دورية أكاديمية

MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS.

التفاصيل البيبلوغرافية
العنوان: MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS.
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%.
References: Mass Spectrom Rev. 2023 Jul-Aug;42(4):1261-1299. (PMID: 34859467)
Drug Discov Today Technol. 2021 Dec;39:49-56. (PMID: 34906325)
J Am Soc Mass Spectrom. 2017 Jun;28(6):1192-1202. (PMID: 28374315)
J Am Soc Mass Spectrom. 2019 Jan;30(1):58-66. (PMID: 30280315)
Front Pharmacol. 2020 Feb 19;11:70. (PMID: 32140107)
Expert Rev Proteomics. 2013 Dec;10(6):551-66. (PMID: 24206228)
Chem Phys Lipids. 2019 May;220:14-22. (PMID: 30802434)
Anal Chem. 2021 Aug 31;93(34):11669-11678. (PMID: 34308633)
Biochemistry. 2014 Mar 11;53(9):1511-20. (PMID: 24512177)
Nat Methods. 2019 Jul;16(7):587-594. (PMID: 31249407)
Anal Chem. 2010 Jul 1;82(13):5415-9. (PMID: 20518534)
Mass Spectrom Rev. 2023 Jan;42(1):131-143. (PMID: 34145627)
Protein Sci. 2020 Jun;29(6):1285-1301. (PMID: 32170968)
Anal Chem. 2019 Jul 2;91(13):8564-8573. (PMID: 31141659)
Anal Chem. 2015 May 19;87(10):5247-54. (PMID: 25893550)
Rapid Commun Mass Spectrom. 2008 Sep;22(18):2898-904. (PMID: 18727141)
J Pharm Sci. 2021 Jun;110(6):2355-2361. (PMID: 33640336)
Nat Commun. 2018 Oct 8;9(1):4151. (PMID: 30297844)
Science. 2015 Oct 9;350(6257):aac7365. (PMID: 26450213)
J Pharm Sci. 2020 Jan;109(1):340-352. (PMID: 31201906)
ACS Chem Biol. 2020 May 15;15(5):1154-1160. (PMID: 31869199)
Nat Commun. 2017 May 17;8:15383. (PMID: 28513578)
Mass Spectrom Rev. 2023 Nov-Dec;42(6):2324-2348. (PMID: 35645145)
J Am Chem Soc. 2023 Apr 12;145(14):7768-7779. (PMID: 36976935)
Nat Methods. 2019 Jul;16(7):595-602. (PMID: 31249422)
J Am Soc Mass Spectrom. 2019 Nov;30(11):2185-2195. (PMID: 31493234)
Chem Rev. 2022 Apr 27;122(8):7562-7623. (PMID: 34493042)
Anal Chem. 2018 Oct 2;90(19):11315-11323. (PMID: 30170487)
J Am Soc Mass Spectrom. 2020 Apr 1;31(4):996-999. (PMID: 32141743)
Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7057-62. (PMID: 12773622)
Methods. 2018 Jul 15;144:27-42. (PMID: 29704663)
Nat Commun. 2020 Dec 2;11(1):6162. (PMID: 33268777)
Mol Cell Proteomics. 2011 Feb;10(2):M110.001479. (PMID: 20627868)
J Proteomics. 2020 Aug 15;225:103845. (PMID: 32480080)
Structure. 2018 Dec 4;26(12):1651-1663.e3. (PMID: 30293810)
Nat Methods. 2014 Feb;11(2):167-70. (PMID: 24336358)
Biotechnol J. 2022 Feb;17(2):e2100358. (PMID: 34747565)
Essays Biochem. 2023 Mar 29;67(2):187-200. (PMID: 36876893)
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
الوصف
تدمد:1879-1123
DOI:10.1021/jasms.4c00093