why do we denature proteins before mass spectroscopy? I'm learning about mass spectroscopy in particular the use of it in analyzing protein structure. they said we have to use trypsinolysis to cut the protein to segments, but why does the protein have to be denatured first before trypsinolysis?
Trypsin is an enzyme, and has to bind to a target protein in a specific way in order to be active. Without first denaturing your protein, most of the protein will be conformationally/sterically inaccessible to trypsin, and you will only get partial digestion (or maybe no digestion at all).