Protein Structure Prediction by Protein Threading
Abstract
The seminal work of Bowie, Lüthy, and Eisenberg (Bowie et al., 1991) on “the inverse protein folding problem” laid the foundation of protein structure prediction by protein threading. By using simple measures for fitness of different amino acid types to local structural environments defined in terms of solvent accessibility and protein secondary structure, the authors derived a simple and yet profoundly novel approach to assessing if a protein sequence fits well with a given protein structural fold. Their follow-up work (Elofsson et al., 1996; Fischer and Eisenberg, 1996; Fischer et al., 1996a,b) and the work by Jones, Taylor, and Thornton (Jones et al., 1992) on protein fold recognition led to the development of a new brand of powerful tools for protein structure prediction, which we now term “protein threading.” These computational tools have played a key role in extending the utility of all the experimentally solved structures by X-ray crystallography and nuclear magnetic resonance (NMR), providing structural models and functional predictions for many of the proteins encoded in the hundreds of genomes that have been sequenced up to now.
Keywords
Energy Function Query Sequence Tree Decomposition Protein Structure Prediction Query ProteinPreview
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References
- Alexandrov, N., and I. Shindyalov. 2003. PDP: protein domain parser. Bioinformatics 19:429–430.CrossRefGoogle Scholar
- Altschul, S.F., and W. Gish. 1996. Local alignment statistics. Methods Enzymol 266:460–480.CrossRefGoogle Scholar
- Altschul, S.F., T.L. Madden, A.A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D.J. Lipman. 1997. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25:3389–3402.CrossRefGoogle Scholar
- Andreeva, A., D. Howorth, S.E. Brenner, T. J. Hubbard, C. Chothia, and A.G. Murzin. 2004. SCOP database in 2004: Refinements integrate structure and sequence family data. Nucleic Acids Res. 32:D226–D229.CrossRefGoogle Scholar
- Apic, G., J. Gough, and S.A. Teichmann. 2001a. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J. Mol. Biol. 310:311–325.CrossRefGoogle Scholar
- Apic, G., J. Gough, and S.A. Teichmann. 2001b. An insight into domain combinations. Bioinformatics 17(Suppl. l):83–89.Google Scholar
- Arnborg, S., and A. Proskurowski. 1989. Linear time algorithms for NP-hard problems restricted to partial k-tree. Discrete Appl Math. 23:11–24.MATHMathSciNetCrossRefGoogle Scholar
- Bairoch, A., R. Apweiler, C.H. Wu, W.C. Barker, B. Boeckmann, S. Ferro, E. Gasteiger, H. Huang, R. Lopez, M. Magrane, M.J. Martin, D.A. Natale, C. O’Donovan, N. Redaschi, and L.S. Yeh. 2005. The Universal Protein Resource (UniProt). Nucleic Acids Res. 33:D154–D159.CrossRefGoogle Scholar
- Baker, D., and A. Sali. 2001. Protein structure prediction and structural genomics. Science 294:93–96.ADSCrossRefGoogle Scholar
- Barton, G.J., and M.J. Sternberg. 1987. A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons. J. Mol. Biol. 198:327–337.CrossRefGoogle Scholar
- Barton, G.J., and M.J. Sternberg. 1990. Flexible protein sequence patterns. A sensitive method to detect weak structural similarities. J. Mol. Biol. 212:389–402.CrossRefGoogle Scholar
- Bodlaender, H.L. 1996. A linear time algorithm for finding tree-decompositions of small treewidth. SIAMJ. Comput. 25:1305–1317.MATHMathSciNetCrossRefGoogle Scholar
- Bourne, P.E., and H. Weissig (eds.). 2003. Structural Bioinformatics. New York, Wiley-Liss.Google Scholar
- Bowie, J.U., R. Luthy, and D. Eisenberg. 1991. A method to identify protein sequences that fold into a known three-dimensional structure. Science 253:164–170.ADSCrossRefGoogle Scholar
- Branden, C., and J. Tooze. 1999. Introduction to Protein Structure, 2nd ed. New York, Garland Publishing.Google Scholar
- Brassard, G., and P. Bratley. 1996. Fundamentals of Algorithmes. Upper Saddle River, NJ, Prentice-Hall, pp. 265–266.Google Scholar
- Brenner, S.E., C. Chothia, T.J. Hubbard, and A.G. Murzin. 1996. Understanding protein structure: Using scop for fold interpretation. Methods Enzymol. 266:635–643.CrossRefGoogle Scholar
- Bryant, S.H., and S.F. Altschul. 1995. Statistics of sequence-structure threading. Curr. Opin. Struct. Biol. 5:236–244.CrossRefGoogle Scholar
- Calland, P.Y. 2003. On the structural complexity of a protein. Protein Eng. 16:79–86.CrossRefGoogle Scholar
- Chen, W., L. Mirny, and E.I. Shakhnovich. 2003. Fold recognition with minimal gaps. Proteins 51:531–543.CrossRefGoogle Scholar
- Clore, G.M., M.A. Robien, and A.M. Gronenborn. 1993. Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 231:82–102.CrossRefGoogle Scholar
- Cohen, F.E., and M.J. Sternberg. 1980. On the use of chemically derived distance constraints in the prediction of protein structure with myoglobin as an example. J. Mol. Biol. 137:9–22.CrossRefGoogle Scholar
- Coulson, A.F., and J. Moult. 2002. A unifold, mesofold, and superfold model of protein fold use. Proteins 46:61–71.CrossRefGoogle Scholar
- de Bakker, P.I., A. Bateman, D.F. Burke, R.N. Miguel, K. Mizuguchi, J. Shi, H. Shirai, and T.L. Blundell. 2001. HOMSTRAD: Adding sequence information to structure-based alignments of homologous protein families. Bioinformatics 17:748–749.CrossRefGoogle Scholar
- de Haan, CA., K. Stadler, G.J. Godeke, B.J. Bosch, and P.J. Rottier. 2004. Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion. J. Virol 78:6048–6054.CrossRefGoogle Scholar
- De Witte, R.S., and E.I. Shakhnovich. 1996. SMoG: de novo design method based on simple, fast, and accurate free energy estimates. 1. Methodology and supporting evidence. J. Am. Chem. Soc. 118:11733–11744.CrossRefGoogle Scholar
- Dietmann, S., and L. Holm. 2001. Identification of homology in protein structure classification. Nat. Struct. Biol. 8:953–957.CrossRefGoogle Scholar
- Ding, C.H., and I. Dubchak. 2001. Multi-class protein fold recognition using support vector machines and neural networks. Bioinformatics 17:349–358.CrossRefGoogle Scholar
- Doolittle, R.F. 1995. The multiplicity of domains in proteins. Annu. Rev. Biochem. 64:287–314.CrossRefGoogle Scholar
- Dutta, S., and H.M. Berman. 2005. Large macromolecular complexes in the Protein Data Bank: A status report. Structure 13:381–388.CrossRefGoogle Scholar
- Ekman, D., A.K. Bjorklund, J. Frey-Skott, and A. Elofsson. 2005. Multi-domain proteins in the three kingdoms of life: Orphan domains and other unassigned regions. J. Mol. Biol. 348:231–243.CrossRefGoogle Scholar
- Elofsson, A., D. Fischer, D.W. Rice, S.M. Le Grand, and D. Eisenberg. 1996. A study of combined structure/sequence profiles. Fold. Des. 1:451–461.CrossRefGoogle Scholar
- Fetrow, J.S., A. Giammona, A. Kolinski, and J. Skolnick. 2002. The protein folding problem: A biophysical enigma. Curr. Pharm. Biotechnol. 3:329–347.CrossRefGoogle Scholar
- Finkelstein, A.V, and O.B. Ptitsyn. 1987. Why do globular proteins fit the limited set of folding patterns? Prog. Biophys. Mol. Biol. 50: 171–190.CrossRefGoogle Scholar
- Fischer, D. 2000. Hybrid fold recognition: Combining sequence derived properties with evolutionary information. Pacific Symp. Biocomputing, Hawaii, pp. 119–130, World Scientific.Google Scholar
- Fischer, D. 2003. 3D-SHOTGUN: A novel, cooperative, fold-recognition metapredictor. Proteins 51:434–441.CrossRefGoogle Scholar
- Fischer, D., and D. Eisenberg. 1996. Protein fold recognition using sequence-derived predictions. Protein. Sci. 5:947–955.CrossRefGoogle Scholar
- Fischer, D., A. Elofsson, D. Rice, and D. Eisenberg. 1996a. Assessing the performance of fold recognition methods by means of a comprehensive benchmark. Pac. Symp. Biocomput. 300–318.Google Scholar
- Fischer, D., D. Rice, J.U. Bowie, and D. Eisenberg. 1996b. Assigning amino acid sequences to 3-dimensional protein folds. FASEB J. 10:126–136.Google Scholar
- Frederickson, G.N. 1991. Planar graph decomposition and all pairs shortest paths. J. Assoc. Comput. Mach. 38:162–204.MATHMathSciNetGoogle Scholar
- Gaasterland, T. 1998. Structural genomics: Bioinformatics in the driver’s seat. Nat. Biotechnol. 16:625–627.CrossRefGoogle Scholar
- Gelfand, M.S., E.V Koonin, and A.A. Mironov. 2000. Prediction of transcription regulatory sites in Archaea by a comparative genomic approach. Nucleic Acids Res. 28:695–705.CrossRefGoogle Scholar
- Gerlt, J.A., and P.C. Babbitt. 2000. Can sequence determine function? Genome Biol. l(5):reviews 0005.1-0005.10.Google Scholar
- Gerstein, M. 1997. A structural census of genomes: Comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure. J. Mol. Biol. 274:562–576.CrossRefGoogle Scholar
- Gerstein, M. 1998. How representative are the known structures of the proteins in a complete genome? A comprehensive structural census. Fold. Des. 3:497–512.CrossRefGoogle Scholar
- Gerstein, M., and H. Hegyi. 1998. Comparing genomes in terms of protein structure: Surveys of a finite parts list. FEMS Microbiol. Rev. 22:277–304.CrossRefGoogle Scholar
- Godzik, A. 2003. Fold recognition methods. Methods Biochem Anal. 44:525–546.Google Scholar
- Guo, J.T., K. Elliott, W.J. Chung, D. Xu, S. Passovets, and Y. Xu. 2004. PROSPECT-PSPP: An automatic computational pipeline for protein structure prediction. Nucleic Acids Res. 32(Web Server issue):W522–525.CrossRefGoogle Scholar
- Hobohm, U., M. Scharf, R. Schneider, and C. Sander. 1992. Selection of representative protein data sets. Protein Sci. 1:409–417.CrossRefGoogle Scholar
- Holm, L., and C. Sander. 1996a. Mapping the protein universe. Science 273:595–603.ADSCrossRefGoogle Scholar
- Holm, L., and C. Sander. 1996b. The FSSP database: Fold classification based on structure-structure alignment of proteins. Nucleic Acids Res. 24:206–209.CrossRefGoogle Scholar
- Jacobson, M.P., D.L. Pincus, C.S. Rapp, T.J. Day, B. Honig, D.E. Shaw, and R.A. Friesner. 2004. A hierarchical approach to all-atom protein loop prediction. Proteins 55:351–367.CrossRefGoogle Scholar
- Jiang, T., Y. Xu, and M. Zhang (eds.). 2002. Current Topics in Computational Molecular Biology. Cambridge, MA, MIT Press.Google Scholar
- Jones, D.T. 1999a. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195–202.CrossRefGoogle Scholar
- Jones, D.T. 1999b. GenTHREADER: An efficient, and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 287:797–815.CrossRefGoogle Scholar
- Jones, D.T., W.R. Taylor, and J.M. Thornton. 1992. A new approach to protein fold recognition. Nature 358:86–89.ADSCrossRefGoogle Scholar
- Kim, D, D. Xu, J.T. Guo, K. Ellrott, and Y. Xu. 2003. PROSPECT II: Protein structure prediction program for genome-scale applications. Protein Eng. 16:641–650.CrossRefGoogle Scholar
- Kinch, L.N., J.O. Wrabl, S.S. Krishna, I. Majumdar, R.I. Sadreyev, Y. Qi, J. Pei, H. Cheng, and N.V Grishin. 2003. CASP5 assessment of fold recognition target predictions. Proteins 53(Suppl.6):395–409.CrossRefGoogle Scholar
- Koonin, E.V, Y.I. Wolf, and G.P. Karev. 2002. The structure of the protein universe and genome evolution. Nature 420:218–223.ADSCrossRefGoogle Scholar
- Laskowski, R.A., M.W. MacArthur, D.S. Moss, and J.M. Thornton. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J.Appl. Crystallogr. 26:283–291.CrossRefGoogle Scholar
- Lathrop, R.H. 1994. The protein threading problem with sequence amino acid interaction preferences is NP-complete. Protein Eng. 7:1059–1068.CrossRefGoogle Scholar
- Lesk, A. 2001. Introduction to Protein Architecture: The Structural Biology of Proteins. London, Oxford University Press.Google Scholar
- Levitt, M., and M. Gerstein. 1998. A unified statistical framework for sequence comparison and structure comparison. Proc. Natl. Acad. Sci. USA 95:5913–5920.ADSCrossRefGoogle Scholar
- Li, H., R. Helling, C. Tang, and N. Wingreen. 1996. Emergence of preferred structures in a simple model of protein folding. Science 273:666–669.ADSCrossRefGoogle Scholar
- Li, H., C. Tang, and N.S. Wingreen. 1998. Are protein folds atypical? Proc. Natl. Acad. Sci. USA 95:4987–4990.ADSCrossRefGoogle Scholar
- Li, H., C. Tang, and N.S. Wingreen. 2002. Designability of protein structures: A lattice-model study using the Miyazawa-Jernigan matrix. Proteins 49:403–412.CrossRefGoogle Scholar
- Lu, H., and J. Skolnick. 2001. A distance-dependent atomic knowledge-based potential for improved protein structure selection. Proteins 44:223–232.CrossRefGoogle Scholar
- Li, X., and J. Liang. 2005. Geometric cooperativity and anti-cooperativity of three-body interactions in native proteins. Proteins 60:46–65.CrossRefGoogle Scholar
- Lu, L., A.K. Arakaki, H. Lu, and J. Skolnick. 2003. Multimeric threading-based prediction of protein-protein interactions on a genomic scale: Application to the Saccharomyces cerevisiae proteome. Genome Res. 13(6A): 1146–1154.CrossRefGoogle Scholar
- Lund, O., K. Frimand, J. Gorodkin, H. Bohr, J. Bohr, J. Hansen, and S. Brunak. 1997. Protein distance constraints predicted by neural networks and probability density functions. Protein Eng. 10:1241–1248.CrossRefGoogle Scholar
- Lundstrom, J., L. Rychlewski, J. Bujnicki, A. Elofsson. 2001. Peons: A neuralnetwork-based consensus predictor that improves fold recognition. Protein Sci. 10:2354–2362.CrossRefGoogle Scholar
- Madej, T., M.S. Boguski, and S.H. Bryant. 1995. Threading analysis suggests that the obese gene product may be a helical cytokine. FEBSLett. 373:13–18.CrossRefGoogle Scholar
- Makarova, K.S., L. Aravind, M.Y. Galperin, N.V Grishin, R.L. Tatusov, Y.I. Wolf, and E.V Koonin. 1999. Comparative genomics of the Archaea (Euryarchaeota): Evolution of conserved protein families, the stable core, and the variable shell. Genome Res. 9:608–628.Google Scholar
- May, R.M. 1988. How many species are there on earth. Science 241:1441–1449.ADSCrossRefGoogle Scholar
- McGuffin, L.J., and D.T Jones. 2003. Improvement of the GenTHREADER method for genomic fold recognition. Bioinformatics 19:874–881.CrossRefGoogle Scholar
- McGuffin, L.J., S.A. Street, K. Bryson, S.A. Sorensen, and D.T. Jones. 2004. The Genomic Threading Database: A comprehensive resource for structural annotations of the genomes from key organisms. Nucleic Acids Res. 32(Database issue):D196–199.CrossRefGoogle Scholar
- Melo, F., and E. Feytmans. 1997. Novel knowledge-based mean force potential at atomic level. J. Mol. Biol. 267:207–222.CrossRefGoogle Scholar
- Mirny, L.A., A.V. Finkelstein, and E.I. Shakhnovich. 2000. Statistical significance of protein structure prediction by threading. Proc. Natl. Acad. Sci. USA 97:9978–9983.ADSCrossRefGoogle Scholar
- Munson, P.I., and R.K. Singh. 1997. Statistical significance of hierarchical multi-body potentials based on Delaunay tessellation and their application in sequence-structure alignment. Protein Sci. 6:1467–1481.CrossRefGoogle Scholar
- Murzin, A.G., S.E. Brenner, T. Hubbard, and C. Chothia. 1995. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:536–540.Google Scholar
- Orengo, CA., D.T. Jones, and J.M. Thornton. 1994. Protein superfamilies and domain superfolds. Nature 372:631–634.ADSCrossRefGoogle Scholar
- Orengo, CA., A.D. Michie, S. Jones, D.T. Jones, M.B. Swindells, and J.M. Thornton. 1997. CATH—A hierarchic classification of protein domain structures. Structure 5:1093–1108.CrossRefGoogle Scholar
- Orengo, C.A., and W.R. Taylor. 1993. A local alignment method for protein structure motifs. J. Mol. Biol. 233:488–497.CrossRefGoogle Scholar
- Panchenko, A., A. Marchler-Bauer, and S.H. Bryant. 1999. Threading with explicit models for evolutionary conservation of structure and sequence. Proteins Suppl. 3:133–140.CrossRefGoogle Scholar
- Panchenko, A.R., A. Marchler-Bauer, and S.H. Bryant. 2000. Combination of threading potentials and sequence profiles improves fold recognition. J. Mol. Biol. 296:1319–1331.CrossRefGoogle Scholar
- Papadimitriou, C., and H. Christos. 1998. Combinatorial Optimization: Algorithms and Complexity. New York, Dover Publications.Google Scholar
- Prestegard, J.H. 1998. New techniques in structural NMR-anisotropic interactions. Nat. Struct. Biol. 5(Suppl.):517–522.CrossRefGoogle Scholar
- Qu, Y., J.T. Guo, V. Olman, and Y. Xu. 2004a. Protein fold recognition through application of residual dipolar coupling data. Pac. Symp. Biocomput. pp. 459–470.Google Scholar
- Qu, Y., J.T. Guo, V. Olman, and Y. Xu. 2004b. Protein structure prediction using sparse dipolar coupling data. Nucleic Acids Res. 32:551–561.CrossRefGoogle Scholar
- Richardson, J.S. 1981. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34:167–339.CrossRefGoogle Scholar
- Robertson, N., and P.D. Seymour. 1986. Graph minors.2. algorithmic aspects of tree-width. J. Algorithm 7:309–322.MATHMathSciNetCrossRefGoogle Scholar
- Rost, B., R. Schneider, and C Sander. 1997. Protein fold recognition by predictionbased threading. J. Mol. Biol. 270:471–480.CrossRefGoogle Scholar
- Sali, A., and T.L. Blundell. 1990. Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J. Mol. Biol. 212:403–428.CrossRefGoogle Scholar
- Samudrala, R., and J. Moult. 1998. An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J. Mol. Biol. 275:895–916.CrossRefGoogle Scholar
- Shi, J., L. Blund, and K. Mizuguchi. 2001. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structuredependent gap penalties. J. Mol. Biol. 310:243–257.CrossRefGoogle Scholar
- Sippl, M.J.. 1990. Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins. J. Mol. Biol. 213:859–883.CrossRefGoogle Scholar
- Sippl, M.J., P. Lackner, F.S. Domingues, A. Prlic, R. Malik, A. Andreeva, and M. Wiederstein. 2001. Assessment of the CASP4 fold recognition category. Proteins Suppl. 5:55–67.Google Scholar
- Skolnick, J., J.S. Fetrow, and A. Kolinski. 2000. Structural genomics and its importance for gene function analysis. Nat. Biotechnol 18:283–287.CrossRefGoogle Scholar
- Skolnick, J., and D. Kihara. 2001. Defrosting the frozen approximation: PROSPECTOR: A new approach to threading. Proteins 42:319–331.CrossRefGoogle Scholar
- Sommer, I., A. Zien, N. von Ohsen, R. Zimmer, and T. Lengauer. 2002. Confidence measures for protein fold recognition. Bioinformatics 18:802–812.CrossRefGoogle Scholar
- Song, Y., K. Ellrott, C. Liu, J. Guo, Y. Xu, and L. Cai. 2005. Tree decomposition based protein threading. Submitted.Google Scholar
- Sorenson, J.M., and T. Head-Gordon. 1999. Redesigning the hydrophobic core of a model beta-sheet protein: Destabilizing traps through a threading approach. Proteins 37:582–591.CrossRefGoogle Scholar
- Tatusov, R.L., M.Y. Galperin, D.A. Natale, and E.V. Koonin. 2000. The COG database: A tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res. 28:33–36.CrossRefGoogle Scholar
- Taylor, W.R., and C.A. Orengo. 1989. Protein structure alignment. J. Mol. Biol. 208:1–22.CrossRefGoogle Scholar
- Tolman, J.R., J.M. Flanagan, M.A. Kennedy, and J.H. Prestegard. 1995. Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution. Proc. Natl. Acad. Sci. USA 92:9279–9283.ADSCrossRefGoogle Scholar
- Tsigelny, I.F. (eds.). 2002. Protein Structure Prediction: Bioinformatic Approach. La Jolla, CA, International University Line Publishers.Google Scholar
- Venclovas, C., A. Zemla, K. Fidelis, and J. Moult. 2003. Assessment of progress over the CASP experiments. Proteins 53(Suppl. 6):585–595.CrossRefGoogle Scholar
- von Grotthuss, M., L.S. Wyrwicz, and L. Rychlewski. 2003. mRNA cap-1 methyltransferase in the SARS genome. Cell 113:701–702.CrossRefGoogle Scholar
- Vriend, G. 1990. WHAT IF: A molecular modelling and drug design program. J. Mol. Graph. 8:52–56.CrossRefGoogle Scholar
- Wan, X.F., D. Ataman, and D. Xu. 2005. Application of computational biology in understanding emerging infectious diseases: Inferring the biological function for S-M complex of SARS-CoV inProgress in Bioinformatics. New York, Nova Science Publishers, pp. 55–80.Google Scholar
- Wang, G., and R.L. Dunbrack, Jr. 2003. PISCES: A protein sequence culling server. Bioinformatics 19:1589–1591.CrossRefGoogle Scholar
- Wang, Z.X. 1996. How many fold types of protein are there in nature? Proteins 26:186–191.CrossRefGoogle Scholar
- Westhead, D.R., V.P. Collura, M.D. Eldridge, M.A. Firth, J. Li, and C.W. Murray. 1995. Protein fold recognition by threading: Comparison of algorithms and analysis of results. Protein Eng. 8:1197–1204.CrossRefGoogle Scholar
- Wetlaufer, D.B. 1973. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. USA 70:697–701.ADSCrossRefGoogle Scholar
- Xu, D., K. Baburaj, C.B. Peterson, and Y. Xu. 2001. Model for the three-dimensional structure of vitronectin: Predictions for the multi-domain protein from threading and docking. Proteins 44:312–320.CrossRefGoogle Scholar
- Xu, D., D. Kim, P. Dam, M. Shah, E.C. Uberbacher, and Y. Xu. 2003. Characterization of protein structure and function at genome scale with a computational prediction pipeline. In Genetic Engineering, Principles and Methods, Vol. 25, J.K. Setlow (ed.). New York, Kluwer Academic/Plenum Publishers, pp. 269–293.Google Scholar
- Xu, D., M.A. Unseren, Y. Xu, and C. Uberbacher. 2000. Sequence-structure specificity of a knowledge based energy function at the secondary structure level. Bioinformatics 16:257–268.CrossRefGoogle Scholar
- Xu, J., F. Jiao, and B. Berger. 2005. A tree decomposition approach to protein structure prediction. Proceedings of 2005 IEEE Computational Systems Bioinformatics Conference, pp. 247–256.Google Scholar
- Xu, J., and M. Li. 2003. Assessment of RAPTOR’s linear programming approach in CAFASP3. Proteins 53(Suppl. 6):579–584.CrossRefGoogle Scholar
- Xu, J., M. Li, D. Kim, and Y. Xu. 2003a. RAPTOR: Optimal protein threading by linear programming. J. Bioinform. Comput. Biol 1:95–117.CrossRefGoogle Scholar
- Xu, J., M. Li, G. Lin, D. Kim, and Y. Xu. 2003b. Protein threading by linear programming. Pac. Symp. Biocomput. pp. 264–275.Google Scholar
- Xu, Y., and E.C. Uberbacher. 1996. A polynomial-time algorithm for a class of protein threading problems. Comput. Appl. Biosci. 12:511–517.Google Scholar
- Xu, Y., and D. Xu. 2000. Protein threading using PROSPECT: Design and evaluation. Proteins 40:343–354.CrossRefGoogle Scholar
- Xu, Y., D. Xu, O.H. Crawford, and J.R. Einstein. 2000c. A computational method for NMR-constrained protein threading. J. Comput. Biol. 7:449–467.CrossRefGoogle Scholar
- Xu, Y., D. Xu, O.H. Crawford, J.R. Einstein, F. Larimer, E. Uberbacher, M.A. Unseren, and G. Zhang. 1999. Protein threading by PROSPECT: A prediction experiment in CASP3. Protein Eng. 12:899–907.CrossRefGoogle Scholar
- Xu, Y., D. Xu, O.H. Crawford, J.R. Einstein, and E. Serpersu. 2000b. Protein structure determination using protein threading and sparse NMR data. Annual Conference on Research in Computational Molecular Biology, pp. 299–307.Google Scholar
- Xu, Y., D. Xu, and H.N. Gabow. 2000a. Protein domain decomposition using a graph-theoretic approach. Bioinformatics 16:1091–1104.CrossRefGoogle Scholar
- Xu, Y., D. Xu, and V Olman. 2002. A practical method for interpretation of threading scores: An application of neural network. Stat Sinica. 12:159–177.MATHMathSciNetGoogle Scholar
- Xu, Y., D. Xu, and E.C. Uberbacher. 1998. An efficient computational method for globally optimal threading. J. Comput. Biol. 5:597–614.CrossRefGoogle Scholar
- Yan, B., C. Pan, V.N. Olman, R.L. Hettich, and Y. Xu. 2005. A graph-theoretic approach for the separation of b and y ions in tandem mass spectra. Bioinformatics 21:563–574.CrossRefGoogle Scholar
- Ye, X., P.K. O’Neil, A.N. Foster, M.J. Gajda, J. Kosinski, M.A. Kurowski, J.M. Bujnicki, A.M. Friedman, and C. Bailey-Kellogg. 2004.Probabilistic cross-link analysis and experiment planning for high-throughput elucidation of protein structure. Protein Sci. 13:3298–3313.CrossRefGoogle Scholar
- Young, M.M., N. Tang, J.C. Hempel, C.M. Oshiro, E.W. Taylor, I.D. Kuntz, B.W. Gibson, and G. Dollinger. 2000. High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc. Natl. Acad. Sci. USA 97:5802–5806.ADSCrossRefGoogle Scholar
- Zhang, B., L. Jaroszewski, L. Rychlewski, and A. Godzik. 1997. Similarities and differences between nonhomologous proteins with similar folds: Evaluation of threading strategies. Fold. Des. 2:307–317.CrossRefGoogle Scholar
- Zhang, C., and C. DeLisi. 1998. Estimating the number of protein folds. J. Mol. Biol. 284:1301–1305.CrossRefGoogle Scholar
- Zhang, Y., and J. Skolnick. 2004. Scoring function for automated assessment of protein structure template quality. Proteins 57:702–710.CrossRefGoogle Scholar
- Zhou, H.Y., and Y.Q. Zhou. 2002. Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci. 11:2714–2726.CrossRefGoogle Scholar
- Zhou, H., and Y. Zhou. 2005. Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments. Proteins 58:321–328.CrossRefGoogle Scholar