• Content count

  • Joined

  • Last visited

Community Reputation

0 Neutral

About GRG

  • Rank

Profile Information

  • Favorite Area of Science
    Molecular biology
  1. 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?
  2. 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?
  3. Would it be possible to fragment this protein into peptides by a tryptic in-gel digestion?
  4. 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