Answer:
<em> e) Ala</em>
Explanation:
Alpha helix is a secondary structure of proteins, it is made of 3.6 aminoacids residues per turn, this structure is possible thanks to local hydrogen bonding between C=O and N-h groups. The result is a cylindrical structure with a hydrogen-bonded backbone and the outside studded with side chains.
Glycin has an -H in its side chain, this makes it a too flexible molecule, therefore it's unusual to find them in alpha-helical structures because their presence could cause the helix to deform. Large R-groups can also affect this stability, phenylalanine has a bulky aromatic side group, this discards it as a stabilizer. Serine has a hydrogen bond donor or acceptor as a side chain, due to the proximity to the main chain it competes with the main chain to form NH and CO bonds. Alanine is the most common amino acid in alpha-helix structures because it has a short and no charged R group (unlike arginine that even when it's short it has a charged R-group), this makes it flexible enough to keep the structure stabilized.
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Sugar is a monomer called monosaccharides and sugar cubes are polymer because a polymer has a molecular structure
D. cell wall
both animals and walls have cell membranes for support
the cytoplasm holds the organelles in place
Answer:
all of the above can lead to increase in nitrogen
