Abstract

I will describe recent advances we have made in using fast, continuum elasticity theory to describe membrane deformations around proteins. I will show that our calculations match the deformations predicted from all atom molecular dynamics simulations for two proteins: gramicidin (a small antibiotic ion channel) and nhTMEM16 (a member of the calcium activated chloride channel family). Our calculations reveal that nhTMEM16 produces large distortions in the membrane potentially related to its ability to scramble lipids from one leaflet to the other. This hypothesis is supported by atomistic simulations in which we observe lipids flipping from one leaflet to the other. Experiments to test the lipid flipping mechanism in a mammalian TMEM16 family member will also be discussed.

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