메뉴 건너뛰기




Volumn 33, Issue 16, 2005, Pages 5343-5353

Gibbs sampling and helix-cap motifs

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; INFORMATION RETRIEVAL; MOLECULAR MODEL; PEPTIDE MAPPING; PREDICTION; PRIORITY JOURNAL; PROBABILITY; PROTEIN DATABASE; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; RECEIVER OPERATING CHARACTERISTIC; RIBOSOMAL FRAMESHIFTING; RNA CAPPING; SCORING SYSTEM; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; EVALUATION; METHODOLOGY;

EID: 24944461865     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gki842     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson,J.S. and Richardson,D.C. (1988) Amino acid preferences for specific locations at the ends of alpha helices. Science, 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 2
    • 0032101291 scopus 로고    scopus 로고
    • Dissecting alpha-helices: Position-specific analysis of alpha-helices in globular proteins
    • Kumar,S. and Bansal,M. (1998) Dissecting alpha-helices: position-specific analysis of alpha-helices in globular proteins. Proteins, 31, 460-476.
    • (1998) Proteins , vol.31 , pp. 460-476
    • Kumar, S.1    Bansal, M.2
  • 4
    • 0037468399 scopus 로고    scopus 로고
    • Exceptional pairs of amino acid neighbors in alpha helices
    • Goliaei,B. and Minuchehr,Z. (2003) Exceptional pairs of amino acid neighbors in alpha helices. FEBS Lett., 537, 121-127.
    • (2003) FEBS Lett. , vol.537 , pp. 121-127
    • Goliaei, B.1    Minuchehr, Z.2
  • 5
    • 1842523274 scopus 로고    scopus 로고
    • Amino acid propensities are position-dependent throughout the length of alpha-helices
    • Engel,D.E. and DeGrado,W.F. (2004) Amino acid propensities are position-dependent throughout the length of alpha-helices. J. Mol. Biol., 337, 1195-1204.
    • (2004) J. Mol. Biol. , vol.337 , pp. 1195-1204
    • Engel, D.E.1    DeGrado, W.F.2
  • 6
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta,L.G. and Rose,G.D. (1988) Helix signals in proteins. Science, 240, 1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 7
    • 0027207221 scopus 로고
    • Comparison of three algorithms for the assignment of secondary structure in proteins: The advantages of a consensus assignment
    • Colloc'h,N., Etchebest,C., Thoreau,E., Henrissat,B. and Mornon,J.P. (1993) Comparison of three algorithms for the assignment of secondary structure in proteins: The advantages of a consensus assignment. Protein Eng., 6, 377-382.
    • (1993) Protein Eng. , vol.6 , pp. 377-382
    • Colloc'h, N.1    Etchebest, C.2    Thoreau, E.3    Henrissat, B.4    Mornon, J.P.5
  • 8
    • 2942541294 scopus 로고    scopus 로고
    • Use of a structural alphabet for analysis of short loops connecting repetitive structures
    • Fourrier,L., Benros,C. and de Brevern,A. (2004) Use of a structural alphabet for analysis of short loops connecting repetitive structures. Bioinformatics, 5, 58-71.
    • (2004) Bioinformatics , vol.5 , pp. 58-71
    • Fourrier, L.1    Benros, C.2    de Brevern, A.3
  • 9
    • 0036174712 scopus 로고    scopus 로고
    • Continuum secondary structure captures protein flexibility
    • Andersen,C.A., Palmer,A.G., Brunak,S. and Rost,B. (2002) Continuum secondary structure captures protein flexibility. Structure, 10, 175-184.
    • (2002) Structure , vol.10 , pp. 175-184
    • Andersen, C.A.1    Palmer, A.G.2    Brunak, S.3    Rost, B.4
  • 10
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Wang,Y. and Jardetzky,O. (2002) Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci., 11, 852-861.
    • (2002) Protein Sci. , vol.11 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 11
    • 21244473258 scopus 로고    scopus 로고
    • 3(10)-helix adjoining alpha-helix and beta-strand: Sequence and structural features and their conservation
    • Pal,L., Dasgupta,B. and Chakrabarti,P. (2005) 3(10)-helix adjoining alpha-helix and beta-strand: Sequence and structural features and their conservation. Biopolymers, 78, 147-162.
    • (2005) Biopolymers , vol.78 , pp. 147-162
    • Pal, L.1    Dasgupta, B.2    Chakrabarti, P.3
  • 12
    • 0031660702 scopus 로고    scopus 로고
    • Geometrical and sequence characteristics of alpha-helices in globular proteins
    • Kumar,S. and Bansal,M. (1998) Geometrical and sequence characteristics of alpha-helices in globular proteins. Biophys. J., 75, 1935-1944.
    • (1998) Biophys. J. , vol.75 , pp. 1935-1944
    • Kumar, S.1    Bansal, M.2
  • 13
    • 1842532057 scopus 로고    scopus 로고
    • Exapanded turn conformations: Characterization and sequence-structure correspondence in α-turns with implications in helix folding
    • Dasgupta,B., Lipika,P., Basu,G. and Chakrabarti,P. (2004) Exapanded turn conformations: Characterization and sequence-structure correspondence in α-turns with implications in helix folding. Proteins, 55, 305-315.
    • (2004) Proteins , vol.55 , pp. 305-315
    • Dasgupta, B.1    Lipika, P.2    Basu, G.3    Chakrabarti, P.4
  • 14
    • 0035314041 scopus 로고    scopus 로고
    • Pex, analytical tools for pdb files. II. H-Pex: Noncanonical H-bonds in alpha-helices
    • Thomas,A., Benhabiles,N., Meurisse,R., Ngwabije,R. and Brasseur,R. (2001) Pex, analytical tools for pdb files. II. H-Pex: Noncanonical H-bonds in alpha-helices. Proteins, 43, 37-44.
    • (2001) Proteins , vol.43 , pp. 37-44
    • Thomas, A.1    Benhabiles, N.2    Meurisse, R.3    Ngwabije, R.4    Brasseur, R.5
  • 15
    • 0033994775 scopus 로고    scopus 로고
    • HELANAL: A program to characterize helix geometry in proteins
    • Bansal,M., Kumar,S. and Velavan,R. (2000) HELANAL: A program to characterize helix geometry in proteins. J. Biomol. Struct. Dyn., 17, 811-819.
    • (2000) J. Biomol. Struct. Dyn. , vol.17 , pp. 811-819
    • Bansal, M.1    Kumar, S.2    Velavan, R.3
  • 19
    • 0024316598 scopus 로고
    • PKB: A program system and data base for analysis of protein structure
    • Bryant,S.H. (1989) PKB: A program system and data base for analysis of protein structure. Proteins, 5, 233-247.
    • (1989) Proteins , vol.5 , pp. 233-247
    • Bryant, S.H.1
  • 20
    • 0034628901 scopus 로고    scopus 로고
    • Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae
    • Hughes,J., Estep,P., Tavazoie,S. and Church,G. (2000) Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae. J. Mol. Biol., 296, 1205-1214.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1205-1214
    • Hughes, J.1    Estep, P.2    Tavazoie, S.3    Church, G.4
  • 22
  • 23
    • 0029144601 scopus 로고
    • Gibbs motif sampling: Detection of bacterial outer membrane protein repeats
    • Neuwald,A.F., Liu,J.S. and Lawrence,C.E. (1995) Gibbs motif sampling: detection of bacterial outer membrane protein repeats. Protein Sci., 4, 3836-3845.
    • (1995) Protein Sci. , vol.4 , pp. 3836-3845
    • Neuwald, A.F.1    Liu, J.S.2    Lawrence, C.E.3
  • 24
    • 0037627753 scopus 로고    scopus 로고
    • Identifying residue-residue clashes in protein hybrids by using second-order mean-field approach
    • Moore,G.L. and Maranas,C.D. (2003) Identifying residue-residue clashes in protein hybrids by using second-order mean-field approach. Proc. Natl Acad. Sci. USA, 100, 5091-5096.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5091-5096
    • Moore, G.L.1    Maranas, C.D.2
  • 26
    • 0142179047 scopus 로고    scopus 로고
    • Revisiting the Ramachandran plot: Hard-sphere repulsion, electrostatics, and H-bonding in the α-helix
    • Ho,B.K., Thomas,A. and Brasseur,R. (2003) Revisiting the Ramachandran plot: Hard-sphere repulsion, electrostatics, and H-bonding in the α-helix. Protein Sci., 12, 2508-2522.
    • (2003) Protein Sci. , vol.12 , pp. 2508-2522
    • Ho, B.K.1    Thomas, A.2    Brasseur, R.3
  • 27
    • 0034047548 scopus 로고    scopus 로고
    • Bayesian segmentation of protein secondary structure
    • Schmidler,S.C., Liu,J.S. and Brutlag,D.L. (2000) Bayesian segmentation of protein secondary structure. J. Comput. Biol., 7, 233-248.
    • (2000) J. Comput. Biol. , vol.7 , pp. 233-248
    • Schmidler, S.C.1    Liu, J.S.2    Brutlag, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.