دورية أكاديمية
Evaluation of front-end higher energy collision-induced dissociation on a benchtop dual-pressure linear ion trap mass spectrometer for shotgun proteomics.
| العنوان: | Evaluation of front-end higher energy collision-induced dissociation on a benchtop dual-pressure linear ion trap mass spectrometer for shotgun proteomics. |
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| المؤلفون: | Bereman MS; Department of Genome Sciences, University of Washington, Seattle, Washington 98195, USA., Canterbury JD, Egertson JD, Horner J, Remes PM, Schwartz J, Zabrouskov V, MacCoss MJ |
| المصدر: | Analytical chemistry [Anal Chem] 2012 Feb 07; Vol. 84 (3), pp. 1533-9. Date of Electronic Publication: 2012 Jan 12. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370536 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-6882 (Electronic) Linking ISSN: 00032700 NLM ISO Abbreviation: Anal Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Chemical Society. |
| مواضيع طبية MeSH: | Mass Spectrometry/*instrumentation , Proteomics/*instrumentation, Animals ; Caenorhabditis elegans/metabolism ; Glycopeptides/analysis ; Mass Spectrometry/methods ; Phosphopeptides/analysis ; Pressure ; Software |
| مستخلص: | We report the implementation of front-end higher energy collision-induced dissociation (fHCD) on a benchtop dual-pressure linear ion trap. Software and hardware modifications were employed, described in detail vide-infra, to allow isolated ions to undergo collisions with ambient gas molecules in an intermediate multipole (q00) of the instrument. Results comparing the performance of fHCD and resonance excitation collision-induced dissociation (RE-CID) in terms of injection time, total number of scans, efficiency, mass measurement accuracy (MMA), unique peptide identifications, and spectral quality of labile modified peptides are presented. fHCD is approximately 23% as efficient as RE-CID, and depending on the search algorithm, it identifies 6.6% more or 15% less peptides (q < 0.01) from a soluble whole-cell lysate ( Caenorhabditis elegans ) than RE-CID using Mascot or Sequest search algorithms, respectively. fHCD offers a clear advantage for the analysis of phosphorylated and glycosylated (O-GlcNAc) peptides as the average cross-correlation score (XCorr) for spectra using fHCD was statistically greater (p < 0.05) than for spectra collected using RE-CID. (© 2011 American Chemical Society) |
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| معلومات مُعتمدة: | P41 GM103533 United States GM NIGMS NIH HHS; U01 HG004263-04 United States HG NHGRI NIH HHS; R01 DK069386 United States DK NIDDK NIH HHS; T32 HG000035-13 United States HG NHGRI NIH HHS; U01 HG004263 United States HG NHGRI NIH HHS; P41 RR011823 United States RR NCRR NIH HHS; R01 DK069386-07 United States DK NIDDK NIH HHS; F31 AG037265 United States AG NIA NIH HHS; P41 RR011823-10 United States RR NCRR NIH HHS; T32 HG000035 United States HG NHGRI NIH HHS; F31 AG037265-02 United States AG NIA NIH HHS |
| المشرفين على المادة: | 0 (Glycopeptides) 0 (Phosphopeptides) |
| تواريخ الأحداث: | Date Created: 20111224 Date Completed: 20120618 Latest Revision: 20211021 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC3277647 |
| DOI: | 10.1021/ac203210a |
| PMID: | 22192247 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-6882 |
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| DOI: | 10.1021/ac203210a |