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Volumn 31, Issue 15, 2003, Pages 4625-4631

Structural details (kinks and non-α conformations) in transmembrane helices are intrahelically determined and can be predicted by sequence pattern descriptors

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; POLYPEPTIDE; PROTEIN; MEMBRANE PROTEIN; RHODOPSIN;

EID: 0041660896     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg639     Document Type: Article
Times cited : (26)

References (22)
  • 1
    • 0014003909 scopus 로고
    • Role of amino-acid 'code' and selection for conformation in the evolution of proteins
    • Epstein,C.J. (1966) Role of amino-acid 'code' and selection for conformation in the evolution of proteins. Nature, 210, 25-28.
    • (1966) Nature , vol.210 , pp. 25-28
    • Epstein, C.J.1
  • 2
    • 0014214038 scopus 로고
    • Non-randomness of amino-acid changes in the evolution of homologous proteins
    • Epstein,C.J. (1967) Non-randomness of amino-acid changes in the evolution of homologous proteins. Nature, 215, 355-359.
    • (1967) Nature , vol.215 , pp. 355-359
    • Epstein, C.J.1
  • 3
    • 0027122748 scopus 로고
    • Proteins - 1000 families for the molecular biologist
    • Chothia,C. (1992) Proteins - 1000 families for the molecular biologist. Nature, 357, 543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 4
  • 5
    • 0023176681 scopus 로고
    • Determinants of a protein fold: Unique features of the globin amino acid sequences
    • Bashford,D., Chothia,C. and Lesk,A.M. (1987) Determinants of a protein fold: unique features of the globin amino acid sequences. J. Mol. Biol., 196, 199-216.
    • (1987) J. Mol. Biol. , vol.196 , pp. 199-216
    • Bashford, D.1    Chothia, C.2    Lesk, A.M.3
  • 6
    • 0029933671 scopus 로고    scopus 로고
    • Effective protein sequence comparison
    • Pearson,W.R. (1996) Effective protein sequence comparison. Methods Enzymol., 266, 227-258.
    • (1996) Methods Enzymol. , vol.266 , pp. 227-258
    • Pearson, W.R.1
  • 8
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith,T.F. and Waterman,M.S. (1981) Identification of common molecular subsequences. J. Mol. Biol., 147, 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 9
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson,T.J., Higgins,D.G. and Gibson,T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, T.J.1    Higgins, D.G.2    Gibson, T.J.3
  • 10
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus,K., Barrett,C. and Hughey,R. (1998) Hidden Markov models for detecting remote protein homologies. Bioinformatics, 14, 846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 11
    • 0031684427 scopus 로고    scopus 로고
    • Combinatorial pattern discovery in biological sequences: The TEIRESIAS algorithm
    • Rigoutsos,I. and Floratos,A. (1998) Combinatorial pattern discovery in biological sequences: the TEIRESIAS algorithm. Bioinformatics, 14, 55-67.
    • (1998) Bioinformatics , vol.14 , pp. 55-67
    • Rigoutsos, I.1    Floratos, A.2
  • 12
    • 0032719352 scopus 로고    scopus 로고
    • Dictionary building via unsupervised hierarchical motif discovery in the sequence space of natural proteins
    • Rigoutsos,I., Floratos,A., Ouzounis,C., Gao,Y. and Parida,L. (1999) Dictionary building via unsupervised hierarchical motif discovery in the sequence space of natural proteins. Proteins, 37, 264-277.
    • (1999) Proteins , vol.37 , pp. 264-277
    • Rigoutsos, I.1    Floratos, A.2    Ouzounis, C.3    Gao, Y.4    Parida, L.5
  • 13
    • 0033957834 scopus 로고    scopus 로고
    • The Swiss-Prot protein sequence database and its supplement TrEMBL in 2000
    • Bairoch,A. and Apweiler,R. (2000) The Swiss-Prot protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res., 28, 45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 15
    • 0037096851 scopus 로고    scopus 로고
    • Dictionary-driven prokaryotic gene finding
    • Shibuya,T. and Rigoutsos,I. (2002) Dictionary-driven prokaryotic gene finding. Nucleic Acids Res., 30, 2710-2725.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2710-2725
    • Shibuya, T.1    Rigoutsos, I.2
  • 16
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability and evolution
    • Popot,J.L. and Engelman,D.M. (2000) Helical membrane protein folding, stability and evolution. Annu. Rev. Biochem., 69, 881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 17
    • 0035895421 scopus 로고    scopus 로고
    • Non-α-helical elements modulate polytopic membrane architecture
    • Riek,R.P., Rigoutsos,I., Novotny,J. and Graham,R.M. (2001) Non-α-helical elements modulate polytopic membrane architecture. J. Mol. Biol., 306, 349-362.
    • (2001) J. Mol. Biol. , vol.306 , pp. 349-362
    • Riek, R.P.1    Rigoutsos, I.2    Novotny, J.3    Graham, R.M.4
  • 18
    • 0035367173 scopus 로고    scopus 로고
    • Helical membrane proteins: Diversity of functions in the context of simple architecture
    • Ubarretxena-Belandia,I. and Engelman,D.M. (2001) Helical membrane proteins: diversity of functions in the context of simple architecture. Curr. Opin. Struct. Biol., 11, 370-376.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 370-376
    • Ubarretxena-Belandia, I.1    Engelman, D.M.2
  • 19
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen bonded helical conformations of the polypeptide chain
    • Pauling,L., Corey,R.B. and Branson,H.R. (1951) The structure of proteins: two hydrogen bonded helical conformations of the polypeptide chain. Proc. Natl Acad. Sci. USA, 37, 205-211.
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 20
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow,D.J. and Thornton,J.M. (1988) Helix geometry in proteins. J. Mol. Biol., 201, 601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 22
    • 0037076531 scopus 로고    scopus 로고
    • Mutation of a single TMVI residue, Phe(282), in the beta(2)-adrenergic receptor results in structurally distinct activated receptor conformations
    • Chen,S., Lin,F., Xu,M., Riek,P., Novotny,J. and Graham,R.M. (2002) Mutation of a single TMVI residue, Phe(282), in the beta(2)-adrenergic receptor results in structurally distinct activated receptor conformations. Biochemistry, 41, 6045-6053.
    • (2002) Biochemistry , vol.41 , pp. 6045-6053
    • Chen, S.1    Lin, F.2    Xu, M.3    Riek, P.4    Novotny, J.5    Graham, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.