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Everything in this video is take from the following website:
www.garlandscience.com/garland...
The bacterial potassium channel is a multipass transmembrane protein in the plasma membrane. It is built from four identical subunits that are arranged symmetrically. A pore in the center of the protein allows selective passage of potassium ions across the membrane.
Four rigid protein loops, one contributed by each subunit, form a selectivity filter at the narrowest part of the pore. This structure is responsible for the channel's high degree of selectivity for potassium ions over sodium ions.
In the selectivity filter, carbonyl groups line the walls of the pore. These carbonyl groups are spaced precisely to interact with an unsolvated potassium ion, balancing the energy required to remove its hydration shell. Passage of a sodium ion through the channel is energetically unfavorable because the sodium is too small for optimal interaction with the carbonyl groups.