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

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.

authors

Maher PA,Singer SJ

doi

10.1073/pnas.82.4.958

subject

Has Abstract

pub_date

1985-02-01 00:00:00

pages

958-62

issue

4

eissn

0027-8424

issn

1091-6490

journal_volume

82

pub_type

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