Abstract
The computer simulation of the distribution of biologically active fragments and bonds which are predicted to be susceptible to the action of endopeptidases of known specificity, hydropathy index and prediction of secondary structures were performed. The average values of hydropathy index calculated for bioactive fragments of selected animal proteins predicted in silica to be released by proteolytic enzymes as well as surroundings of such fragments show that they are hydrophilic. The most frequently occurring structure in the animal proteins bioactive fragments with surroundings is β-strand. There is no preferable secondary structure in the bioactive fragments encrypted in the animal protein sequences. Our findings suggest that the distribution of bioactive fragments may favour their release by proteinases.
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