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lüll Ion channel gating: insights via molecular simulations Beckstein O; Biggin PC; Bond P; Bright JN; Domene C; Grottesi A; Holyoake J; Sansom MSFEBS Lett 2003[Nov]; 555 (1): 85-90Ion channels are gated, i.e. they can switch conformation between a closed and an open state. Molecular dynamics simulations may be used to study the conformational dynamics of ion channels and of simple channel models. Simulations on model nanopores reveal that a narrow (<4 A) hydrophobic region can form a functionally closed gate in the channel and can be opened by either a small (approximately 1 A) increase in pore radius or an increase in polarity. Modelling and simulation studies confirm the importance of hydrophobic gating in K channels, and support a model in which hinge-bending of the pore-lining M2 (or S6 in Kv channels) helices underlies channel gating. Simulations of a simple outer membrane protein, OmpA, indicate that a gate may also be formed by interactions of charged side chains within a pore, as is also the case in ClC channels.|*Ion Channel Gating[MESH]|Bacterial Outer Membrane Proteins/chemistry/metabolism[MESH]|Hydrophobic and Hydrophilic Interactions[MESH]|Ion Channels/*chemistry/*metabolism[MESH]|Models, Molecular[MESH]|Potassium Channels/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Thermodynamics[MESH] |