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. Therefore, a central theme of this workshop is highlighting the importance of lipids in MP research and how they can be preserved.
Various experimental and computational tools, including novel expression and stabilisation strategies, have been developed to overcome the challenges posed by a variety of MPs. These technologies have delivered spectacular insights into membrane-protein structure, dynamics and function within the last few 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.
- New mimetics for MP research
- Expression and purification of MPs
- Biophysics of lipid bilayers
- X-ray methods for structural research of MPs
- Binding proteins for structural and functional MP research
- Advances in cryo-EM for small MPs
- Cryo-EM and cryo-tomography on large MP complexes
- Mass spectrometry and single-molecule FRET on MPs
- Computational methods to probe structure and dynamics of MPs