Pathway for unfolding of ubiquitin in sodium dodecyl sulfate, studied by capillary electrophoresis

The complexes formed by a small protein, ubiquitin (UBI), and a negatively charged surfactant, sodium dodecyl sulfate (SDS), are characterized by using capillary electrophoresis (CE), circular dichroism (CD) and amide hydrogen-deuterium exchange (HDX). The study has helped in understanding the formation of the protein-SDS complexes formed during SDS polyacrylamide gel electrophoresis and has provided a new tool for studying proteins and detergents.