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Table 1.
Identity rate, as a percent of of identical residues in the whole pool of
amino acids.
Positions
Total
Percentage content
Identic
1313
49,21%
89,09% in total pool
among identic
507
19% identic pool
38,61% in total pool
Semihomologous
980
36,73%
Deletions
375
14%
On the basis of the consensus sequence, estimating the general parameters
characterizing the whole family of proteins (E-spectrins) is possible. The consensus
sequence is a perfect average of results, it decreases considerably their amount and gives a
reliable piece of information about probable location of amino acid residues, that are
responsible for forming very important structural and functional units of proteins.
3. Summary
The B.S. Thesis, that was the basis of writing this paper, concerns also a detailed analysis
of amino acid composition of the E-spectrin protein family, as well as the analysis of
genetic relations among amino acid residues occurring several positions. Using the
algorithm of genetic semihomology makes the analysis of the primary structure of proteins
easier and more reliable. Such analysis of the protein primary structure is only an
introduction to complete examinations of structure and functions of proteins; mechanism of
variability of proteins, location of gaps, mutational correlations at particular positions and
their contact with each other, evolutionary pathways and future evolutionary changes of
protein structure.
Currently, the research within the primary structure of members of the E-spectrin
protein family is continued. The research concerns improving the features of the algorithm
of genetic semihomology (ascribing concrete values of probability to particular changes of
amino acid residues within several positions) and testing it using the E-spectrin protein
family. The studies will also probably concern detailed examinations of the evolutionary
pathways (in the past and in the future) within E-spectrins.
References
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[2]
Broderick M.J.F, Winder S.J.; “Towards a Complete Atomic Structure of Spectrin Family Proteins”,
Journal of Structural Biology 137, 184-193, 2002.
[3]
Djinovic-Carugo K., Gautel M., Ylanne J., Young P.; “The spectrin repeat: a structural platform for
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[4]
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domains”, FEBS Letters, Vol. 513, Issue 1, 98-106, 2002.
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