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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
Author(s) -
Rodionov M.A.,
Galaktionov S.G.,
Akhrem A.A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80327-7
Subject(s) - proteolysis , protease , proteases , globular protein , trypsin , residue (chemistry) , chemistry , protease inhibitor (pharmacology) , biochemistry , biology , enzyme , immunology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
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.