My name is Eric Tam and I'm a biochemistry PhD student here at the
University of British Columbia in Vancouver, Canada. I was recommended this
address by the Nucleic Acids and Protein Services (NAPS) of UBC. I have a
question regarding biotin modification and trypsin digestion.
If a primary amine is modified by a biotinylation reagent (say from Pierce),
is trypsin able to cleave at this modified site? The reason I'm asking this
is that I'm proposing to biotinylate a protein to identify surface exposed
Lys residues. I then want to be able to digest the protein and sequence
only the biotinylated peptides.
Your response is greatly appreciated,
Eric Tam