation and its impact on phylogenetic analysis. TREE 11: 367-372.
    • (1996) TREE , vol.11 , pp. 367-372
    • Yang, Z.1
  • 47
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • YANG, Z., 1997 PAML: a program package for phylogenetic analysis by maximum likelihood. CABIOS 13: 555-556.
    • (1997) CABIOS , vol.13 , pp. 555-556
    • Yang, Z.1
  • 48
    • 0028267146 scopus 로고
    • Comparison of models for nucleotide substitution used in maximum-likelihood phylogenetic estimation
    • YANG, Z., N. GOLDMAN and A. FRIDAY, 1994 Comparison of models for nucleotide substitution used in maximum-likelihood phylogenetic estimation. Mol. Biol. Evol. 11: 316-324.
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 316-324
    • Yang, Z.1    Goldman, N.2    Friday, A.3
  • 49
    • 0028805929 scopus 로고
    • Molecular evolution of the hepatitis B virus genome
    • YANG, Z., I. J. LAUDER and H. J. LIN, 1995 Molecular evolution of the hepatitis B virus genome. J. Mol. Evol. 41: 587-596.
    • (1995) J. Mol. Evol. , vol.41 , pp. 587-596
    • Yang, Z.1    Lauder, I.J.2    Lin, H.J.3
  • 50
    • 0026699257 scopus 로고
    • Phylogeny and evolutionary rates of G protein α subunit genes
    • YOKOYAMA, S., and W. T. STARMER, 1992 Phylogeny and evolutionary rates of G protein α subunit genes. J. Mol. Evol. 35: 230-238.
    • (1992) J. Mol. Evol. , vol.35 , pp. 230-238
    • Yokoyama, S.1    Starmer, W.T.2
  • 51
    • 0027428004 scopus 로고
    • Molecular phylogeny and evolutionary rates of alcohol dehydrogenases in vertebrates and plants
    • YOKOYAMA, S., and D. E. HARRY, 1993 Molecular phylogeny and evolutionary rates of alcohol dehydrogenases in vertebrates and plants. Mol. Biol. Evol. 10: 1215-1226.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 1215-1226
    • Yokoyama, S.1    Harry, D.E.2


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