Towards the physiologically relevant state with high-resolution solid state NMR

Abstract

Understanding how biomolecules work provides the basis to explain the cellular mechanisms that drive life. Structural biology addresses this challenge by describing the 3D structures of biomolecules using a range of structural techniques, such as Nuclear Magnetic Resonance. This thesis exploits new methods of solid state Nuclear Magnetic Resonance to study, at the atomic level, the structures of membrane proteins in their native environment. This is important because it provides a method to validate the biological relevance of findings obtained with other techniques, and to probe unexpected phenomena that only occur at the cell. The results revealed biologically important features that can only appreciated when proteins are measured within their physiologically relevant environment, as it is shown with the potassium channel KcsA and the antibiotic Nisin. Therefore, the approach presented here can provide critical information for the development of new and better drugs, for example.