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|Author(s):||Pedatsur Neta; Quan-Long Pu; Lisa E. Kilpatrick; Xiaoyu Yang; Stephen E. Stein;|
|Title:||Dehydration vs. Deamination of N-Terminal Glutamine in Collision-Induced Dissociation of Protonated Peptide Ions|
|Published:||August 11, 2006|
|Abstract:||Some of the most prominent neutral losses in peptide ion fragmentation are the loss of ammonia and water from N-terminal glutamine. These processes are studied by electrospray ionization mass spectrometry in singly- and doubly-protonated peptide ions undergoing collision-induced dissociation in a triple quadrupole and in an ion trap instrument. For this study, four sets of peptides were synthesized: (a) QLLLPLLLK and similar peptides with K replaced by R, H, or L, and Q replaced by a number of amino acids, (b) QLnK (n = 0, 1, 3, 5, 7, 9, 11), (c) QLnR (n = 0, 1, 3, 5, 7, 9), and (d) QLn (n = 1, 2, 3, 4, 8). The results for QLLLPLLLK and QLLLPLLLR show that the singly protonated ions undergo loss of ammonia and to a smaller extent loss of water, whereas the doubly protonated ions undergo predominantly loss of water. The fast fragmentation next to P (forming the y5 ion) occurs to a larger extent than the neutral losses from the singly protonated ions but much less than the water loss from the doubly protonated ions. The results from these and other peptides show that, in general, when N-terminal glutamine peptides have no mobile protons , that is, the number of charges on the peptide is no greater than the number of basic amino acids (K, R, H), deamination is the predominant neutral loss fragmentation, but when mobile protons are present the predominant process is the loss of water. Both of these processes are faster than backbone fragmentation at the proline.|
|Citation:||Journal of the American Society for Mass Spectrometry|
|Pages:||pp. 27 - 36|
|Keywords:||collision induced dissociation,mass spectrometry,peptides,proteomics|
|PDF version:||Click here to retrieve PDF version of paper (441KB)|