RT info:eu-repo/semantics/article
T1 Five structures of the Pro-Gly dipeptide unveiled by laser ablation rotational spectroscopy
A1 León Ona, Iker
A1 Alonso Alonso, Elena Rita
A1 Municio, Sofía
A1 Mato Domínguez, Sergio
A1 Mendolicchio, Marco
A1 Mata, Santiago
A1 Cabezas, Carlos
A1 Barone, Vincenzo
A1 Alonso Hernández, José Luis
K1 Dipéptido Pro-Gly
K1 Pro-Gly dipeptide
K1 Rotational spectroscopy
K1 Espectroscopia rotacional
K1 Laser
K1 23 Química
AB Herein, for the first time, solid samples of Pro–Gly have been vaporized by laser ablation (LA), and a chirped pulse Fourier transform microwave spectrometer (CP-FTMW) has been employed to explore the broadband rotational spectrum in the 3.0–8.0 GHz range. By integrating experimental data with quantum-chemical computations, we accurately characterized the conformational landscape of this flexible dipeptide, identifying up to five distinct conformers. The N–H⋯N–H hydrogen bond between the amine group of the glycine residue and the amine in the proline ring is highly stabilizing and is present in all conformers. Furthermore, the four most stable conformers exhibit additional stabilizing O–H⋯O[double bond, length as m-dash]C hydrogen bonds between the hydroxyl group and the carbonyl group of proline. We analyzed the key differences between Pro–Gly and Gly-Pro, providing insights into Pro–Gly dipeptide's greater tendency to form β-turn configurations in proteins, in contrast to the Gly-Pro dipeptide's preference for extended conformations. We have illustrated how collisional relaxation distorts the equilibrium conformational distribution, giving rise to missing conformers in the conformational landscape.
PB Royal Society chemistry
SN 1463-9076
YR 2025
FD 2025
LK https://uvadoc.uva.es/handle/10324/80777
UL https://uvadoc.uva.es/handle/10324/80777
LA eng
NO Physical Chemistry Chemical Physics, 2025, vol. 27, n. 44, p. 23645-23654
NO Producción Científica
DS UVaDOC
RD 13-ene-2026