Unveiling the Neutral Forms of Glutamine.

Neutral glutamine has been evaporated by laser ablation of its solid sample to seed a rare gas carrier prior to a supersonic expansion and proved by Fourier transform microwave techniques. We report on three distinct neutral conformers that show a singular non-interacting and flexible amide sidechain in contrast with the other proteinogenic aliphatic amino acids. It could explain the essential biological role of glutamine as a nitrogen source, and its unique ability to form a variety of hydrogen bonds with peptide backbones. Common computational methods fail to predict the delicate balance of intramolecular interactions controlling the geometry of the most stable conformer. The spectroscopic data here reported can be used to benchmark novel computational methods in quantum chemistry.
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