And then if we have disulfide bonds between our two polypeptide chains, we want to expose them to beta mercapto ethanol to basically break down those covalent interactions. So let's suppose we're dealing with a protein that consists of two individual subunits, two polypeptide chains. We have the green one and we have the blue one. And these red lines are basically our disulfide bonds. So if we take this protein and place it into a solution that contains urea and betama captive ethanol, we're going to denature the structure and separate these two polypeptide chains. So we are going to have a mixture of the green individual chain and the blue individual chain.