| Autor: |
Jakob Meier-Credo, Laura Preiss, Imke Wüllenweber, Anja Resemann, Christoph Nordmann, Jure Zabret, Detlev Suckau, Hartmut Michel, Marc M. Nowaczyk, Thomas Meier, Julian D. Langer |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Journal of the American Society for Mass Spectrometry. 33(7) |
| ISSN: |
1879-1123 |
| Popis: |
Identification and sequence determination by mass spectrometry have become routine analyses for soluble proteins. Membrane proteins, however, remain challenging targets due to their hydrophobicity and poor annotation. In particular small membrane proteins often remain unnoticed as they are largely inaccessible to Bottom-Up proteomics. Recent advances in structural biology, though, have led to multiple membrane protein complex structures being determined at sufficiently high resolution to detect uncharacterized, small subunits. In this work we offer a guide for the mass spectrometric characterization of solvent extraction-based purifications of small membrane proteins isolated from protein complexes and cellular membranes. We first demonstrate our Top-Down MALDI-MS/MS approach on a Photosystem II preparation, analyzing target protein masses between 2.5 and 9 kDa with high accuracy and sensitivity. Then we apply our technique to purify and sequence the mycobacterial ATP synthase |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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