메뉴 건너뛰기




Volumn 55, Issue 3, 2004, Pages 508-518

Evaluation of Local Structure Alphabets Based on Residue Burial

Author keywords

Fold recognition; Hidden Markov model; Local structure alphabet; Multi track HMM; Neighborhood counts; Protein structure prediction; Residue burial; Solvent accessibility

Indexed keywords

SOLVENT;

EID: 2442436935     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20008     Document Type: Article
Times cited : (56)

References (48)
  • 1
    • 0038278386 scopus 로고    scopus 로고
    • Hidden Markov models that use predicted local structure for fold recognition: Alphabets of backbone geometry
    • Karchin R, Cline M, Mandel-Gutfreund Y, Karplus K. Hidden Markov models that use predicted local structure for fold recognition: alphabets of backbone geometry. Proteins 2003;51:504-514.
    • (2003) Proteins , vol.51 , pp. 504-514
    • Karchin, R.1    Cline, M.2    Mandel-Gutfreund, Y.3    Karplus, K.4
  • 3
    • 0036321534 scopus 로고    scopus 로고
    • Assessing the relative importance of the biophysical properties of amino acid substitutions associated with human genetic disease
    • Terp BN, Cooper DN, Christensen IT, Jorgensen FS, Bross P, Gregersen N, Krawczak M. Assessing the relative importance of the biophysical properties of amino acid substitutions associated with human genetic disease. Human Mutation 2002;20:98-109.
    • (2002) Human Mutation , vol.20 , pp. 98-109
    • Terp, B.N.1    Cooper, D.N.2    Christensen, I.T.3    Jorgensen, F.S.4    Bross, P.5    Gregersen, N.6    Krawczak, M.7
  • 5
    • 0036387236 scopus 로고    scopus 로고
    • Evaluation of structural and evolutionary contributions to deleterious mutation prediction
    • Saunders CT, Baker D. Evaluation of structural and evolutionary contributions to deleterious mutation prediction. J Mol Biol 2002;322:891-901.
    • (2002) J Mol Biol , vol.322 , pp. 891-901
    • Saunders, C.T.1    Baker, D.2
  • 6
    • 0021118508 scopus 로고
    • Principles that determine the structure of proteins
    • Chothia C. Principles that determine the structure of proteins. Annu Rev Biochem 1984;55:537-572.
    • (1984) Annu Rev Biochem , vol.55 , pp. 537-572
    • Chothia, C.1
  • 7
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D, McLachlan AD. Solvation energy in protein folding and binding. Nature 1986;319:199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 8
    • 0032612579 scopus 로고    scopus 로고
    • Ab initio protein structure prediction of CASP III targets using ROSETTA
    • Simons KT, Bonneau R, Ruczinski I, Baker D. Ab initio protein structure prediction of CASP III targets using ROSETTA. Protein 1999;Suppl 3:171-176.
    • (1999) Protein , Issue.SUPPL. 3 , pp. 171-176
    • Simons, K.T.1    Bonneau, R.2    Ruczinski, I.3    Baker, D.4
  • 9
    • 0033005899 scopus 로고    scopus 로고
    • Pair potentials for protein folding: Choice of reference states and sensitivity of predicted native states to variations in the interaction schemes
    • Betancourt MR, Thirumalai D. Pair potentials for protein folding: choice of reference states and sensitivity of predicted native states to variations in the interaction schemes. Protein Sci 1999;8:361-319.
    • (1999) Protein Sci , vol.8 , pp. 361-319
    • Betancourt, M.R.1    Thirumalai, D.2
  • 11
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • Baker D, Sali A. Protein structure prediction and structural genomics. Science 2001;294:93-96.
    • (2001) Science , vol.294 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 12
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:151-176.
    • (1971) J Mol Biol , vol.55 , pp. 151-176
    • Lee, B.1    Richards, F.M.2
  • 13
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms
    • Shrake A, Rupley JA. Environment and exposure to solvent of protein atoms. J Mol Biol 1973;79:351-371.
    • (1973) J Mol Biol , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 14
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards FM. Areas, volumes, packing and protein structure. Ann Rev Biophys Bioeng 1977;6:151-176.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 15
    • 0001018540 scopus 로고
    • Analytical approximation to the accessible surface area of proteins
    • Wodak SJ, Janin J. Analytical approximation to the accessible surface area of proteins. Proc Nat Acad Sci USA 1980;77:1736-1740.
    • (1980) Proc Nat Acad Sci USA , vol.77 , pp. 1736-1740
    • Wodak, S.J.1    Janin, J.2
  • 16
    • 0021755764 scopus 로고
    • Solvent accessible surface area and excluded volume in proteins
    • Richmond DJ. Solvent accessible surface area and excluded volume in proteins. J Mol Biol 1984;177:63-89.
    • (1984) J Mol Biol , vol.177 , pp. 63-89
    • Richmond, D.J.1
  • 17
    • 84986519265 scopus 로고
    • A vectorized algorithm for calculating the accessible surface area of macromolecules
    • Wang Y, Levinthal C. A vectorized algorithm for calculating the accessible surface area of macromolecules. J Comput Chem 1991; 12:868-871.
    • (1991) J Comput Chem , vol.12 , pp. 868-871
    • Wang, Y.1    Levinthal, C.2
  • 18
    • 84912079256 scopus 로고
    • Rapid approximation to molecular surface area via the use of boolean logic and lookup tables
    • Le Grand SM, Merz JKM. Rapid approximation to molecular surface area via the use of boolean logic and lookup tables. J Comput Chem 1993;14:349-352.
    • (1993) J Comput Chem , vol.14 , pp. 349-352
    • Le Grand, S.M.1    Merz, J.K.M.2
  • 20
    • 0642340510 scopus 로고    scopus 로고
    • Amino acid empirical contact energy definitions for fold recognition in the space of contact maps
    • Berrera M, Molinari H, Fogolari F. Amino acid empirical contact energy definitions for fold recognition in the space of contact maps. BMC Bioinformatics 2003;4:8.
    • (2003) BMC Bioinformatics , vol.4 , pp. 8
    • Berrera, M.1    Molinari, H.2    Fogolari, F.3
  • 22
    • 0034565448 scopus 로고    scopus 로고
    • Prediction of the number of residue contacts in proteins
    • Altman R, Bailey TL, Bourne P, Gribskov M, Lengauer T, Shindyalov IN, Ten Eych LF, Weissig H, editors. San Diego, CA: AAAI Press
    • Fariselli P, Casadio R. Prediction of the number of residue contacts in proteins. In Altman R, Bailey TL, Bourne P, Gribskov M, Lengauer T, Shindyalov IN, Ten Eych LF, Weissig H, editors. Proceedings of the Eighth International Conference on Intelligent Systems for Molecular Biology, p 146-151. San Diego, CA: AAAI Press, 2000.
    • (2000) Proceedings of the Eighth International Conference on Intelligent Systems for Molecular Biology , pp. 146-151
    • Fariselli, P.1    Casadio, R.2
  • 23
    • 0036568293 scopus 로고    scopus 로고
    • Prediction of coordination number and relative solvent accessibility in proteins
    • Pollastri G, Baldi P, Fariselli P, Casadio R. Prediction of coordination number and relative solvent accessibility in proteins. Proteins 2002;47:142-153.
    • (2002) Proteins , vol.47 , pp. 142-153
    • Pollastri, G.1    Baldi, P.2    Fariselli, P.3    Casadio, R.4
  • 24
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost B, Sander C. Conservation and prediction of solvent accessibility in protein families. Proteins 1994;20:216-226.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 26
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science 1996;273: 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 28
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Meth Enzymol 1996;266:525-539.
    • (1996) Meth Enzymol , vol.266 , pp. 525-539
    • Rost, B.1
  • 29
    • 0029885547 scopus 로고    scopus 로고
    • Predicting solvent accessibility: Higher accuracy using Bayesian statistics and optimized residue substitution classes
    • Thompson MJ, Goldstein RA. Predicting solvent accessibility: higher accuracy using Bayesian statistics and optimized residue substitution classes. Protein 1996;25:38-47.
    • (1996) Protein , vol.25 , pp. 38-47
    • Thompson, M.J.1    Goldstein, R.A.2
  • 30
    • 0033459568 scopus 로고    scopus 로고
    • The bottom line for prediction of residue solvent accessibility
    • Richardson CJ, Barlow DJ. The bottom line for prediction of residue solvent accessibility. Protein Eng 1999;12:1051-1054.
    • (1999) Protein Eng , vol.12 , pp. 1051-1054
    • Richardson, C.J.1    Barlow, D.J.2
  • 32
    • 0028064006 scopus 로고
    • Redefining the goals of protein secondary structure prediction
    • Rost B, Sander C, Schneider R. Redefining the goals of protein secondary structure prediction. J Mol Biol 1994;235:13-26.
    • (1994) J Mol Biol , vol.235 , pp. 13-26
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 33
    • 0001969211 scopus 로고    scopus 로고
    • Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching
    • Gribskov M, Robinson NL. Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching. Compu Chem 1996;20:25-33.
    • (1996) Compu Chem , vol.20 , pp. 25-33
    • Gribskov, M.1    Robinson, N.L.2
  • 34
    • 0036188264 scopus 로고    scopus 로고
    • Predicting reliable regions in protein sequence alignments
    • Cline M, Hughey R, Karplus K. Predicting reliable regions in protein sequence alignments. Bioinformatics 2002;18:306-314.
    • (2002) Bioinformatics , vol.18 , pp. 306-314
    • Cline, M.1    Hughey, R.2    Karplus, K.3
  • 35
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 36
    • 0036145846 scopus 로고    scopus 로고
    • Statistical potentials for fold assessment
    • Melo F, Sanchez R, Sali A. Statistical potentials for fold assessment. Protein Sci 2002;11:430-448.
    • (2002) Protein Sci , vol.11 , pp. 430-448
    • Melo, F.1    Sanchez, R.2    Sali, A.3
  • 38
  • 39
    • 0031938039 scopus 로고    scopus 로고
    • Comprehensive assessment of automatic structural alignment against a manual standard, the SCOP classification of proteins
    • Gerstein M, Levitt M. Comprehensive assessment of automatic structural alignment against a manual standard, the SCOP classification of proteins. Protein Sci 1998;7:445-456.
    • (1998) Protein Sci , vol.7 , pp. 445-456
    • Gerstein, M.1    Levitt, M.2
  • 41
    • 0038634975 scopus 로고    scopus 로고
    • Improvement of the genTHREADER method for genomic fold recognition
    • McGuffin LJ, Jones DT. Improvement of the genTHREADER method for genomic fold recognition. Bioinformatics 2003;19:874-881.
    • (2003) Bioinformatics , vol.19 , pp. 874-881
    • McGuffin, L.J.1    Jones, D.T.2
  • 42
    • 0034651866 scopus 로고    scopus 로고
    • An alternative view of protein fold space
    • Shindyalov IN, Bourne PE. An alternative view of protein fold space. Proteins 2000;38:247-260.
    • (2000) Proteins , vol.38 , pp. 247-260
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 43
    • 0022798896 scopus 로고
    • Radial locations of amino acid residues in a globular protein: Correlation with the sequence
    • Nishikawa K, Ooi T. Radial locations of amino acid residues in a globular protein: correlation with the sequence. J Biochem 1986; 100:1043-1047.
    • (1986) J Biochem , vol.100 , pp. 1043-1047
    • Nishikawa, K.1    Ooi, T.2
  • 45
    • 0036404919 scopus 로고    scopus 로고
    • On the significance of alternating patterns of polar and nonpolar residues in beta strands
    • Mandel-Gutfreund Y, Gregoret L. On the significance of alternating patterns of polar and nonpolar residues in beta strands. J Mol Biol 2002;323:453-461.
    • (2002) J Mol Biol , vol.323 , pp. 453-461
    • Mandel-Gutfreund, Y.1    Gregoret, L.2
  • 46
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, Argos P. Knowledge-based protein secondary structure assignment. Proteins 1995;23:566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 47
    • 0034604368 scopus 로고    scopus 로고
    • HMMSTR: A hidden Markov model for local sequence-structure correlations in proteins
    • Bystroff C, Thorsson V, Baker D. HMMSTR: a hidden Markov model for local sequence-structure correlations in proteins. J Mol Biol 2000;301:173-190.
    • (2000) J Mol Biol , vol.301 , pp. 173-190
    • Bystroff, C.1    Thorsson, V.2    Baker, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.