| Auteurs | B.J. Bythell, R.P. Dain, S.S. Curtice, J. Oomens, J.D. Steill, G.S. Groenewold, B. Paizs, M.J. van Stipdonk | | Titel | Structure of [M + H - H2O]+ from protonated tetraglycine revealed by tandem mass spectrometry and IRMPD spectroscopy |
| Tijdschrift | The journal of physical chemistry. A |
| Jaargang | 114 |
| Jaar | 2010 |
| Nummer | 15 |
| Pagina's | 5076-5082 |
| ISSN | 10895639 |
| Faculteit | Faculteit der Natuurwetenschappen, Wiskunde en Informatica |
| Instituut/afd. | FNWI: Van 't Hoff Institute for Molecular Sciences (HIMS) |
| Samenvatting | Multiple-stage tandem mass spectrometry and collision-induced dissociation were used to investigate loss of H2O or CH3OH from protonated versions of GGGX (where X = G, A, and V), GGGGG, and the methyl esters of these peptides. In addition, wavelength-selective infrared multiple photon dissociation was used to characterize the [M + H - H2O](+) product derived from protonated GGGG and the major MS3 fragment, [M + H - H2O - 29](+) of this peak. Consistent with the earlier work [Ballard, K. D.; Gaskell, S. J. J. Am. Soc. Mass Spectrom. 1993, 4, 477-481; Reid, G. E.; Simpson, R. J.; O'Hair, R. A. J. Int..J. Mass Spectrom. 1999, 190/191, 209-230000], CID experiments show that [M + H - H2O](+) is the dominant peak generated from both protonated GGGG and protonated GGGG-OMe. This strongly suggests that the loss of the H2O molecule occurs from a position other than the C-terminal free acid and that the product does not correspond to formation of the b(4) ion. Subsequent CID of [M + H - H2O](+) supports this proposal by resulting in a major product that is 29 mass units less than the precursor ion. This is consistent with loss of HN=CH2 rather than loss of carbon monoxide (28 mass units), which is characteristic of oxazolone-type b(n) ions. Comparison between experimental and theoretical infrared spectra ''or a group of possible structures confirms that the [M + H - H2O](+) peak is not a substituted oxazolone but instead suggests formation of an ion that features a five-membered ring along the peptide backbone, close to the ammo terminus. Additionally. transition structure calculations and comparison of theoretical and experimental spectra of the [M + H - H2O - 29](+) peak also support this proposal. |
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