Proteolytic

proteolytic cleavage is breaking of peptide bond

See entire post

... proteins in the vesicle are usually degraded by the lysosomal enzymes. For the protein to enter using endosomes, it would have to either resist proteolytic degradation or prevent fusion of the endosome and lysosome. Further, the protein would have to escape from the endosome if it is to function ...

See entire post

Q1: well, you have answered, why is it so stable, but does that relate to its function? Q2: I don't think the Cys-Cys bonds prevent proteolytic degradation (but I may be wrong), but otherwise it seems OK

See entire post

... Cysteine residues play a valuable role by crosslinking proteins, which increases the rigidity of proteins and also functions to confer proteolytic resistance. Can you help me please?

See entire post

... epitopes, as long as they are intrinsically resistant to the action of pepsin, trypsin, chymotrypsin, and elastase. By flanking such epitopes with proteolytically stable high-affinity tTGase substrates [e.g., the sequence PQPQLPYPQPQLP from gliadin (21)], they could be protected from exposure to ...

See entire post