Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.
Combining powerful simulation methods uncovers the structural and dynamical changes driving G protein activation in atomic detail, revealing the allosteric network that triggers GDP release and reconciling diverse experimental data.
It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.
A fast evolutionary approach to engineer membrane protein kinetic stability yields folded excitatory neurotransmitter transporters and provides insights into their denaturing pathway.
The first structure of the human epithelial sodium channel provides vital insight into the assembly, stoichiometry and molecular mechanism of the ion channel central to sodium homeostasis.
The glycine T-box riboswitch recognizes tRNAgly and senses its aminoacylation state by first interacting with the anticodon region and subsequently probing the 3' end of the ligand using both specific structural elements and conformational dynamics.
Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.
