Please help me, I am deeply confused in this class and trying so hard to underst

Question

Please help me, I am deeply confused in this class and trying so hard to understand. Please give detailed answers. I know some of these might be confusing but your help will really help me learn. The teacher requires very very detailed answers and he gives nearly no (and I mean literally nearly zero) partial credit so I'm dying here. Thank you sooooooo much, you have no idea.

Also, I am nearly leaglly blind and I am dyslexic so if you could please write clear it would help so much. I just want to learn like everyone else. SUPER SUPER THANK YOU

The following represent two transmembrane proteins within the plasma membrane ofa eukaryotic cell 3. (3 pts total) The region that transverses the membrane is a single alpha helix. Which of the following images best represents the arrangement of the amino acids in this portion of the protein? The black line represents the protein backbone and blue circles represent R groups. Smaller circles are used to indicate R groups farther down the chain. [1 pt] A. B. List three amino acids you are likely to find in this region of the helix. [1 pt] C. What role(s) do these amino acids play in stabilizing the alpha helix in this context? [1 pt]

Explanation / Answer

Ans: QA: Right answer is ‘A’: Side chain R groups extend away, slightly down from the helix and interact with aliphatic chains of phospholipids by hydrophobic interactions, hence blue dots represented outside

QB: Amino acids with hydrophobic side chains and tend to form alpha helices are Alanine, leucine, valine, methionine etc

QC: Lenth of alpha helices is usally 4-40 amino acid long and on average 10 amino acids can make three turns (3.33 amino acids a turn) for example in a leucine zipper coiled coil every 1st and 4th amino acid is hydrophobic and 4th amino acid is always leucine. For example When we look at the side chains of Alanine, valine, leucine having short hydrophobic chains can rightly fit and stabilise the helix also hydrophobically interact laterally (form cross links) along the length of the helix and can provide a firm backbone, this interactions furhter increases in hydrophobic environment

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