4.8 Article

Detergent-free mass spectrometry of membrane protein complexes

期刊

NATURE METHODS
卷 10, 期 12, 页码 1206-+

出版社

NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.2691

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资金

  1. Wellcome Trust [060208/Z/00/Z]
  2. WT [093305/Z/10/Z]
  3. Medical Research Council
  4. European Research Council
  5. Science Foundation Ireland [07/IN.1/B1836, 12/IA/1255]
  6. US National Institutes of Health [GM75915, P50GM073210, U54GM094599]
  7. Biotechnology and Biological Sciences Research Council
  8. Cambridge Overseas Trust
  9. Taiwan Ministry of Education
  10. Royal Society
  11. Biotechnology and Biological Sciences Research Council [BB/K01983X/1, BB/G011915/1] Funding Source: researchfish
  12. Engineering and Physical Sciences Research Council [EP/J01835X/1] Funding Source: researchfish
  13. Medical Research Council [G1000819] Funding Source: researchfish
  14. BBSRC [BB/G011915/1, BB/K01983X/1] Funding Source: UKRI
  15. EPSRC [EP/J01835X/1] Funding Source: UKRI
  16. MRC [G1000819] Funding Source: UKRI
  17. Wellcome Trust [093305/Z/10/Z] Funding Source: Wellcome Trust

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We developed a method that allows release of intact membrane protein complexes from amphipols, bicelles and nanodiscs in the gas phase for observation by mass spectrometry (MS). Current methods involve release of membrane protein complexes from detergent micelles, which reveals subunit composition and lipid binding. We demonstrated that oligomeric complexes or proteins requiring defined lipid environments are stabilized to a greater extent in the absence of detergent.

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