Specific features of enteropeptidase hydrolysis of chimeric proteins at the specific linker (Asp)4Lys depending on the refolding conditions
Refolding from inclusion bodies of chimeric proteins containing the enteropeptidase-specific linker (Asp)4Lys was carried out. It was shown that, depending on the refolding conditions, chimeric proteins function as substrates or inhibitors of the enteropeptidase. The efficiency of the enteropeptidase hydrolysis of chimeric proteins containing the (Asp)4Lys linker may depend not only on the amino acid sequence of the protein binding site for the enzyme but also on the site’s conformation.
Key wordschimeric proteins folding limited proteolysis enteropeptidase
protein of the VP1 region of the hepatitis A virus
protease of the human immunodeficiency virus
protease covalently joined with reverse transcriptase of the human immunodeficiency virus
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