The aim is to acquire a detailed understanding of the mechanisms of water and glycerol selectivity and transport as well as proton exclusion and how they differ between subclasses of AQPs, employing an interdisciplinary approach centered on neutron protein crystallography.
The most recent techniques for membrane protein overproduction to structure determination will be exploited, as allowed by the assembled interdisciplinary team.
Promising initial results include crystals of the human aquaglyceroporins AQP7 and AQP10. Positive results from the initiative will decipher the selectivity and transport mechanisms of human aquaglyceroporins, shed further light on proton exclusion in orthodox AQPs, and provide new methods for neutron crystallography for membrane proteins, which will represent a major contribution to basic bioscience with implications beyond physiology and biomedicine.
