Towards biomolecular structure determination by high-resolution solid-state NMR: Assignment of solid peptides

High-resolution solid-state NMR is rapidly evolving into a tool for determi ning the structure of biomolecules in solid phase, thereby opening up avenu es for studying systems which are difficult to access by other methods. In this contribution, we focus on assigning the resonances of a uniformly isot ope-enriched peptide or protein to its primary structure. This represents a first step towards the goal of determining the complete three-dimensional structure of proteins by solid-state NMR. The assignment strategy relies on polarization-transfer experiments involving C-13 and N-15 spins. The prosp ects for structural studies based on such assignments are discussed.