000200080 001__ 200080 000200080 005__ 20190316235931.0 000200080 0247_ $$2doi$$a10.1021/ja5053544 000200080 022__ $$a1520-5126 000200080 02470 $$2ISI$$a000338692700014 000200080 037__ $$aARTICLE 000200080 245__ $$aIdentification of Tyrosine-Phosphorylated Peptides Using Cold Ion Spectroscopy 000200080 260__ $$bAmer Chemical Soc$$c2014$$aWashington 000200080 269__ $$a2014 000200080 300__ $$a4 000200080 336__ $$aJournal Articles 000200080 520__ $$aThe accurate and unambiguous detection of post-translational modifications in proteins and peptides remains a challenging task. We report here the use of cold ion spectroscopy for the identification of phosphorylated tyrosine residues in peptides. This approach employs the wavelength-specific UV fragmentation of cryogenically cooled protonated peptides in the gas phase. In addition to the appearance of specific photofragments, the phosphorylation of tyrosine induces large spectral shifts of the peptide electronic band origins. Quantum chemical calculations and experiments together suggest a certain generality of the use of such shifts in the spectroscopic identification of phosphotyrosines. The enhanced selectivity offered by the joint application of wavelength-specific fragmentation and mass spectrometry of cold molecules can also be used in the identifications of aromatic residues in protonated peptides and, potentially, of other UV-absorbing groups in a variety of large polyatomic ions. 000200080 700__ $$0246389$$g221741$$aKopysov, Vladimir 000200080 700__ $$0242816$$g176885$$aNagornova, Natalia S. 000200080 700__ $$aBoyarkin, Oleg V.$$g104570$$0242817 000200080 773__ $$tJournal of the American Chemical Society$$q140624084934005 000200080 8564_ $$uhttps://infoscience.epfl.ch/record/200080/files/ja5053544.pdf$$zPublisher's version$$s629843$$yPublisher's version 000200080 909C0 $$xU10106$$0252096$$pLCPM 000200080 909CO $$ooai:infoscience.tind.io:200080$$qGLOBAL_SET$$pSB$$particle 000200080 917Z8 $$x104570 000200080 937__ $$aEPFL-ARTICLE-200080 000200080 973__ $$rNON-REVIEWED$$sPUBLISHED$$aEPFL 000200080 980__ $$aARTICLE