00:02
The hydroxyl containing amino acids are hydrophilic,
and because the hydroxyl that's contained
on the ends of each of these can interact
with water. They include serine, threonine,
and tyrosine. Again. serine and threonine
are very similar to each other, differing
only in a carbon; tyrosine as discussed before
has an aromatic ring, but it also contains
a hydroxyl group. At physiological pH, we
can see that serine, threonine and tyrosine
all have a zero charge arising from
the positive charge on the alpha amine and
the negative charge on the alpha carboxyl
group. As I noted previously, the hydroxyl
group on tyrosine can ionize at a high pH,
but this is not a factor at physiological
pH.
00:51
The next amino acid is one of the more interesting
amino acids and it's cysteine, you've seen
it previously. Cysteine has an R group that
contains a sulfhydryl group as shown here.
01:02
Now the sulfhydryl group gives cysteine some
very interesting properties, you'll note that
it ionizes at a relatively high pH,
that of 8. It's not too far from physiological
pH, but we tend not to think of this group
having a negative charge and the reason is
that because the sulfur that is found in the
R group of cysteine is very reactive. If you
place two cysteine sulfhydryls next to each
other, what you will see is that they will
form a covalent disulfide bond with each other
and when they do that, they form a very tight
linkage that helps to stabilize the structure
of proteins. The overall charge of cysteine,
like the other amino acids at physiological
pH is zero.
01:50
The next two amino acids are those that are
called the carboxamide or carboxyamide and
these include asparagine and glutamine. These
two amino acids are related to the amino acids
aspartic acid, and glutamic acid. The difference
being that in the case of these two amino
acids, the hydroxyl in the R group of the
amino acids of aspartic acid and glutamic
acid are replaced by an amine, giving rise
to the carboxamide group that I described
earlier. These amino acids interestingly have
for example at physiological pH, no ionization
in their R group, the NH2 does not ionize
at all. So this is in contrast to what we
saw with aspartic acid and glutamic acid.
02:38
The last group of amino acid that I will talk
about are those that ionize and form a positive
charge. These are the so-called basic or amine
containing amino acids. Within their R groups
you can see that each have different forms
of amines that exist. You'll note that these
basic amino acids also have longer side chains
than the acidic amino acids did. Now this
group includes arginine, lysine and histidine.
And at physiological pH these molecules will
tend to have a positive charge, and because
of this we can see that the overall charge
of each molecule is +1. Now arginine and lysine
are interesting in that they are both abundantly
found in proteins called histones. Histones
are positively charged proteins, the positive
charge arising from the arginine and lysine,
that are wound with DNA to make chromosomes.
03:36
The positive charge of the amino acids here
is attracted to the negative charge of the
phosphate backbone of DNA, and allows them
to interact considerably.
03:46
Lysine is a target for acetylation, that is
the attachment of an acetyl group to the amine
at the end of lysine. The effective acetylation
of lysine is to cover up the positive charge.
04:00
And so if you have a DNA that is interacting
with the positive charge of lysine and you
cover it up with an acetyl group, you change
the nature of the interaction between the
protein that contains the lysine and the DNA.
And this has some very important implications
for transcription.
04:18
The last amino acid here is histidine, and
it's notable because in contrast to the R
groups of arginine and lysine which have pKa
values both well over 10, histidine's R group
has a pKa value of about six. Now this is close
to physiological pH and means as a result,
that histidine can readily ionize or deionize
at physiological pH. This property turns out
to be very important in the active site of
enzymes where charge differences can make
a tremendous difference for catalysis.