Электронный журнал | Том 11 Выпуск 2 Год 2016

Данилкович А.В., Туробов В.И., Соболев Е.В. Удовиченко И.П.

Применение метода Тагучи для изучения структуры пептидного лиганда в составе сложного комплекса

Математическая биология и биоинформатика. 2016;11(2):385-393.

doi: 10.17537/2016.11.385.

Список литературы

Verma J., Khedkar V.M., Coutinho E:3D-QSAR in drug design – a review. Curr. Top. Med. Chem. 2010:10;95-115. doi: 10.2174/156802610790232260
Taguchi G. System of experimental design: engineering methods to optimize quality and minimize costs. V. 1. UNIPUB/Kraus International Publications; 1987.
Abbasian M.A., Moallem M., Fahimi B. Double stator switched reluctance machines (DSSRM): fundamentals and magnetic force analysis. IEEE Trans. on Energy Con. 2010;25:589-597. doi: 10.1109/TEC.2010.2051547
Chapman P.L., Sudhoff S.D. Design and precise realization of optimized current waveform for switched reluctance drive. IEEE Trans. Power Electronics. 2002;17:76-83. doi: 10.1109/63.988672
Feiz J., Finch J.W., Metwally H.M.B. A novel switched reluctance motor with multiple teeth per stator pole and comparison of such motors. Electric Power System Research. 1995;34:197-203. doi: 10.1016/0378-7796(95)00978-3
Cobb B.D., Clarkson J.M. A simple procedure for optimising the polymerase chain reaction (PCR) using modified Taguchi methods. Nucleic Acids Res. 1994;22:3801-3805. doi: 10.1093/nar/22.18.3801
Burch G.J., Ferguson C.H., Cartwright G., Kwong F.Y. Application of Taguchi experimental design to the optimisation of a baculovirus expression system. Biochem. Soc. Trans. 1995;23:107S. doi: 10.1042/bst023107s
Jeney C., Dobay O., Lengyel A., Adam E., Nasz I. Taguchi optimisation of ELISA procedures. J. Immunol. Methods. 1999;223:137-146. doi: 10.1016/S0022-1759(98)00185-9
Vijayasarathy S., Datta S. Method: U.S. Patent № 20080200649.
Rogov S.I., Nekrasov A.N. A numerical measure of amino acid residues similarity based on the analysis of their surroundings in natural protein sequences. Protein Engineering. 2001;14:459-463. doi: 10.1093/protein/14.7.459
Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis. 1997;18:2714-2723. doi: 10.1002/elps.1150181505
Danilkovich A.V., Sobolev E.V., Tikhonov D.A., Shadrina T.E., Udovichenko I.P. Molecular dynamic of the complexes of (RADA)₄ - the self-organizing ionic peptides. Mathematical Biology and Bioinformatics. 2011;6:92-101 (in Russ.). doi: 10.17537/2011.6.92
Danilkovich A.V., Sobolev E.V., Tikhonov D.A., Udovichenko I.P., Lipkin V.M. Distinctive H-(RLDL)4-OH peptide complexes potentiate nanostructure self-assembling in water. Dokl. Biochem. Biophys. 2012;443:96-99. doi: 10.1134/S160767291202010X
van Gunsteren W.F., Billeter S.R., Eising A.A., Hünenberger P.H., Krüger P., Mark A.E., Scott W.R.P., Tironi I.G. Biomolecular Simulation: The GROMOS96 Manual and User Guide. Switzerland, Zürich: Vdf Hochschulverlag AG an der ETH Zürich; 1996. 1042 p.
Martenson R.E. Myelin basic protein speciation. In: Experimental Allergic Encephalomyelitis: A Useful Model for Multiple Sclerosis: Progress in Clinical and Biological Research. V. 146. Eds. E.C. Alvord Jr., M.W. Kies, A.J. Suckling. New York: Alan R. Liss, Inc, 1983.
Stepaniak J.A., Gould K.E., Sun D., Swanborg R.H. A comparative study of experimental autoimmune encephalomyelitis in Lewis and DA rats. J. Immunol. 1995;155:2762-2769.
Burns F.R., Li X.B., Shen N., Offner H., Chou Y.K., Vandenbark A.A., Heber-Katz E. Both rat and mouse T cell receptors speciﬁc for the encephalitogenic determinant of myelin basic protein use similar Vα and Vβ chain genes even though the major histocompatibility complex and encephalitogenic determinants being recognized are different. J. Exp. Med. 1989;169:7-39. doi: 10.1084/jem.169.1.27
Lenschow D.J., Walunas T.L., Bluestone J.A. CD28/B7 system of T cell costimulation. Annu. Rev. Immunol. 1996;14:233-258. doi: 10.1146/annurev.immunol.14.1.233