Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding | Semantic Scholar

The results indicate that the thermodynamic stability of monomeric λ repressor within the cell is the same as its stability measured in a simple buffer in vitro, but when the E. coli are placed in a hyperosmotic environment, the in vivo stability is greatly enhanced.

The method uses hydrogen exchange to estimate the stability of microgram quantities of unpurified protein extracts by using matrix-assisted laser desorption/ionization MS and the stabilities of maltose binding protein and monomeric lambda repressor variants determined by SUPREX agree well with stability data obtained from conventional CD denaturation of purified protein.