2006
DOI: 10.1016/j.jasms.2006.04.020
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Isotope-labeled cross-linkers and fourier transform ion cyclotron resonance mass spectrometry for structural analysis of a protein/peptide complex

Abstract: For structural studies of proteins and their complexes, chemical cross-linking combined with mass spectrometry presents a promising strategy to obtain structural data of protein interfaces from low quantities of proteins within a short time. We explore the use of isotope-labeled cross-linkers in combination with Fourier transform ion cyclotron resonance (FTICR) mass spectrometry for a more efficient identification of cross-linker containing species. For our studies, we chose the calcium-independent complex bet… Show more

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Cited by 73 publications
(68 citation statements)
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“…To exploit this information, both peptides that are involved in a crosslink need to be identified. Improvement in mass spectrometry (MS) technology has made this conceivable, in particular high mass precision spectrometers and the development of isotopically coded cross-linkers [3][4][5] . Several studies have proven the general feasibility of this approach 3,[6][7][8][9] .…”
Section: Introductionmentioning
confidence: 99%
“…To exploit this information, both peptides that are involved in a crosslink need to be identified. Improvement in mass spectrometry (MS) technology has made this conceivable, in particular high mass precision spectrometers and the development of isotopically coded cross-linkers [3][4][5] . Several studies have proven the general feasibility of this approach 3,[6][7][8][9] .…”
Section: Introductionmentioning
confidence: 99%
“…These include incorporating an affinity tag into the linker for peptide purification [7][8][9][10][11][12][13][14], as well as various isotope labeling strategies [15][16][17][18][19]. These methods, however, often yield complex, difficult to analyze MS/MS data, as the intermolecular cross-links consist of two peptides covalently joined, and product ions from both peptides are present in the spectrum [20].…”
mentioning
confidence: 99%
“…For example 3,3'-dithiobis(sulfosuccinimidyl propionate) (DTSSP) results in the presence of a 66Da doublet peak and disappearance of the crosslinked peak after addition of reducing agent (17,(19)(20)(21)(22)(23). But only Protein Prospector software considers reporter ions that are naturally embedded in every cross-linked lysine regardless which cross-linker is used.…”
Section: Incomplete Knowledge About the Fragmentation Of Cross-linkedmentioning
confidence: 99%