This article reviews recent¹HNMR studies on peptides carried out in the author’s laboratory. Methods for the delineation of hydrogen bonded NH groups are discussed and exemplified by studies of conformationally constrained peptides. The application of concentration dependences ofNMR parameters for NH groups in peptides to the study of peptide aggregation in apolar solvents is considered. Investigations on chemotactic peptide analogs and suzukacillin fragments are briefly summarized. Nuclear-Overhauser effect studies on β-sheet and β-turn conformational models are described.NMR studies on conformational transitions accompanying dissolution of single crystals are illustrated by a study of a peptide containing a -Pro-Pro- segment.