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Investigation of the structural and functional relationships of oneogene protiens

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posted on 2024-11-23, 03:33 authored by Elena PirogovaElena Pirogova, John Fang, M Akay, Irena CosicIrena Cosic
Proteins are the biomolecular workhorses driving the most biological processes in any living organism. These processes are based on selective interactions between particular proteins. So far, the rules governing the coding of the protein's biological function, i.e. its ability to selectively interact with other biomolecules, have not been elucidated. The resonant recognition model (RRM) is a novel physicomathematical approach established to analyze the interaction between a protein and its target. The RRM assumes that the specificities of protein interactions are based on the resonant electromagnetic energy transfer at the specific frequency for each interaction. One of the main applications of this model is to predict the location of a protein's biological active site(s) using digital signal processing. This paper incorporates the continuous wavelet transform (CWT) into the RRM to predict the active sites, for a chosen protein example. We have investigated the oncogene functional group using digital signal analysis methods, in particular Fourier transform and CWT; determined oncogenes' characteristic frequency and functional active sites; and performed the design of the peptide analogous. The results obtained provide new insights into the structure-function relationships of the analyzed oncogene protein family.

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    ISSN - Is published in 00189219

Journal

Proceedings of the IEEE

Volume

90

Issue

12

Start page

1859

End page

1867

Total pages

9

Publisher

IEEE

Place published

USA

Language

English

Copyright

© 2002 IEEE. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from the IEEE.

Former Identifier

2002000383

Esploro creation date

2020-06-22

Fedora creation date

2009-07-17

Open access

  • Yes

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