The core principle ;linking all the function of all passive transporters (Gramicidin A, Porins, K+ channels, and Aquaporins is that transport specificity is determined by
The precise positioning of amino acid residues in the channel
The peptide ________________forms membrane-spanning channel that facilitates the passive diffusion of Na+ and K+. This channel is unique because it is formed by a linear peptide with alternating L- and D- amino acids
Gramicidin A
T/F: The K+ channel protein displays a selectivity of approximately 100- fold for K+ ions over Na+ ions
False, 10,000 fold not an 100 fold
What is the molecular basis for the high selectivity of the K+ channel that allows it to exclude Na+?
The channel’s carbonyl oxygen atoms interact favorably with desolated K+ ions, but not with Na+ ions
To pass through the selectivity filter of the K+ channel, the K+ ion must first perform what critical step regarding its structure?
The K+ ion must shed its hydration layer (or desolvate ) to favorable interact with the backbone carbonyl oxygens of the channel
Aquaporins provide an efficient means for H2O molecules to pass through membranes. This transport occurs solely in response to:
An osmotic gradient
T/F: aquaporin selectivity is achieved primarily by two short alpha-helices that for a physical restriction point, preventing any molecule larger than water from passing
True
While the Asn residues are also critical, the two short alpha helices form the core physical restriction
The two short alpha helices that form the constriction point in the aquaporins contain a conserved __________________________ motif
Asn-Pro-Ala (NPA)
Besides physical restriction, how do the Asn residues within the aquaporin channel’s constriction point contribute to water selectivity and the exclusion of H+ (protons)
The ASN residues hydrogen bond with the H2O molecules, ensuring single-file movement and disrupting the H2O hydrogen bonding chain that is essential for proton transport or proton hopping, thus excluding H+
Porin proteins such as the VDAC in mitochondria are structurally characterized by what common motif that spans the membrane?
A transmembrane beta-barrel structure