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In structural biology, integrated approaches are often used to investigate complex systems. Membrane proteins, as one example of these systems, are a particularly important class of biomolecules, with their structure, dynamics, and function being dependent on the lipid environment they are embedded in. Solid-state NMR is one of a few techniques able to analyze those biomolecules in their native surroundings and under physiological conditions. Complemented by a variety of different molecular dynamics (MD) simulation-based techniques, many different protein systems can be characterized in detail regarding not only their structure, but also their interactions with other proteins, the environment, or small molecules. In this chapter, we describe a combination of solid-state NMR and MD simulations to characterize the structure and function of membrane proteins, focusing on ion channels and rhomboid proteases as two representative examples, and give an outlook on future perspectives in the field.

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