دورية أكاديمية
MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS.
العنوان: | MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS. |
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المؤلفون: | Rincon Pabon JP; Faculty of Biology, Medicine and Health, Division of Molecular and Cellular Function, The University of Manchester, Manchester M13 9PT, U.K.; Manchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester M1 7DN, U.K., Akbar Z; Faculty of Biology, Medicine and Health, Division of Molecular and Cellular Function, The University of Manchester, Manchester M13 9PT, U.K.; Manchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester M1 7DN, U.K., Politis A; Faculty of Biology, Medicine and Health, Division of Molecular and Cellular Function, The University of Manchester, Manchester M13 9PT, U.K.; Manchester Institute of Biotechnology, University of Manchester, Princess Street, Manchester M1 7DN, U.K. |
المصدر: | Journal of the American Society for Mass Spectrometry [J Am Soc Mass Spectrom] 2024 Jul 03; Vol. 35 (7), pp. 1383-1389. Date of Electronic Publication: 2024 Jun 06. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: ACS Publications Country of Publication: United States NLM ID: 9010412 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-1123 (Electronic) Linking ISSN: 10440305 NLM ISO Abbreviation: J Am Soc Mass Spectrom Subsets: MEDLINE |
أسماء مطبوعة: | Publication: 2020- : Washington, DC : ACS Publications Original Publication: New York, NY : Elsevier, c1990- |
مواضيع طبية MeSH: | Membrane Proteins*/chemistry , Membrane Proteins*/analysis , Hydrogen Deuterium Exchange-Mass Spectrometry*/methods, Proteomics/methods ; Amino Acid Sequence ; Peptides/chemistry ; Peptides/analysis |
مستخلص: | Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has evolved as an essential technique in structural proteomics. The use of ion mobility separation (IMS) coupled to HDX-MS has increased the applicability of the technique to more complex systems and has been shown to improve data quality and robustness. The first step when running any HDX-MS workflow is to confirm the sequence and retention time of the peptides resulting from the proteolytic digestion of the nondeuterated protein. Here, we optimized the collision energy ramp of HDMS E experiments for membrane proteins using a Waters SELECT SERIES cIMS-QTOF system following an HDX workflow using Phosphorylase B, XylE transporter, and Smoothened receptor (SMO) as model systems. Although collision energy (CE) ramp 10-50 eV gave the highest amount of positive identified peptides when using Phosphorylase B, XylE, and SMO, results suggest optimal CE ramps are protein specific, and different ramps can produce a unique set of peptides. We recommend cIMS users use different CE ramps in their HDMS E experiments and pool the results to ensure maximum peptide identifications. The results show how selecting an appropriate CE ramp can change the sequence coverage of proteins ranging from 4 to 94%. |
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المشرفين على المادة: | 0 (Membrane Proteins) 0 (Peptides) |
تواريخ الأحداث: | Date Created: 20240606 Date Completed: 20240703 Latest Revision: 20240710 |
رمز التحديث: | 20240710 |
مُعرف محوري في PubMed: | PMC11228973 |
DOI: | 10.1021/jasms.4c00093 |
PMID: | 38842540 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1879-1123 |
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DOI: | 10.1021/jasms.4c00093 |