GRG

I have a mature protein that has been proteolytically cleaved at its N-terminus. I wonder if this degraded protein may subsequently undergo acetylation at its (new) N-terminus? Can a mature protein be acetylated?

Would the protease-resistant core be digestible by trypsin if I wanted to digest the protein into peptides by the means of a tryptic in-gel digest ahead of sending it for analysis by mass spectrometry?

Would it be possible to fragment this protein into peptides by a tryptic in-gel digestion?

Hello there, I wonder if anyone might be able to explain to me what a protease-resistant core of a protein is, specifically in regard to its amino acid sequence (does it lack protease specific amino acids, e.g. K and R in the case of trypsin?) and means of formation? Many thanks