Abstract
The hydrogen bond consisting of a hydrogen atom positioned asymmetrically between a nitrogen and an oxygen atom $(\mathrm{N}---\mathrm{H}\ensuremath{\cdot}\ensuremath{\cdot}\ensuremath{\cdot}\mathrm{O})$ plays a central role in the structure and functionality of proteins and amino acids. The urea crystal is a simple system in which such a hydrogen bond exists. We have measured Compton profile anisotropies in crystalline urea which reveal subtle modulations linked to this chemical bond. The data presented here have sufficient statistical accuracy to isolate features arising from intermolecular interaction which is weak in urea and consequently difficult to detect experimentally.
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