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 sidechai...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2019-11, Vol.58 (45), p.16002-16007
Main Authors: León, Iker, Alonso, Elena R., Mata, Santiago, Cabezas, Carlos, Alonso, Jose Luis
Format: Article
Language:English
Subjects:
Aliphatic compounds
amino acid
Amino acids
Computer applications
Fourier transforms
FTMW spectroscopy
Glutamine
Hydrogen bonding
Hydrogen bonds
Laser ablation
non-covalent interactions
Organic chemistry
Quantum chemistry
Rare gases
rotational spectroscopy
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Summary: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. Three neutral forms of the proteinogenic glutamine, intimately connected to its biological functions, have been generated by laser ablation and structurally characterized by microwave spectroscopy.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201907222