期刊
NATURE METHODS
卷 13, 期 4, 页码 333-336出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.3771
关键词
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资金
- Royal Commission for the Exhibition of 1851 Fellowship
- Junior Research Fellowship at St Catherine's College, Oxford
- Engineering and Physical Sciences Research Council
- UK Medical Research Council [G1000819]
- European Research Council [268851]
- Royal Society Research Professorship
- Wellcome Trust [104633/Z/14/Z]
- BBSRC [BB/L021234/1]
- BBSRC [BB/L021234/1] Funding Source: UKRI
- MRC [G1000819] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L021234/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1240748] Funding Source: researchfish
- Medical Research Council [G1000819] Funding Source: researchfish
- European Research Council (ERC) [268851] Funding Source: European Research Council (ERC)
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.
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