Integral membrane proteins: bottom-up, top-down and structural proteomics
| العنوان: | Integral membrane proteins: bottom-up, top-down and structural proteomics |
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| المؤلفون: | Upendra K. Kar, Julian P. Whitelegge, Margaret Simonian |
| المصدر: | Expert review of proteomics, vol 14, iss 8 |
| بيانات النشر: | Informa UK Limited, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | Proteomics, bilayer, 0301 basic medicine, Biochemistry & Molecular Biology, Glycosylation, Proteome, 1.1 Normal biological development and functioning, FPOP, Computational biology, Biology, 01 natural sciences, Biochemistry, Article, Mass Spectrometry, 03 medical and health sciences, FASP, Underpinning research, micelle, HDX, Humans, Molecular Biology, Integral membrane protein, Nanodisc, Organelles, 010401 analytical chemistry, Membrane Proteins, Transmembrane protein, 0104 chemical sciences, Transmembrane domain, 030104 developmental biology, Membrane, Membrane protein, LILBID, CyTOF, Generic health relevance, Biochemistry and Cell Biology, FT-ICR, nanodisc, Biotechnology |
| الوصف: | IntroductionIntegral membrane proteins and lipids constitute the bilayer membranes that surround cells and sub-cellular compartments, and modulate movements of molecules and information between them. Since membrane protein drug targets represent a disproportionately large segment of the proteome, technical developments need timely review. Areas covered: Publically available resources such as Pubmed were surveyed. Bottom-up proteomics analyses now allow efficient extraction and digestion such that membrane protein coverage is essentially complete, making up around one third of the proteome. However, this coverage relies upon hydrophilic loop regions while transmembrane domains are generally poorly covered in peptide-based strategies. Top-down mass spectrometry where the intact membrane protein is fragmented in the gas phase gives good coverage in transmembrane regions, and membrane fractions are yielding to high-throughput top-down proteomics. Exciting progress in native mass spectrometry of membrane protein complexes is providing insights into subunit stoichiometry and lipid binding, and cross-linking strategies are contributing critical in-vivo information. Expert commentary: It is clear from the literature that integral membrane proteins have yielded to advanced techniques in protein chemistry and mass spectrometry, with applications limited only by the imagination of investigators. Key advances toward translation to the clinic are emphasized. |
| وصف الملف: | application/pdf |
| تدمد: | 1744-8387 1478-9450 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7a3d5cb566a242a33cbf166ca4c7710Test https://doi.org/10.1080/14789450.2017.1359545Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....b7a3d5cb566a242a33cbf166ca4c7710 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17448387 14789450 |
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