Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly.

ABSTRACT: The effects of detergent sodium dodecyl sulfate (SDS) on protein structure and dynamics are fundamental to the most common laboratory technique used to separate proteins and determine their molecular weights: polyacrylamide gel electrophoresis. However, the mechanism by which SDS induces protein unfolding and the microstructure of protein-SDS complexes remain largely unknown. Here, we report a detailed account of SDS-induced unfolding of two proteins-I27 domain of titin and β-amylase-obtained through all-atom molecular dynamics simulations. Both proteins were found to spontaneously unfold in the presence of SDS at boiling water temperature on the time scale of several microseconds. The protein unfolding was found to occur via two distinct mechanisms in which specific interactions of indivi

SUBMITTER: Winogradoff D 

PROVIDER: S-EPMC7291819 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature