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The transmembrane domains of the nicotinic acetylcholine receptor contain alpha‐helical and beta structures.
Author(s) -
GörneTschelnokow U.,
Strecker A.,
Kaduk C.,
Naumann D.,
Hucho F.
Publication year - 1994
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1994.tb06266.x
Subject(s) - biology , nicotinic acetylcholine receptor , acetylcholine receptor , beta (programming language) , alpha (finance) , transmembrane protein , nicotinic agonist , ganglion type nicotinic receptor , biophysics , biochemistry , receptor , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
The transmembrane domain of the nicotinic acetylcholine receptor (nAChR) from Torpedo californica electric tissue contains both alpha‐helical and beta structures. The secondary structure was investigated by Fourier transform infrared (FTIR) spectroscopy after the extramembrane moieties of the protein from the extracellular and intracellular sides of the membrane were removed by proteolysis using proteinase K. The secondary structure composition of this membrane structure was: alpha‐helical 50%, beta structure and turns 40%, random 10%. The alpha‐helices are shown to be oriented with respect to the membrane plane in a way allowing them to span the membrane, while no unidirectional structure for the beta structures was observed. These findings contradict previous secondary structure models based on hydropathy plots alone.