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The Structure of the Elusive Simplest Dipeptide Gly‐Gly
Author(s) -
Cabezas Carlos,
Varela Marcelino,
Alonso José L.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201702425
Subject(s) - conformational isomerism , dipeptide , intramolecular force , chemistry , glycylglycine , hyperfine structure , quadrupole , hydrogen bond , spectroscopy , crystallography , stereochemistry , peptide , molecule , atomic physics , physics , amino acid , glycine , biochemistry , organic chemistry , quantum mechanics
Among the hundreds of peptide compounds for which conformations have been determined by using different spectroscopic techniques, the structure of the simplest dipeptide glycylglycine (Gly‐Gly) is conspicuously absent. Herein, for the first time, solid samples of Gly‐Gly have been vaporized by laser ablation and three different structures have been revealed in a supersonic expansion by Fourier transform microwave spectroscopy. The intramolecular hydrogen bonding interactions that stabilize the observed forms have been established based on the 14 N nuclear quadrupole hyperfine structure. We have illustrated how conformer interconversion distorts the equilibrium conformational distribution, giving rise to missing conformers in the conformational landscape.