Prediction of exposure degree diagram and sites of limited proteolysis in globular proteins as an approach to computer-aided design of protein bioregulators with prolonged action.
In order to prolong the lifetime of protein bioregulators in blood it is possible to engineer analogs with protected sites of limited proteolysis. To determine the sites, primarily accessible to trypsin-like proteases, a computer procedure has been developed, including a prediction algorithm, to produce the residue diagram of a globular protein and a discriminant algorithm to determine the sites most liable to proteolysis. The accuracy of prediction of amino acid residue exposure is characterised by correlation coefficients between experimental and theoretical exposure values, the coefficients being about 0.7 as calculated for 10 globular proteins. The classification of Arg and Lys residues into two groups, susceptible or insusceptible to protease, has an error percentage of about 25.
D001120:Arginine; D013006:Growth Hormone / Q000378:metabolism; D008239:Lysine; D008962:Models, Theoretical; D010447:Peptide Hydrolases / Q000378:metabolism*; D011384:Proinsulin / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000378:metabolism
D011506:Proteins; D013006:Growth Hormone; D011384:Proinsulin; D001120:Arginine; D010447:Peptide Hydrolases; D014357:Trypsin; D008239:Lysine