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. |
---|---|
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) |
References: | Mol Cell Proteomics. 2011 May;10(5):O111.009456. (PMID: 21393638) J Proteome Res. 2011 Sep 2;10(9):4088-104. (PMID: 21740066) J Am Soc Mass Spectrom. 1993 Nov;4(11):882-93. (PMID: 24227532) Nat Methods. 2007 Sep;4(9):709-12. (PMID: 17721543) Rapid Commun Mass Spectrom. 2008 May;22(10):1563-6. (PMID: 18421754) Nat Methods. 2007 Nov;4(11):923-5. (PMID: 17952086) Anal Chem. 2003 Apr 1;75(7):1699-705. (PMID: 12705605) Anal Chem. 1999 Oct 1;71(19):4250-3. (PMID: 10517147) Mol Cell Proteomics. 2004 Dec;3(12):1154-69. (PMID: 15385600) J Am Soc Mass Spectrom. 2002 Jun;13(6):659-69. (PMID: 12056566) Biochim Biophys Acta. 2010 Feb;1800(2):80-95. (PMID: 19647043) J Am Soc Mass Spectrom. 2003 Jul;14(7):777-84. (PMID: 12837600) Biochim Biophys Acta. 2004 Jul 6;1673(1-2):13-28. (PMID: 15238246) J Proteome Res. 2010 Dec 3;9(12):6786-94. (PMID: 20873877) J Mass Spectrom. 2004 Apr;39(4):402-11. (PMID: 15103654) Mol Cell Proteomics. 2009 May;8(5):904-12. (PMID: 19131326) Anal Chem. 2011 Jul 1;83(13):5442-6. (PMID: 21619048) Sci STKE. 2005 Nov 29;2005(312):re13. (PMID: 16317114) Eur J Biochem. 2001 Oct;268(19):5001-10. (PMID: 11589691) J Proteome Res. 2010 Feb 5;9(2):1138-43. (PMID: 19938873) Mol Cell Proteomics. 2009 Dec;8(12):2759-69. (PMID: 19828875) J Proteome Res. 2006 Mar;5(3):695-700. (PMID: 16512685) J Proteome Res. 2004 May-Jun;3(3):621-6. (PMID: 15253445) J Mass Spectrom. 2005 Apr;40(4):430-43. (PMID: 15838939) J Proteome Res. 2009 Jun;8(6):3176-81. (PMID: 19338334) Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9528-33. (PMID: 15210983) Proteomics. 2011 Jul;11(14):2931-5. (PMID: 21656683) Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8894-9. (PMID: 19458039) J Am Soc Mass Spectrom. 2001 Oct;12(10):1106-13. (PMID: 11605972) J Mass Spectrom. 2000 Sep;35(9):1069-90. (PMID: 11006601) |
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 |
كن أول من يترك تعليقا!