Nanopores are nanoscale apertures in transmembrane proteins such as ion channels through which water and ions can pass. Some of these nanopores contain a hydrophobic gate which prevents water from passing through the pore without complete steric occlusion of the aperture. These hydrophobic gates are formed by a pore lining of hydrophobic residues accompanied by a constriction in the local radius of the pore. Using molecular dynamics simulations, we use the transmembrane protein TMEM175 as a template to investigate the competing effects of pore lining hydrophobicity and pore radius on the open/closed state of the pore. In addition to this, we investigate the effect of water models and use alternative simulation techniques to gain further insights into wetting/de-wetting behaviours.<br/>

Simulations of hydrophobic gating in an ion channel: TMEM175

2019 Spring National Meeting

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