00:00
some of the proteins and their fibrous nature
as you can see on the screen here.
00:00
Now when we get to tertiary structure, predicting
tertiary structure from primary sequence is
almost impossible to do, at least with computing
and our understanding of this process today.
00:12
We see this protein that has alpha helices
and we also see within the protein, the yellow
regions called beta strands that have been
organized to form a sheet. The reverse turns
that I described earlier are shown at this
point and there's yet another feature of this
protein that's very important, it's called
the random coil. The random coil is a part
of the protein that doesn't have a specific
structure. It's not random in the sense that
it doesn't go off on tangents, but what it
does, is it doesn't form a regular repeating
structure like I've already described. Because
of random coils and because of variabilites
within the alpha helices, beta strands and
reverse turns, predicting tertiary structure
proteins is very, very difficult to do.
01:03
Now tertiary structure proteins arise as a
result of folding, meaning that we can have
a linear sequence of amino acids that ultimately
come together and make what we describe as
a globular protein. Now globular proteins
are called that, I like to tell students,
because if you were to look at them in a macroscopic
world, you would look at that and say, that's
a glob of something, because they're all folded
up and while that folding appears to be quite
random, it is in fact quite specific. The sequence
of amino acids in the primary structure
will determine ultimately the folding that
a protein does. Now the folding of a protein
gives the protein its characteristic functions,
whether it's catalysis, whether it's structure,
or whether it's other functions that it's
performing. In primary structure, we said
that the peptide bond was the stabilizing
force that held together the amino acids.
01:58
In secondary structure we said that hydrogen
bonds held together alpha helices and also
the beta strands. When we get to tertiary
structure, we discover that there are different
forces, in addition to hydrogen bonds, that
help to stabilize tertiary structure and they
are shown in this schematic figure that shows
a protein that has folded, albeit in an unusual
way. We start on the right side of this figure,
showing an alpha helical region of the protein
and we're reminded that hydrogen bonds stabilize
alpha helices. The next region of the protein
is also stabilized by hydrogen bonds, but
these hydrogen bonds are occurring between
amino acids that are not close to each other
in primary sequence. And so when we have interactions
that arise between sequences that are not
close in primary sequence, that means they
must be tertiary by definition.
02:54
The disulfide bonds become a factor in tertiary
structure. Disulfide bonds, you may remember,
are bonds that arise as a result of interactions
between the sulfhydryls of two cysteine groups.
03:07
When these two cysteine groups get into close
proximity, they will form a covalent bond
called the disulfide bond that you see in
this structure. Now disulfide bonds are covalent
bonds and therefore, are the strongest bonds
that help to stabilize protein structure.
03:26
Moving further to the left and at the bottom,
we can see interactions arising between positively
charged amines and negatively charged carboxyl
groups. These are R groups of the individual
proteins, either let's say a basic amino acid
like lysine with the amine group, and a R
group carboxyl, like aspartic acid that they have
ionized and are interacting as a result of
charge attractions to each other. These ionic
bonds can play a very important role in organizing
and helping to stabilize a tertiary structure.
Now another bond that occurs in tertiary structure,
that is a little bit harder to understand,
is that of a hydrophobic bond. The hydrophobic
bond is shown above the ionic bonds and you
can see the side chains of isoleucine, valine
and phenylalanine that are all interacting
with each other. Now what does this mean?
Each of these amino acids is fairly hydrophobic,
meaning it has a side chain that does not
like to interact with water. Globular proteins
are commonly soluble in the cytoplasm of the
cell, meaning abundant water. Well since these
amino acids have side chains that don't like
to interact with water, they will tend to
avoid water and they will tend to interact
with each other, instead of interacting with
water. Very much like oil, when you mix it
with water, will separate and associate with
itself and not associate with the water. Now
it's interesting that when we compare different
proteins and we look at the location of the
hydrophobic amino acids, for proteins that
are soluble in water, proteins will fold,
so as to prefer the location of the hydrophobic
amino acid side chains on the interior part
of the protein. And that's because again, in
avoiding water, they get stability, and that
stability translates to stability for the
protein. The last of the individual bonds
that help to stabilize proteins that I'll
discuss here are those of metallic bonds and
in this particular figure you can see an iron
atom that has stabilized two regions of a
protein.