Abstract
In this paper we develop data mining techniques to predict 3D contact potentials among protein residues (or amino acids) based on the hierarchical nucleation-propagation model of protein folding. We apply a hybrid approach, using a Hidden Markov Model to extract folding initiation sites, and then apply association mining to discover contact potentials. The new hybrid approach achieves accuracy results better than those reported previously.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
S. Altschul, T. Madden, A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D. Lipman. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Research, 25(17), 3389–402, 1997.
C. Bystroff and D. Baker. Prediction of local structure in proteins using a library of sequence- structure motifs. Journal of Molecular Biology, 281(3), 565–77, 1998.
C. Bystroff, V. Thorsson, and D. Baker. HMMSTR: A hidden markov model for local sequence-structure correlations in proteins. Journal of Molecular Biology, (to appear), 2000.
S. Eddy. Profile hidden markov models. Bioinformatics, 14(9), 755–63, 1998.
P. Fariselli and R. Casadio. A neural network based predictor of residue contacts in proteins. Protein Engineering, 12(1), 15–21, 1999.
K. Han and D. Baker. Global properties of the mapping between local amino acid sequence and local structure in proteins. Proc. Natl Acad. Set USA, 93(12), 5814–5818, 1996.
B. Honig. Protein folding: from the levinthal paradox to structure prediction. Journal of Molecular Biology, 293(2), 283–93, 1999.
U. Hobohm and C. Sander. Enlarged representative set of protein structures. Protein Science, 3(3), 522–524, 1994.
W. Kabsch and C. Sander. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577–2637, 1983.
J. Moult, J.T. Pedersen, R. Judson, and K. Fidelis. A large-scale experiment to assess protein structure prediction methods. Proteins, 23(3), ii-v, 1995.
O. Olmea and A. Valencia. Improving contact predictions by the combination of correlated mutations and other sources of sequence information. Folding & Design, 2, S25-S32, June 1997.
L. Rabiner. A tutorial on hidden markov models and selected applications in speech recognition. Proceedings of the IEEE, 77(2):257–86, 1989.
L. Serrano, A. Matouschek, and A.R. Fersht. The folding of an enzyme. m. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. Journal of Molecular Biology, 224(3), 805–18, 1992.
D. Thomas, G. Casari, and C. Sander. The prediction of protein contacts from multiple sequence aligments. Protein Engineering, 9(11):941–48, 1996.
M. Vendruscolo, E. Kussell, and E. Domany. Recovery of protein structure from contact maps. Folding & Design, 2(5), 295–306, September 1997.
J. Wootton and S. Federhen. Analysis of compositionally biased regions in sequence databases. Methods Enzymol., 266, 554–71, 1996.
Y. I. Wolf, N. V. Grishin, and E. V. Koonin. Estimating the number of protein folds and families from complete genome data. Journal of Molecular Biology, 299(4), 897–905, 2000.
Q. Yi, C. Bystroff, P. Rajagopal, R. E. Klevit, and D. Baker. Prediction and structural characterization of an independently folding substructure in the src sh3 domain. Journal of Molecular Biology, 283(1), 293–300, 1998.
C. Zhao and S.-H. Kim. Environment-dependent residue contact energies for proteins. Proc. Natl Acad. Sci. USA, 97(6), 2550–5, 2000.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Zaki, M.J., Bystroff, C. (2001). Mining Residue Contacts in Proteins. In: Grossman, R.L., Kamath, C., Kegelmeyer, P., Kumar, V., Namburu, R.R. (eds) Data Mining for Scientific and Engineering Applications. Massive Computing, vol 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1733-7_9
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1733-7_9
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4020-0114-7
Online ISBN: 978-1-4615-1733-7
eBook Packages: Springer Book Archive