In this chapter, typical peptide‐specific properties are highlighted, including lack of secondary and tertiary structure, high solvent exposure, small core volume, natural isotope abundance, and low spectral crowding. NMR experiments and structure calculation protocols developed for the investigation of peptides with distinct preferred conformations, as observed in constrained (cyclic or N‐methylated) peptides, are also presented. Many of these approaches differ greatly from NMR experiments and structure calculation strategies designed for studying proteins, as demonstrated by the following:
Different types of ROESY experiments, methods for the determination of coupling constants, as well as an overview of residual dipolar coupling‐based peptide NMR studies and the alignment media used therein are described. The impact of peptide flexibility for conformational studies is discussed in the context of distance and dihedral restraints. Furthermore, a common peptide structure calculation protocol including distance geometry and molecular dynamics calculations is presented.