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Probing conformational changes in membrane-embedded proteins by measuring diffusion

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  • UserRichard Morris, University of Warwick
  • ClockThursday 01 October 2015, 13:45-15:00
  • HouseTheory Library.

If you have a question about this talk, please contact Mike Gunn.

The function of membrane-embedded proteins such as ion channels depends crucially on their conformation. In this talk, I demonstrate how conformational changes in asymmetric membrane proteins may be inferred from measurements of their diffusion. The approach combines a covariant formulation of low Reynolds number hydrodynamics with a linear elastic model of the protein. Motivated by recent experimental results, I focus on the example of KvAP, a ubiquitous voltage-gated potassium channel. The conformation of KvAP is found to change considerably due to tension, with its `walls’, where the protein meets the membrane, undergoing significant angular strains. The torsional stiffness is determined to be 26.8 kT at room temperature. This has implications for both the structure and function of such proteins in the environment of a tension-bearing membrane.

This talk is part of the Theoretical Physics Seminars series.

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