Abstract
This chapter shows how proteins can be represented in processes performed in scientific fields, such as functional genomics, comparative bioinformatics, and molecular modeling. The chapter begins with the general definition of protein spatial structure, which can be treated as a base for deriving other forms of representation. The general definition is then referenced to four representation levels of protein structure: primary, secondary, tertiary, and quaternary structure. This is followed by short description of protein geometry. And finally, at the end of the chapter, we will discuss energy features that can be calculated based on the general description of protein structure. The formal model defined in the chapter will be used in the description of algorithms presented in the following chapters of the book.
Proteins are where the action is. Arthur M. Lesk, 2010
The great promise of structural bioinformatics is predicted on the belief that the availability of high-resolution structural information about biological systems will allow us to precisely reason about the function of these systems and the effects of modifications or perturbations.
Jenny Gu, Philip E. Bourne, 2009
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References
Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J.: Basic local alignment search tool. J. Mol. Biol. 215, 403–410 (1990)
Arnold, K., Bordoli, L., Kopp, J., Schwede, T.: The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22(2), 195–201 (2009)
Berardi, M., Bushweller, J.: Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction. J. Mol. Biol. 292, 151–161 (1999)
Berman, H., et al.: The Protein Data Bank. Nucleic Acids Res. 28, 235–242 (2000)
Branden, C., Tooze, J.: Introduction to Protein Structure, 2nd edn. Garland Science, New York (1999)
Brooks, B.R., Bruccoleri, R.E., Olafson, B.D., States, D.J., Swaminathan, S., Karplus, M.: CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem. 4(2), 187–217 (1983)
Brown, N., Noble, M., Lawrie, A., Morris, M., et al.: Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity. J. Biol. Chem. 274, 8746–8756 (1999)
Burkowski. F.: Structural Bioinformatics: An Algorithmic Approach, 1st edn. Chapman and Hall/CRC, Boca Raton (2008)
Can, T., Wang, Y.: CTSS: a robust and efficient method for protein structure alignment based on local geometrical and biological features. In: Proceedings of the 2003 IEEE Bioinformatics Conference (CSB 2003), pp. 169–179 (2003)
Chen, P.Y., Lin, K.C., Lin, J.P., et al.: Phenethyl isothiocyanate (PEITC) inhibits the growth of human oral squamous carcinoma HSC-3 cells through G0/G1 phase arrest and mitochondria-mediated apoptotic cell death. Evidence-Based Complementary and Alternative Medicine, vol. 2012. Article ID 718320, pp. 1–12 (2012)
Chime and Jmol Homepage: Molecular Visualization Resources. http://www.umass.edu/microbio/chime/
Cornell, W.D., Cieplak, P., Bayly, C.I., Gould, I.R., Merz, K.M. Jr., Ferguson, D.M., Spellmeyer, D.C., Fox, T., Caldwell, J.W., Kollman, P.A.: A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117, 5179–5197 (1995)
Eswar, N., Marti-Renom, M.A., Webb, B., Madhusudhan, M.S., Eramian, D., Shen, M., Pieper, U., Sali, A.: Comparative Protein Structure Modeling with MODELLER. Current Protocols in Bioinformatics, Supplement 15, pp. 5.6.1–5.6.30. John Wiley & Sons Inc, New York (2006)
Fermi, G., Perutz, M.F., Shaanan, B., Fourme, R.: The crystal structure of human deoxyhaemoglobin at 1.74 A resolution. J. Mol. Biol. 175, 159–174 (1984)
Frishman, D., Argos, P.: 75% accuracy in protein secondary structure prediction. Proteins 27, 329–335 (1997)
Gans, J., Shalloway, D.: Qmol: a program for molecular visualization on windows-based PCs. J. Mol. Graph Model 19(6), 557–559 (2001)
Garnier, J., Gibrat, J.F., Robson, B.: GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 266, 540–553 (1996)
Hammel, L., Patel, J.M.: Searching on the secondary structure of protein sequences. In: Proceedings of the 28th International Conference on Very Large Data Bases. Hong Kong, China, pp. 634–645 (2002)
Harrington, D., Adachi, K., Royer Jr, W.: The high resolution crystal structure of deoxyhemoglobin S. J. Mol. Biol. 272, 398–407 (1997)
Heinke, F., Schildbach, S., Stockmann, D., Labudde, D.: eProSa database and toolbox for investigating protein sequence-structure-function relationships through energy profiles. Nucleic Acids Res. 41(D1), D320–D326 (2013)
Holm, L., Kaariainen, S., Rosenstrom, P., Schenkel, A.: Searching protein structure databases with DaliLite v. 3. Bioinformatics 24, 2780–2781 (2008)
Hong, H.J., Chen, P.Y., Shih, T.C., Ou, C.Y., Jhuo, M.D., Huang, Y.Y., Cheng, C.H., Wu, Y.C., Chung, J.G.: Computational pharmaceutical analysis of anti-Alzheimer’s Chinese medicine Coptidis Rhizoma alkaloids. Mol. Med. Rep. 5(1), 142–147 (2012)
Jmol Homepage: Jmol: an Open-Source Java Viewer for Chemical Structures in 3D. http://www.jmol.org
Källberg, M., Wang, H., Wang, S., Peng, J., Wang, Z., Lu, H., Xu, J.: Template-based protein structure modeling using the RaptorX web server. Nat. Protoc. 7, 1511–1522 (2012)
Kelley, L.A., Sternberg, M.J.E.: Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 4(3):363–371 (2009)
Kim, D.E., Chivian, D., Baker, D.: Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res. 32(Suppl 2), W526–W531 (2004)
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M.: PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283–291 (1993)
Leach, A.: Molecular Modelling: Principles and Applications, 2nd edn. Pearson Education EMA, London (2001)
Leaver-Fay, A., Tyka, M., Lewis, S.M., Lange, O.F., Thompson, J., Jacak, R., et al.: ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules. Methods Enzymol. 487, 545–574 (2011)
Małysiak, B., Momot, A., Kozielski, S., Mrozek, D.: On using energy signatures in protein structure similarity searching. In: Rutkowski, L., et al. (eds.) AISC 2008, Lecture Notes Computer Science, vol. 5097, pp. 939–950. Springer, Heidelberg (2008)
Mrozek, D., Małysiak, B., Kozielski, S.: An optimal alignment of proteins energy characteristics with crisp and fuzzy similarity awards. In: Proceedings of the IEEE International Conference on Fuzzy Systems (FUZZ-IEEE), pp. 1508–1513 (2007)
Mrozek, D., Małysiak, B., Kozielski, S.: EAST: energy alignment search tool. In: Wang, L., et al. (eds.): Proceedings of the 3rd IEEE International Conference on Fuzzy Systems and Knowledge Discovery. Xi’an, China, Lecture Notes Computer Science, vol. 4223, pp. 696–705. Springer, Berlin (2006)
Mrozek, D., Małysiak, B., Kozielski, S.: Energy profiles in detection of protein structure modifications. In: Proceedings of the IEEE International Conference on Computing and Informatics, Kuala Lumpur, pp. 1–6 (2006)
Mrozek, D., Małysiak, B., Kozielski, S.: Energy properties of protein structures in the analysis of the human RAB5A cellular activity. Adv. Intell. Soft Comput. 59, 121–131 (2009)
Mrozek, D., Małysiak-Mrozek, B., Kozielski, S., Górczynska-Kosiorz, S.: The EDML format to exchange energy profiles of protein molecular structures. Lecture Notes Computer Science, vol. 5754, Springer, pp. 146–157 (2009)
Mrozek, D., Małysiak-Mrozek, B., Kozielski, S., Świerniak, A.: The Energy Distribution Data Bank: collecting energy features of protein molecular structures. In Proceedings of the 9th IEEE International Conference on Bioinformatics and Bioengineering, IEEE, pp. 1–6 (2009)
Mrozek, D., Małysiak-Mrozek, B., Kozielski, S.: Alignment of protein structure energy patterns represented as sequences of fuzzy numbers. In: Fuzzy Information Processing Society, 2009. NAFIPS 2009. Annual Meeting of the North American Fuzzy Information Processing Society, pp. 1–6 (2009)
Mrozek, D., Małysiak-Mrozek, B.: An improved method for protein similarity searching by alignment of fuzzy energy signatures. Int. J. Comput. Intell. Syst. 4(1):75–88 (2011)
Mrozek, D., Małysiak-Mrozek, B.: CASSERT: a two-phase alignment algorithm for matching 3D structures of proteins. In: Kwiecień, A., Gaj, P., Stera, P. (eds.) CN 2013, CCIS, vol. 370, pp. 334–343 (2013)
Mrozek, D., Mastej, A., Małysiak, B.: Protein molecular viewer for visualizing structures stored in the PDBML format. In: Pietka, E., Kawa, J. (eds.) Information Technologies in Biomedicine, AISC, vol. 47, pp. 377–386. Springer, Berlin (2008)
Mrozek, D., Wieczorek, D., Małysiak-Mrozek, B., Kozielski, S.: PSS-SQL: protein secondary structure–structured query language. In: Proceedings of 32th Annual International Conference of the IEEE Engineering in Medicine and Biology Society, EMBS 2010, Buenos Aires, Argentina, pp. 1073–1076 (2010)
Mrozek, D., Małysiak-Mrozek, B., Kozielski, S.: Protein comparison by the alignment of fuzzy energy signatures. RSKT 2009. Lect. Notes Comput. Sci. 5589, 289–296 (2009)
Mrozek, D., Brożek, M., Małysiak-Mrozek, B.: Parallel implementation of 3D protein structure similarity searches using a GPU and the CUDA. J. Mol. Model 20, 2067 (2014)
Needleman, S.B., Wunsch, C.D.: A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48(3), 443–453 (1970)
Oostenbrink, C., Villa, A., Mark, A.E., van Gunsteren, W.: A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6. J. Comp. Chem. 25, 1656–1676 (2004)
Pearson, W.R.: Flexible sequence similarity searching with the FASTA3 program package. Methods Mol. Biol. 132, 185–219 (2000)
Ramachandran, G.N., Ramakrishnan, C., Sasisekaran, V.: Stereochemistry of polypeptide chain configurations. J. Mol. Biol. 7, 95–99 (1963)
Rost, B., Liu, J.: The predict protein server. Nucleic Acids Res. 31(13), 3300–3304 (2003)
Sayle, R.: RasMol, molecular graphics visualization tool. Biomolecular Structures Group, Glaxo Welcome Research & Development, Stevenage, Hartfordshire, 5/02/2013 (1998). http://www.umass.edu/microbio/rasmol/
Schrödinger, L.L.C.: The PyMOL molecular graphics system, version 1.3r1 (2010). http://www.pymol.org
Schulz, G.E., Schirmer, R.H.: Principles of Protein Structure. Springer, New York (1979)
Shapiro, J., Brutlag, D.: FoldMiner and LOCK2: protein structure comparison and motif discovery on the web. Nucleic Acids Res. 32, 536–541 (2004)
Shindyalov, I., Bourne, P.: Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11(9), 739–747 (1998)
Smith, T., Waterman, M.: Identification of common molecular subsequences. J. Mol. Biol. 147, 195–197 (1981)
Smith, G.D., Dodson, G.G.: The structure of a rhombohedral R6 insulin hexamer that binds phenol. Biopolymers 32(4), 441–445 (1992)
Söding, J.: Protein homology detection by HMM-HMM comparison. Bioinformatics 21, 951–960 (2005)
Stanek, D., Mrozek, D., Małysiak-Mrozek, B.: MViewer: visualization of protein molecular structures stored in the PDB, mmCIF and PDBML data formats. In: Kwiecień, A., Gaj, P., Stera, P. (eds.) CN 2013, CCIS vol. 370, pp. 323–333 (2013)
Taylor, W.R., Orengo, C.A.: A local alignment method for protein structure motifs. J. Mol. Biol. 233, 488–497 (1993)
Warecki, S., Znamirowski, L.: Random simulation of the nanostructures conformations. In: Proceedings of International Conference on Computing, Communication and Control Technology, vol. 1, The International Institute of Informatics and Systemics, Austin, Texas, pp. 388–393 (2004)
Watson, H.: The stereochemistry of the protein myoglobin. Prog. Stereochem. 24, 299 (1969)
Wu, S., Skolnick, J., Zhang, Y.: Ab initio modeling of small proteins by iterative TASSER simulations. BMC Biol. 5, 17 (2007)
Xu, J., Li, M., Kim, D., Xu, Y.: RAPTOR: optimal protein threading by linear programming, the inaugural issue. J. Bioinform. Comput. Biol. 1(1), 95–117 (2003)
Xu, D., Zhang, Y.: Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field. Proteins 80(7), 1715–1735 (2012)
Yang, Y., Faraggi, E., Zhao, H., Zhou, Y.: Improving protein fold recognition and template-based modeling by employing probabilistic-based matching between predicted one-dimensional structural properties of the query and corresponding native properties of templates. Bioinformatics 27, 2076–2082 (2011)
Ye, Y., Godzik, A.: Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 19(2), 246–255 (2003)
Zhu, J., Weng, Z.: FAST: a novel protein structure alignment algorithm. Proteins 58, 618–627 (2005)
Znamirowski, L.: Non-gradient, sequential algorithm for simulation of nascent polypeptide folding. Computational Science ICCS 2005. Lecture Notes in Computer Science vol. 3514, pp. 766–774 (2005)
Znamirowski, L.: Switching. VLSI Structures, Reprogrammable FPAA Structures, Nanostructures. Studia Informatica, vol. 25, no. 4A (60), Gliwice, pp. 1–236 (2004)
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Mrozek, D. (2014). Formal Model of 3D Protein Structures for Functional Genomics, Comparative Bioinformatics, and Molecular Modeling. In: High-Performance Computational Solutions in Protein Bioinformatics. SpringerBriefs in Computer Science. Springer, Cham. https://doi.org/10.1007/978-3-319-06971-5_1
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