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Molecular mechanisms in biological membranes

  • Full or part time
  • Application Deadline
    Applications accepted all year round
  • Self-Funded PhD Students Only
    Self-Funded PhD Students Only

About This PhD Project

Project Description

Processes at cell membranes are fundamental to biological systems, but are challenging to study at the structural level. We are studying a human heart membrane potassium channel protein (HERG) using molecular modeling to assess the structural basis of drug-induced pathologies that result from drug interactions with HERG. Current work involves construction of atomic resolution structural models of HERG embedded in membranes, the use of dynamics simulations to analyze how voltage sensor domains interact with the pore domain, and the molecular mechanism of voltage sensing in ion channels. Computational analysis of drug binding to hERG models is being done in collaboration with experimental electrophysiology of HERG in Professor Hancox’s lab in the Bristol School Physiology and Pharmacology.

Webpage: http://www.bristol.ac.uk/biochemistry/research/cd.html

References


Colenso, CK, Sessions, RB, Zhang, Y-H, Hancox, JC and Dempsey, CE (2013) Interactions between voltage sensor and pore domains in a hERG K+ channel model from molecular simulations and the effects of a voltage sensor mutation. J. Chem. Inf. Model. 53, 1358-1370.

Colenso, CK, Cao Y, Sessions, RB, Hancox, JC and Dempsey CE (2014) Voltage sensor gating charge transfer in a hERG potassium channel model. Biophys J.107, L25-8.

Melgari, D, Zhang, YH, El Harchi, Dempsey, CE and Hancox, JC (2015) Molecular basis of hERG potassium channel blockade by the class Ic antiarrhythmic flecainide. J. Mol. Cell. Cardiol. 86, 42-53.

Related Subjects

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