Abstract

Integral membrane proteins (IMPs) are encoded by 20-30 % of genes in a genome and provide key functions in the cell. Due to their hydrophobic nature, they are structurally and biochemically difficult to study. Traditionally, IMPs have been extracted using detergents which are a poor mimic of the lipid membrane and have been shown to denature membrane proteins. However, newly developed lipid-nanodisc approaches enable structural and functional studies of IMPs in a detergent-free, near-native membrane environment. Recent studies have also focused on further developments of novel membrane mimetics including novel expression and stabilisation strategies to overcome the remaining methodological challenges posed by avariety of IMPs. These technologies have delivered fascinating new insights into membrane protein structure, dynamics and function within the last years. This conference will bring together researchers developing and applying these new methodologies. In addition to providing a forum to exchange the latest developments in the field, the conference provides excellent opportunities for early-career scientist in the field to learn all aspects of a variety of tools to study the structure and function of membrane proteins.