The hydrogen bond consisting of a hydrogen atom positioned asymmetrically b
etween a nitrogen and an oxygen atom (N-H . . .O) plays a central role in t
he structure and functionality of proteins and amino acids. The urea crysta
l is a simple system in which such a hydrogen bond exists. We have measured
Compton profile anisotropies in crystalline urea which reveal subtle modul
ations linked to this chen-deal bond. The data presented here have sufficie
nt statistical accuracy to isolate features arising from intermolecular int
eraction which is weak in urea and consequently difficult to detect experim
entally.