Do we need to know whether amino acids are hydrophobic vs hydrophilic and positive vs negative or can we just assume that the structure will change due to interactions between these groups?
Hey there! Hydrophobic amino acids are non-polar, and hydrophilic ones are polar. You’d have to look at the charges of the molecule and see if they cancel out to 0 or end up as either a negative or positive charge. I’m not sure what you mean by “change due to interactions between groups,” since groups interact certain ways because of their charges. Let me know if that helps!
Thank you. I meant that if there was a specific amino acid mutation, would we need to know the properties of that SPECIFIC amino acid. For example, if I said that the conformation of the protein would change because the interaction between positive and negative molecules would need to accommodate the mutation, but in reality both amino acids had the same overall charge, would that be something that I could lose points for? Or would they not get so specific?
This is assuming that we would not be given the diagram of both Amino Acids. I understand the content but am just worried about the specificity of the FRQ
Yeah I don’t think you’ll need to be that specific, so I wouldn’t worry about that too much! Just know that mutations may replace, delete, or add amino acids, and each amino acid has its own unique structure and charge, so that would throw off the whole structure.
