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. 1985 Feb;82(4):958–962. doi: 10.1073/pnas.82.4.958

Anomalous interaction of the acetylcholine receptor protein with the nonionic detergent Triton X-114.

P A Maher, S J Singer
PMCID: PMC397172  PMID: 3856260

Abstract

Integral membrane proteins that form water-filled channels through membranes often exist as aggregates of similar or identical subunits spanning the membrane. It has been suggested that the insertion into the membrane of the channel-forming domains of the subunits may impart unusual structural features to the membrane-intercalated portions of the protein. To test this proposal, we have investigated the interaction of a multisubunit channel-forming integral membrane protein, the acetylcholine receptor protein, with the nonionic detergent Triton X-114. Whereas non-channel-forming integral membrane proteins that have heretofore been studied form mixed micelles with the detergent, the acetylcholine receptor was excluded from the Triton X-114 micelles. The structural implications of this result are discussed.

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Selected References

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