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

Abstract

High-resolution solid-state NMR is rapidly evolving into a tool for determining the structure of biomolecules in solid phase, thereby opening up avenues for studying systems which are difficult to access by other methods. In this contribution, we focus on assigning the resonances of a uniformly isotope-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 13C and 15N spins. The prospects for structural studies based on such assignments are discussed.