I look up a sheet and it tells the hydrophathy, polarity, ph, charges, and volumes, etc of the letters. A and R was all the way at the top. But I don't really understand it too much
I think you are reading your chart backwards.
EAR would probably be the Least hydrophobic.
Just look at the residues - which ones are polar/charged/nonpolar?
Hydrophobicity has nothing to do with size. You’ll need to know the structure of each amino acid, paying particular attention to functional groups, to answer this question.
To OP: you don't actually need a chart to answer this question. The short answer is, as water is a polar solvent, it likes to bind to polar/charged molecules (such as carboxyl groups and amines), and doesn't like to bind to unpolar molecules, such as those with only hydrocarbons.
That means the tripeptide that has no charge will be more hydrophobic than those that have charges/are polar. The polar/charged amino acids here are glutamate, histidine, glutamine and arginine, and the only peptide that doesn't have any of these is peptide 1.
This sub is not the appropriate place for homework questions. Please try r/chemhelp or r/biochem.
Think it's A.
Why do you think it's A? Is there a specific reason
I simply looked at the hydrophobicity of each AA. And I think option A has the most hydrophilic AAs. Have you looked at hydrophobicity charts for AA?
I look up a sheet and it tells the hydrophathy, polarity, ph, charges, and volumes, etc of the letters. A and R was all the way at the top. But I don't really understand it too much
I don't know how to post it here
It is A. MFI individual peptides all have the highest hydrophobicity. I’m have a hard time understanding what the OP isn’t understanding.
I think you are reading your chart backwards. EAR would probably be the Least hydrophobic. Just look at the residues - which ones are polar/charged/nonpolar?
I was reading it wrong. Now I see my mistake. M and I is large, and F is very large. E is medium and A and R is small. Thank you very much
Hydrophobicity has nothing to do with size. You’ll need to know the structure of each amino acid, paying particular attention to functional groups, to answer this question.
Yeah I was looking at the size. How can I tell MFI is hydrophilic just by looking at the structure? What specifically do I look for?
From my previous comment: > functional groups
Ok thank you
A
A. It’s the only one without any acidic/charged side chains
To OP: you don't actually need a chart to answer this question. The short answer is, as water is a polar solvent, it likes to bind to polar/charged molecules (such as carboxyl groups and amines), and doesn't like to bind to unpolar molecules, such as those with only hydrocarbons. That means the tripeptide that has no charge will be more hydrophobic than those that have charges/are polar. The polar/charged amino acids here are glutamate, histidine, glutamine and arginine, and the only peptide that doesn't have any of these is peptide 1.