Question

the two models on the left show a glucose molecule (red and white balls) binding to the exterior of the carrier and then releasing to the inside. the ribbon model on the right shows the same carrier in a way that makes it easier to see elements of secondary structure. credit: images created by codon learning using using glut1 and pdb entry seq1 kapoor, finer - moore et al(2016) mechanism of inhibition of human glucose transporter glut1 is conserved between cytochalasin b and phenylalanine amides doi.org/10.2210/pdb5eql/pdb based on your analysis of these models, select all of the following statements that are correct. the carrier undergoes a dramatic change in shape (or conformation) after glucose binds. the parts of the carrier that interact directly with the hydrocarbon tails inside the lipid bilayer are primarily alpha - helices. the carrier should be classified as a peripheral membrane protein, because it has regions that project into the interior of the cell. its logical to predict that the glucose binding site consists of specific r - groups, and that if a mutation changes the amino acids at the binding site, the carriers activity would change. one other quick point. and this one can be extremely hard to wrap your brain around, because humans are wired to interpret events as purposeful and directed. in particular, we are extremely bad at understanding the role of randomness when we try to make sense of events. but its critically important to realize that the arrow from glucose to its binding site on the carrier—the arrow shown in the model you just analyzed—is misleading. glucose doesnt did you fully understand the concept covered in this section? its muddy its clear submit answer

Explanation:

• The first statement is correct as carrier - protein conformation often changes upon ligand binding to facilitate transport.
• The second statement is correct because alpha - helices are common in transmembrane regions that interact with the lipid bilayer.
• The third statement is incorrect as the carrier spans the membrane and is an integral membrane protein, not a peripheral one.
• The fourth statement is correct since the binding site is composed of amino - acid R - groups and mutations can alter function.

Answer:

The carrier undergoes a dramatic change in shape (or conformation) after glucose binds.
The parts of the carrier that interact directly with the hydrocarbon tails inside the lipid bilayer are primarily alpha - helices.
It's logical to predict that the glucose binding site consists of specific R - groups, and that if a mutation changes the amino acids at the binding site, the carrier's activity would change.