%0 Journal Article
%A Leroux, Juliette
%A Ortiz Mahecha, Carlos Andres
%A Schubert, Kaja
%A Trinter, Florian
%A Unger, Isaak
%A Schwob, Lucas
%A Bari, Sadia
%T Tautomerism of a backbone protonated peptide revealed by soft X-ray action spectroscopy
%J Physical chemistry, chemical physics
%V 27
%@ 1463-9076
%C Cambridge
%I RSC Publ.
%M PUBDB-2025-00794
%P 8320 - 8326
%D 2025
%X The structure and reactivity of peptides can be influenced by their protonation state. Notably, protonation of the backbone can induce structural changes, such as tautomerism, shifting from the stable keto form to the enol form. This phenomenon, particularly in the backbone protonated peptide acetyl-pentaglycine, was examined using a combination of soft X-ray action spectroscopy at the nitrogen K-edge and theoretical calculations based on density functional theory (DFT). We identified a resonance at 400 eV that can be clearly attributed to π<sup>*</sup>(C[double bond, length as m-dash]N) transitions, linked exclusively to the enol form, as no keto form structures could replicate this resonance. These findings enhanced our understanding of the effect of protonation on the structure of peptides and could be employed for future dynamic studies. 
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 40183417
%U <Go to ISI:>//WOS:001459353700001
%R 10.1039/d5cp00506j
%U https://bib-pubdb1.desy.de/record/623828