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Amino acid sequence10/13/2023 The counting is performed by single amino acids or by a defined polypeptide length. The script sorts polypeptides according to the number of polypeptide occurrences for the defined amino acid sequence or totally at random. Due to software limitations, only the listing of all the available di- (400) and tripeptides (8000) could be visualized. 2 METHODSĪ script was developed which counts the number of polypeptides with a defined length. Homology-based methods for designing protein tertiary structures are a useful consequence of this. The distribution of polypeptides is a good measure of the randomness of changes in the environment ( Lenski, 1998, Bennett et al., 1990) for respective species and it also represents the statistical distribution of selected polypeptides. As a result, the 20 standard amino acids encoded by nucleic acids, which form proteins found in all species, occur in precisely defined quantities in each protein. Furthermore, an innovative approach to the mass analysis of bioinformatic data is presented.Ĭontact: information: Supplementary data are available at Bioinformatics online.Īccording to the evolution theory of life development on Earth ( Darwin, 1859 Kaplan et al., 2000), the process of species' assimilation to the environment has generated genetic changes leading to optimum acclimatization. First, it confirms the Darwinian theory of evolution and second, it opens up opportunities for designing pharmaceuticals among rarely represented short peptide combinations. ![]() It seems interesting that certain short peptide combinations occur relatively rarely or even not at all. We have proved that the distribution of amino acids, dipeptides and tripeptides is statistical which confirms that the evolutionary biodiversity development model is subject to the theory of independent events. Due to the distinct metabolic pathways of amino acid syntheses and their physicochemical properties, the quantities of subpeptides in proteins vary. UNIPROT–TREMBL contains protein sequences associated with computationally generated annotations and large-scale functional characterization. Motivation: The article presents results of the listing of the quantity of amino acids, dipeptides and tripeptides for all proteins available in the UNIPROT–TREMBL database and the listing for selected species and enzymes.
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