Confinement and Crowding Effects on Folding of a Multidomain Y-Family DNA Polymerase.

ABSTRACT: Proteins in vivo endure highly various interactions from the luxuriant surrounding macromolecular cosolutes. Confinement and macromolecular crowding are the two major effects that should be considered while comparing the results of protein dynamics from in vitro to in vivo. However, efforts have been largely focused on single domain protein folding up to now, and the quantifications of the in vivo effects in terms of confinements and crowders on modulating the structure and dynamics as well as the physical understanding of the underlying mechanisms on multidomain protein folding are still challenging. Here we developed a topology-based model to investigate folding of a multidomain Y-family DNA polymerase (DPO4) within spherical confined space and in the presence of repulsive and attractive

SUBMITTER: Chu X 

PROVIDER: S-EPMC7258223 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature