The Escherichia coli UraA H+-uracil symporter is a member of the nucleobase/ascorbate transporter (NAT) family of proteins, and is responsible for the proton-driven uptake of uracil. Multiscale molecu
Protein trajectories analyzed in the paper "Computer simulations reveal changes in the conformational space of the transcriptional regulator MosR upon the formation of a disulphide bond an in the coll
Agonist-activated G protein-coupled receptors (GPCRs) interact with GDP-bound G protein heterotrimers (Gαβγ) promoting GDP/GTP exchange, which results in dissociation of Gα from the receptor and Gβγ.
Raw trajectory data for forthcoming publication in MDPI Membranes journal. All simulations have been stripped of waters and ions and contain only YidC protein in 3 different membrane compositions. pe:
