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

Journal article

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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Authors: Law, R; Forrest, L; Ranatunga, K; La Rocca, P; Tieleman, D

• Publication status: Published
• Journal: Proteins
• Volume: 39
• Issue: 1
• Pages: 47-55
• Publication date: 2000-04-01
• DOI: 10.1002/(sici)1097-0134(20000401)39:1<47::aid-prot5>3.0.co;2-a
• EISSN: 1097-0134
• ISSN: 0887-3585
• Language: English
• Keywords: Models, Molecular; Lipid Bilayers; Protein Structure, Secondary; Receptors, Nicotinic; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Time Factors; Leucine; Kinetics; Computer Simulation; Water