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Amino Acids

An amino acid is a molecule that contains both amine and carboxylic acid groups. The general structure is
shown below, the only thing that changes is the R group for different amino acids:

amino acids are all chiral i.e. have 4 different groups attached to the central carbon, except for
glycine has R= H, which makes it not chiral.

The chiral amino acids can then of course form optical isomers (mirror images).

Addition of acid and base

Amino acids can react as amines or carboxylic acids. There is nothing special about the amine or acid
groups in these molecules, they just react as normal amines and acids.

Amines are basic and therefore will react with acids i.e. pick up an H+ to give NH3+

Carboxylic acids are obviously acidic and therefore will react with base i.e. lose an H+ to give COO-

This leads us to very common exam questions. What happens to the structure at a low pH or if you add
acid? (both mean the same thing). The amine simply picks up an H+.

Low pH (add something like HCl)

High pH (add something like NaOH)

And vice versa, what happens at high pH or if you add base? This just means the acid loses an H+ to form
What if there is more than one amine or acid group? Well, it depends on the conditions. For example, if
there are two amine groups and it is in excess acid, then put a + on both amines. If they dont specify
excess, then you can do what you want.

Amino acids are solids and exist as zwitterions

You can view zwitterions as a combination of the low and high pH reactions above i.e. the + on the amine
and the on the acid are both present:

Due to the + and charges there is a strong electrostatic attraction (ionic bond) which means that amino
acids exist as crystalline solids and have high melting points.

The zwitterion forms due to a proton transfer from the acid to the amine.

When do zwitterions form?

Zwitterions form at very specific pHs, which varies depending upon the amino acid.

the pH where a zwitterion forms is called the isoelectric point

Different amino acids have different isoelectric points. So in a question they would have to give you some
information, you wouldnt be expected to guess just by looking at the amino acid to know when the
zwitterion forms.

If the pH in the question is the same as the pH of the isoelectric point, then you draw the zwitterion.

What if there is more than one amine or acid group? For a zwitterion it has to be neutral overall, so you
can only have one + and one -. You can choose which amine and acid groups the charges go on.

Amide/peptide bond formation

This is the third time this reaction has been done in Topics 17 and 18. We saw it in ester/polyester
formation and again in the first part of this tutorial to make polyamides.

try to keep this simple. Whether you are making/breaking an ester, polyester, amide or polyamide,
the reaction is more or less identical!
In the example below we are joining together alanine and serine. The only product you ever get is an
amide, which is highlighted in the red circle on the right.

they often refer to the amide as a peptide bond (they are the same thing). Its just the application is
different as joining many amides derived from amino acids together peptide (polyamide). Many of
those joined together protein. So this is the basis of DNA.

Rule: remove one H from the NH2 and the OH from the acid H2O. Then join the two units together:

you could do the same reaction with two units of the same amino acid reacting with itself.

Breaking the amides (hydrolysis)

As we saw already for the esters and amides hydrolysis:

Rule: split the molecule between the C-N bond then add an H to the NH and add an OH to the C=O.

the products I have written out above are not technically correct as I didnt specify acidic or basic
conditions. It was just to demonstrate how to get back to the amino acids.

Thin Layer Chromatography (TLC)

If you break up a polyamide or peptide to form many amino acid molecules, you can identify which amino
acids you have by using thin-layer chromatography (TLC) (see chromatography tutorial).

When doing this technique the TLC plate will have several or many spots on it, each corresponding to an
amino acid.
They use the Rf value to try to identify which amino acids are present as each should have a slightly
different value. You would compare the Rf value with a literature value in order to identify which amino
acid you have.

The problem with this is of course that many things could have very similar R f values so it is not a perfect
method and can still be difficult to identify the amino acids.

Rf values:

the distance from the bottom of the silica plate to the centre of the spot/distance from the bottom
to the top (solvent front)

front Spot that has
ran up the
3.06 2.62
cm cm
Original sample

Rf = 2.62/3.06 = 0.86 (always a number less than 1)

Amino acids are colourless and cannot be seen on the TLC plate. To get round this they stain the plate
with ninhydrin to give a purple colour where the amino acids are.

Ninhydrin reacts with all amino acids to give the same purple colour.