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Probing the agonist binding pocket in the nicotinic acetylcholine receptor: a high-resolution solid-state NMR approach.

Abstract:

Acetylcholine, the agonist for the nicotinic acetylcholine receptor, has been observed directly when bound specifically to its binding site in the fully functional receptor-enriched membranes from Torpedo nobiliana. High-resolution solid-state, magic angle spinning 13C NMR methods have been used to observe selectively N+(13CH3)3 acetylcholine bound in as few as 20 nmol of receptor binding sites, against a background of natural abundance membrane resonances and excess acetylcholine in free sol...

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Publication status:
Published

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Publisher copy:
10.1021/bi980390q

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Biochemistry
Volume:
37
Issue:
30
Pages:
10854-10859
Publication date:
1998-07-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:28b4011c-6dd0-491b-8756-9bda33a9f807
Source identifiers:
410490
Local pid:
pubs:410490

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