In a subset of voltage-gated $\mathrm{K}^{+}$ channels, the N-terminus of each subunit acts like a tethered ball that occludes the cytoplasmic end of the pore soon after it opens, thereby inactivating the channel. This "ball-andchain" model for the rapid inactivation of voltage-gated $\mathrm{K}^{*}$ channels has been elegantly supported for the shaker $\mathrm{K}^{+}$ channel from Drosophila melanogaster. (The shaker $\mathrm{K}^{*}$ channel in Drosophila is named after a mutant form that causes excitable behavior-even anesthetized flies keep twitching.) Deletion of the N-terminal amino acids from the normal shaker channel gives rise to a channel that opens in response to membrane depolarization, but stays open instead of rapidly closing as the normal channel does. A peptide (MAAVAGLYGLGEDRQHRKKQ) that corresponds to the deleted N-terminus can inactivate the open channel at $100 \mu \mathrm{M}$
Is the concentration of free peptide $(100 \mu \mathrm{M})$ that is required to inactivate the defective $K^{+}$ channel anywhere near the local concentration of the tethered ball on a normal channel? Assume that the tethered ball can explore a hemisphere [volume $\left.=(2 / 3) \pi r^{3}\right]$ with a radius of $21.4 \mathrm{nm}$ which is the length of the polypeptide "chain" (Figure Q1 $1-2$ ). Calculate the concentration for one ball in this hemisphere. How does that value compare with the concentration of free peptide needed to inactivate the channel?