Amino structure

I am feeling fundamentally lazy when writing this. In case you forgot, all amino acids have this formula:

Such that R is the functional group that decides basically the fundamental properties of each molecule
There is a lot of groups and other bullshit you can study about these but its probably easier to learn the fundamental structures of each amino acid because you can just re-derive the properties from first principles at that point

The most fundamental amino acid is #Glycine, which has an R group of hydrogen, giving it a structure of:

The next most simple are ones that just have hydrocarbon chains, giving them hydrophobic properties, w/ variable shapes and masses

#Alanine: Methyl group addition

#Valine: Isopropyl addition

This is quickly becoming difficult to visualize but that's what the anki cards are for
Just found a cool plugin to let me render this easily, if it looks like gibberish and/or basic SMILES code to you you need to install obsidian-chem
#Leucine: iso-butyl addition

#Isoleucine:Think an isomer of leucine, 2-butyl addition

It gets a little weirder from here but not at all unintuitive
#Methionine: Thioether group addition idk

Think meth-thio-nine. I.e. there's a sulfur and a methyl on the R terminal end
#Proline: This one can only be described as absolutely bizarre.

The hydrocarbon bonds back to the amino nitrogen which causes steric strain, which makes this a common structural amino acid in areas of the protein where it bends. Yes I promise this is still an amino acid.

#Phenylalanine:Like phenol + alanine dehydration synthesis. Its a benzene ring on an amino acid. Don't let the name confuse you, it does not have an OH group.

#Tyrosine: Phenylalanine's polar cousin. There is an OH in the para position of the benzene, which adds a little bit of shared electronegativity to the ring. Apparently this makes it very useful in cell signaling, and it's a vital part of the tyrosine kinase receptor signaling mechanism

#Tryptophan: Biggest and most complex amino acid. Has a role in protein-protein interactions I guess

Next two are dead simple, just add an OH group
#Serine

#Threonine

#Cysteine: Adds a thiol (SH), helps form disulfide bonds IYKYK

These next ones require some explanation. At physiologic pH, the amino groups on the R group of these molecules are uncharged. Their variants, which will be discussed next, are acidic and become negatively charged
#Asparagine:

#Glutamine:

These are the two acidic variants of the previous ones. The amine + ketone are replaced with a carboxylic acid
#Aspartic-acid:

#Glutamic-acid:

#Lysine: Primary amino takes accepts electrons/binds to negative charges

#Arginine:Contains a guanidinium group, which is highly basic

Side note, the guanidine structure (NH2)2C=(NH2+), at the end is the same guanidine in, #Guanine, the nucleotide.

#Histidine: Has a structure containing an imidazole ring, similar to histamine. Plays a role in enzyme active sites.