Spinster (Spns) transporters are critical for lipid transport across the cellular membrane, a process that regulates growth and migration of the cell in human body. Yet, the details of their molecular mechanism which could potentially help drug hunters, have remained elusive. Guided by DEER measurements and site-directed mutagenesis performed in Dr. Reza Dastvan's lab (St Louis University), molecular dynamics simulations by the Center's researchers were used to identify unknown conformational states of a Spns transporter (HnSpns). This systematic study reveals conserved proton-binding switches that modulate the structural transitions of the transporter, and thereby shed light on its proton-coupled mechanism. The simulations were performed with NAMD and analyzed by VMD. Read more in a Nature Communications.