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111.
Jackson SN Moyer SC Woods AS 《Journal of the American Society for Mass Spectrometry》2008,19(10):1535-1541
Electrospray mass spectrometry (ESI-MS) has become the tool of choice for the study of noncovalent complexes. Our previous
work has highlighted the role of phosphorylated amino acid residues in the formation of noncovalent complexes through electrostatic
interaction with arginine residues’ guanidinium groups. In this study, we employ tandem mass spectrometry to investigate the
gas-phase stability and dissociation pathways of these noncovalent complexes. The only difference in the three phosphopeptides
tested is the nature of the phosphorylated amino acid residue. In addition the absence of acidic residues and an amidated
carboxyl terminus insured that the only negative charge came from the phosphate, which allowed for the comparison of the noncovalent
bond between arginine residues and each of the different phosphorylated residues. Dissociation curves were generated by plotting
noncovalent complex ion intensities as a function of the nominal energy given to the noncovalent complex ion before entering
the collision cell. These results showed that noncovalent complexes formed with phosphorylated tyrosine were the most stable,
followed by serine and threonine, which had similar stability. 相似文献
112.
Moyer SC VonSeggern CE Cotter RJ 《Journal of the American Society for Mass Spectrometry》2003,14(6):581-592
An investigation of phosphate loss from sodium-cationized phosphotyrosine containing peptide ions was conducted using liquid infrared (2.94 microm) atmospheric pressure matrix-assisted laser desorption/ionization (AP MALDI) coupled to an ion trap mass spectrometer (ITMS). Previous experiments in our laboratory explored the fragmentation patterns of protonated phosphotyrosine containing peptides, which experience a loss of 98 Da under CID conditions in the ITMS. This loss of 98 Da is unexpected for phosphotyrosine, given the structure of its side chain. Phosphate loss from phosphotyrosine residues seems to be dependent on the presence of arginine or lysine residues in the peptide sequence. In the absence of a basic residue, the protonated phosphotyrosine peptides do not undergo losses of HPO(3) (Delta 80 Da) nor HPO(3) + H(2)O (Delta 98 Da) in their CID spectra. However, sodium cationized phosphotyrosine containing peptides that do not contain arginine or lysine residues within their sequences do undergo losses of HPO(3) (Delta 80 Da) and HPO(3) + H(2)O (Delta 98 Da) in their CID spectra. 相似文献
113.