Protocols for determining high-resolution 3D structures of solid proteins are essential for structural studies of fibrils and membrane proteins. Advances in solid-state NMR spectroscopy have led to a multitude of approaches to access restraints and to calculate structures from highly ambiguous data sets. 3D structures at atomic resolution have been derived for several model proteins, as well as for the C-terminal portion of the Het-s prion protein.
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Anja Böckmann (2008) studied this question.
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