RT info:eu-repo/semantics/article
T1 Unraveling molecular flexibility in prebiotic chemistry: Tiopronin under the lens of rotational spectroscopy and quantum chemistry
A1 Uribe, Lina
A1 Mato, Sergio
A1 Crisci, Luigi
A1 Municio, Sofia
A1 Alonso, Elena R.
A1 Alonso, José L.
A1 León, Iker
A1 Barone, Vincenzo
K1 Biomolecules
K1 Rotational spectroscopy
K1 Molecular Interactions
K1 Gas Phase
K1 amino acid
K1 23 Química
K1 2210 Química Física
K1 2206.07 Espectroscopia Molecular
AB Tiopronin, an N-substituted glycine derivative bearing a thiol group, is structurally related to HS-peptides, species of increasing interest in prebiotic chemistry. These thiol-terminated peptides, plausibly formed through abiotic dry-down reactions of mercaptoacids and amino acids, represent viable alternatives to classical peptide formation pathways. In this work, we investigate the conformational landscape of tiopronin by combining high-resolution microwave spectroscopy with quantum-chemical calculations. The Pisa composite schemes (PCS) were employed to locate low-energy conformers and to compute their ground-state rotational constants, which are directly comparable with experimental values. The accuracy of the theoretical results enables an unambiguous spectral assignment and a reliable structural interpretation, demonstrating the usefulness of an integrated experimental/theoretical approach, provided that the underlying quantum-chemical description captures accurate equilibrium values and vibrational averaging effects. More broadly, this strategy is well suited for the reliable characterization of other flexible prebiotic and biochemical building blocks.
PB ELSEVIER
SN 1386-1425
YR 2025
FD 2025
LK https://uvadoc.uva.es/handle/10324/81567
UL https://uvadoc.uva.es/handle/10324/81567
LA eng
NO SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY 348, pp. 127250
NO Producción Científica
DS UVaDOC
RD 05-feb-2026