Final Report Summary - PROTDYN2FUNCTION (Functional protein dynamics studied by solution- and solid-state NMR spectroscopy)
In terms of applications, we have characterized chaperones and membrane proteins. Chaperones are “helper proteins” which assist poorly soluble/aggregation-prone/misfolded protein in remaining in solution or refolding. We have provided insight into a large (ca. 1 MDa) chaperone of the Hsp60 family, its conformational states, its interaction with unfolded proteins, and its ATP-driven large-scale rearrangements. Furthermore we have provided detailed insight into the mechanisms by which highly aggregation-prone mitochondrial membrane proteins are transported across the mitochondrial inter-membrane space. Lastly, we have studied the dynamics and interactions of membrane proteins in detergent, and how detergents alter membrane protein structure.
Taken together, this project has gone from the development of advanced NMR methods and integration of various methods, to challenging biological questions, particularly in the chaperone field.