Since 1984 nuclear magnetic resonance (NMR) spectroscopy in solution has been available as a second method, besides X-ray diffraction in single crystals, for three-dimensional structure determination of biological macromolecules. In addition, NMR provides a wealth of insights into physicochemical properties of biopolymers, such as internal mobility, conformational equilibria, hydration, and many aspects of the protein folding problem. The focus of this lecture is on this latter facet of NMR in protein research. Particular emphasis is on studies with prion proteins, where the relative stabilities of different polypeptide spatial structures and the mechanisms of interconversion between different conformers have recently attracted interest far beyond the field of protein science.

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