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Room‐Temperature Infrared Spectroscopy Combined with Mass Spectrometry Distinguishes Gas‐Phase Protein Isomers
Author(s) -
Fung Y. M. Eva,
Besson Thierry,
Lemaire Joël,
Maitre Philippe,
Zubarev Roman A.
Publication year - 2009
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.200901516
Subject(s) - infrared multiphoton dissociation , mass spectrometry , chemistry , infrared spectroscopy , dissociation (chemistry) , infrared , fourier transform ion cyclotron resonance , analytical chemistry (journal) , spectroscopy , gas phase , chromatography , organic chemistry , physics , quantum mechanics , optics
Differential IR spectra of gas‐phase proteins at room temperature can be obtained by a combination of IR multiphoton dissociation (IRMPD) and FT ion cyclotron resonance mass spectrometry. This new approach yields unique spectra for all‐ L and singly D ‐substituted isomers of the protein Trp‐cage (see depicted differential spectrum) and thus avoids possible unfolding of proteins during IR irradiation that can affect conventional IRMPD measurements.