In: Chemistry
Description: In week 1 we discussed which amino acids were termed “essential” but we lacked the knowledge to really understand why these would be difficult to make. Now that we have examined the process of making amino acids, let's take a second look at why the body doesn’t make certain amino acids.
Instructions: Write a response to the following prompt and then review your peers response:
Prompt: Propose a reason for why so many of the essential amino acids belong in the aliphatic and aromatic groups.
Of the 20 total amino acids, there are nine your body can't make on its own.This nine amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.Essential amino acids are those you cannot manufacture. Because you lack the enzymes necessary to create them from other biological molecules, you must supply them from your diet each day.Amino acids are crystalline solids which have the capacity to dissolve in water. Meanwhile, they only dissolve sparingly in organic solvents, and the extent of their solubility depends on the size and nature of the side chain.
Aromatic Amino acids are the largest of the amino acids and include; phenylalanine (F), tyrosine (Y) and tryptophan (W). They can all absorb ultra-violet light however some can absorb more than others, tyrosine and tryptophan absorb more than phenylalanine meaning that tryptophan is the main molecule which absorbs light in the protein. Aromatic amino acids are also hydrophobic so are located in the core of the protein ensuring they are not near water. Humans cannot synthesize phenylalanine or tryptophan, and can only make tyrosine from phenylalanine, this means that aromatic amino acids are a vital component of our diet as we require them in certain proteins but do not synthesize them ourselves.
Aliphatic R groups are nonpolar and hydrophobic. Hydrophobicity increases with increasing number of C atoms in the hydrocarbon chain. Although these amino acids prefer to remain inside protein molecules, alanine and glycine are ambivalent, meaning that they can be inside or outside the protein molecule.