The gramicidin A channel: comparison of the energy profiles of Na+, K+ and Cs+

Abstract
The energy profiles for single occupancy by Cs+ and Na+ in the gramicidin A channel assumed to be in a head-to-head β6.33.3 helical dimeric structure, were computed: (A) allowing complete conformational freedom to the ethanolamine end, (B) constraining it to stay in its intrinsically preferred conformation. Whatever the constraint, both the entrance barrier and the central barrier appear in the order Cs+< K+< Na+. Introducing the flexibility of the tail modifies appreciably the profiles and the location of the extrema along it.Energy profileGramicidin AEthanolamine endCaesiumPotassiumSodiumEnergy barrierTheoretical computatio

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