High-resolution mass spectrometry of small molecules bound to membrane proteins
Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry–based method for analyzing intact membrane protein–ligand co...
| Main Authors: | , , , , , , , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Springer Nature
2016
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| _version_ | 1826261491690504192 |
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| author | Gault, J Donlan, J Liko, I Hopper, J Gupta, K Housden, N Struwe, W Marty, M Mize, T Bechara, C Zhu, Y Wu, B Kleanthous, C Belov, M Damoc, E Makarov, A Robinson, C |
| author_facet | Gault, J Donlan, J Liko, I Hopper, J Gupta, K Housden, N Struwe, W Marty, M Mize, T Bechara, C Zhu, Y Wu, B Kleanthous, C Belov, M Damoc, E Makarov, A Robinson, C |
| author_sort | Gault, J |
| collection | OXFORD |
| description | Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry–based method for analyzing intact membrane protein–ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length. |
| first_indexed | 2024-03-06T19:22:18Z |
| format | Journal article |
| id | oxford-uuid:1a81bf2a-17d1-4bb0-bc7b-7cdb1345b9dc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:22:18Z |
| publishDate | 2016 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:1a81bf2a-17d1-4bb0-bc7b-7cdb1345b9dc2022-03-26T10:55:14ZHigh-resolution mass spectrometry of small molecules bound to membrane proteinsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1a81bf2a-17d1-4bb0-bc7b-7cdb1345b9dcEnglishSymplectic Elements at OxfordSpringer Nature2016Gault, JDonlan, JLiko, IHopper, JGupta, KHousden, NStruwe, WMarty, MMize, TBechara, CZhu, YWu, BKleanthous, CBelov, MDamoc, EMakarov, ARobinson, CSmall molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry–based method for analyzing intact membrane protein–ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length. |
| spellingShingle | Gault, J Donlan, J Liko, I Hopper, J Gupta, K Housden, N Struwe, W Marty, M Mize, T Bechara, C Zhu, Y Wu, B Kleanthous, C Belov, M Damoc, E Makarov, A Robinson, C High-resolution mass spectrometry of small molecules bound to membrane proteins |
| title | High-resolution mass spectrometry of small molecules bound to membrane proteins |
| title_full | High-resolution mass spectrometry of small molecules bound to membrane proteins |
| title_fullStr | High-resolution mass spectrometry of small molecules bound to membrane proteins |
| title_full_unstemmed | High-resolution mass spectrometry of small molecules bound to membrane proteins |
| title_short | High-resolution mass spectrometry of small molecules bound to membrane proteins |
| title_sort | high resolution mass spectrometry of small molecules bound to membrane proteins |
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