Assembly and stability of a-helical membrane proteins

Grease to grease – this is how one might begin to describe the tendency of hydrophobic stretches in protein amino acid sequences to form transmembrane domains. While this simple rule contains a lot of truth, the mechanisms of membrane protein folding, the insertion of hydrophobic protein domains into the lipid bilayer, and the apparent existence of highly polar residues hydrophobic membrane core are subjects of lively debate – an indica unresolved. Here, we present a historical survey of recent insights from studies into the rules and mechanisms of a-helical membrane protein Biomembranes: more than just a barrier Life would not be possible without biological membranes. Not involving cholesterol, also known as lipid rafts.4 Biomembrane ate under physiological condi-action measurements5,6 and) simulations7 reveal detailed erogeneous structure of lipid his Ph.D. in 2010 from the Ruhr. Alfredo Freites earned his Ph.D. in physics at the Univer