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Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers, and transbilayer bundles.

Abstract:

Multiple nanosecond duration molecular dynamics simulations on the pore-lining M2 helix of the nicotinic acetylcholine receptor reveal how its structure and dynamics change as a function of environment. In water, the M2 helix partially unfolds to form a molecular hinge in the vicinity of a central Leu residue that has been implicated in the mechanism of ion channel gating. In a phospholipid bilayer, either as a single transmembrane helix, or as part of a pentameric helix bundle, the M2 helix ...

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Publication status:
Published

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Journal:
Proteins
Volume:
39
Issue:
1
Pages:
47-55
Publication date:
2000-04-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:7c094269-5932-4df8-9956-63934c9848d0
Source identifiers:
100432
Local pid:
pubs:100432

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