Protein-DNA recognition is a central biological process that governs the life of cells. A protein will often undergo a conformational transition to form the functional complex with its …
Approximately three-fourths of eukaryotic proteins are composed of multiple independently folded domains. However, much of our understanding is based on single domain proteins or …
During DNA polymerization, the Y-family DNA polymerases are capable of bypassing various DNA damage, which can stall the replication fork progression. It has been well …
X Chu, Z Suo, J Wang - Journal of chemical theory and …, 2020 - ACS Publications
Proteins in vivo endure highly various interactions from the luxuriant surrounding macromolecular cosolutes. Confinement and macromolecular crowding are the two major …
DNA polymerase (pol) processivity, ie, the bases a polymerase extends before falling off the DNA, and activity are important for copying difficult DNA sequences, including simple …
J Guyette, B Evangelista, SA Tatulian, K Teter - Biochemistry, 2019 - ACS Publications
Protein disulfide isomerase (PDI) is a redox-dependent protein with oxidoreductase and chaperone activities. It is a U-shaped protein with an abb′ xa′ structural organization in …
The way in which multidomain proteins fold has been a puzzling question for decades. Until now, the mechanisms and functions of domain interactions involved in multidomain protein …
The DinB homolog polymerase (Dbh) is a member of the Y-family of translesion DNA polymerases that can synthesize using a damaged DNA template. Since Dbh comes from …
BA Maxwell, C Xu, Z Suo - Biochemistry, 2014 - ACS Publications
Numerous kinetic, structural, and theoretical studies have established that DNA polymerases adjust their domain structures to enclose nucleotides in their active sites and …