Structural data obtained from X-ray crystallography as well as from NMR spectroscopy has clearly provided evidences that many proteins have intrinsic disorder either locally or globally. Emerging evidence suggests that these small or large-scale deformations occur at various time scales and provide important hints for the regulatory mechanisms of the proteins. In this view protein plasticity is becoming an important parameter for molecular organization and recognition. In this project, we aim to probe the molecular dynamics of membrane proteins and protein fibrils at residue level and atomic detail using novel solid-state NMR methods. Using a combination of NMR pulse schemes that probe relaxation and anisotropic interactions in a residue-specific level, our goal is to understand the molecular level assemblies of fibril proteins and various intermediate states of the fibrilization process. The same methods will be used to elucidate the protein plasticity when embedded in lipid bilayers, providing novel possibilities to probe signaling and cellular uptakes in a functional state.
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