Selection of amino acid parameters for Fourier transform-based analysis of proteins
Laboratory for Multidisciplinary Research 180/2, Institute of Nuclear Sciences Vinca PO Box 522, 11001 Belgrade. Yugoslavia
E-mail: elazovij{at}ubbg.etf.bg.ac.yu
Fourier analysis of the parametric profile of a sequence for the detection and localization of the structural motifs that are characteristic for biologically related proteins has been proposed. In order to select parameters that are most appropriate for this analysis, the informational capacity of 226 physicochemical, thermodynamic, structural and statistical amino acid parameters was analyzed. Based on the results, obtained for the four functionally unrelated protein model groups (lysozyme c, HIV-I gp120, tubulin and tau proteins, and steroid hormone receptors), the electronion interaction potential has been selected as the unique amino acid property that can be used in Fourier transform-based analysis of proteins, independently of their biological function.
Received on March 26, 1996; revised on June 6, 1996; accepted on June 18, 1996
This article has been cited by other articles:
![]() |
K. A. Selz, A. J. Mandell, M. F. Shlesinger, V. Arcuragi, and M. J. Owens Designing Human m1 Muscarinic Receptor-Targeted Hydrophobic Eigenmode Matched Peptides as Functional Modulators Biophys. J., March 1, 2004; 86(3): 1308 - 1331. [Abstract] [Full Text] [PDF] |
||||
