Studying the mechanism of phase separation in aqueous solutions of globular proteins via molecular dynamics computer simulations.

ABSTRACT: Proteins are the most abundant biomacromolecules in living cells, where they perform vital roles in virtually every biological process. To maintain their function, proteins need to remain in a stable (native) state. Inter- and intramolecular interactions in aqueous protein solutions govern the fate of proteins, as they can provoke their unfolding or association into aggregates. The initial steps of protein aggregation are difficult to capture experimentally, therefore we used molecular dynamics simulations in this study. We investigated the initial phase of aggregation of two different lysozymes, hen egg-white (HEWL) and T4 WT* lysozyme and also human lens γ-D crystallin by using atomistic simulations. We monitored the phase stability of their aqueous solutions by calculating time-dependen

SUBMITTER: Brudar S 

PROVIDER: S-EPMC8210815 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature