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Cover Picture: Exploring the Mechanism of IR–UV Double‐Resonance for Quantitative Spectroscopy of Protonated Polypeptides and Proteins (Angew. Chem. Int. Ed. 23/2013)
Author(s) -
Nagornova Natalia S.,
Rizzo Thomas R.,
Boyarkin Oleg V.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201303560
Subject(s) - protonation , spectroscopy , chemistry , infrared spectroscopy , resonance (particle physics) , absorption spectroscopy , molecule , ion , resonance raman spectroscopy , nuclear magnetic resonance spectroscopy , photochemistry , crystallography , stereochemistry , raman spectroscopy , organic chemistry , atomic physics , physics , optics , quantum mechanics
Determination of the 3D structures … … of large molecules challenges spectroscopy to perform better. In their Communication on page 6002 ff. O. V. Boyarkin et al. use IR–UV double‐resonance cold‐ion spectroscopy for conformational assignment of the electronic spectra of a protonated decapeptide and for measurements of absolute absorption cross‐sections of vibrational transitions in this species. The limitations of the IR–UV double‐resonance approach are illustrated by measuring the gas‐phase IR spectrum of a cold, protonated intact protein.