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Marlborough School

Mr D Eve
Science Department

Protein Structure

Tertiary and Quaternary


Structure
Tertiary and Quaternary
Structure
Lesson Objectives

• To appreciate the importance of the


tertiary protein structure and describe
the types of bonding that maintain it.
• To describe the quaternary structure of
proteins, for example: haemoglobin
including the role of Fe2+

Marlborough School
Mr D Eve Science Department
Telephone Wires
Telephone wires have a secondary
structure similar to an alpha helix

They also have a tertiary structure!

Marlborough School
Mr D Eve Science Department
Myoglobin
The tertiary structure for
myoglobin is fairly well
understood and is shown
here. Myoglobin has an alpha
helix which then can be
viewed as being enclosed in
this blue sheath, the sheath
doesn't exist but we can draw
it that way. That helix folds
back upon itself into what's
referred to as the tertiary
structure of myoglobin. Bonds
between the side groups of
the amino acid residues are
responsible for holding
together the tertiary structure
of this protein.
Marlborough School
Mr D Eve Science Department
What bonds?
The kinds of bonds that can exist between the side groups include:

• Van der Waals bonds (Hydrophobic) if the side groups are


nonpolar.

• Hydrogen bonds if the side groups contain hydroxyl or amino


groups.

• Ionic bonds if the side groups are acids and bases that can
transfer protons from one to another making a carboxylate ion,
which is negative, and essentially an ammonium or quaternary
ammonium ion which is positive.

• Covalent bonds if the side groups are cysteine residues in which


the sulfur atoms are bonded together by the removal of two
hydrogen atoms.

Marlborough School
Mr D Eve Science Department
Disulphide bridges

Disulfide bonds are formed


by oxidation of the sulfhydryl
groups on cysteine. Different
protein chains or loops within
a single chain are held
together by the strong
covalent disulfide bonds. Both
of these examples are
exhibited by the insulin in the
graphic on the left.

Marlborough School
Mr D Eve Science Department
Hydrogen Bonding
Hydrogen bonding between "side
chains" occurs in a variety of
circumstances. The most usual
cases are between two alcohols, an
alcohol and an acid, two acids, or
an alcohol and an amine or amide.
In giving the structures for various
examples, the backbone of the
protein fragment will be
represented by a short helix with
only the side chain structure given
as in the graphic on the left.
In the prion protein, tyr 128 is
hydrogen bonded to asp 178, which
cause one part of the chain to be
bonding with a part some distance
away.

Marlborough School
Mr D Eve Science Department
Ionic Bonding
Salt bridges result from the
neutralization of an acid and amine
on side chains. The final
interaction is ionic between the
positive ammonium group and the
negative acid group. Any
combination of the various acidic
or amine amino acid side chains
will have this effect.
The example on the left is from the
prion protein with the salt bridge
of glutamic acid 200 and lysine
204. In this case a very small loop
is made because there are only
three other amino acids between
them. This salt bridge has the
effect of straightening an alpha
helix.
Marlborough School
Mr D Eve Science Department
Hydrophobic Interactions
The hydrophobic interactions of non-
polar side chains are believed to
contribute significantly to the
stabilizing of the tertiary structures in
proteins. This interaction is really just
an application of the solubility rule that
"likes dissolve likes". The non-polar
groups mutually repel water and other
polar groups and results in a net
attraction of the non-polar groups for
each other. Hydrocarbon alkyl groups
on ala, val, leu, and ile interact in this
way. In addition, benzene (aromatic)
rings on phe and tyr can "stack"
together.
In many cases this results in the non-
polar side chains of amino acids being
on the inside of a globular protein,
while the outside of the proteins
contains mainly polar groups.
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Mr D Eve Science Department
Examples of the bonds

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Mr D Eve Science Department
Quaternary Structure
Quaternary structure is the final step in
protein building: it is the structure due to
modifications, cofactors (like vitamins
and nucleotides), prosthetic groups (like
haem, and bound metal ions),
glycosylation (the addition of sugar
residues through serine or asparagine
residues) , and the agglomeration of
separate polypeptide chains to form
multimeric proteins. Marlborough School
Mr D Eve Science Department
Haemoglobin

Marlborough School
Mr D Eve Science Department
The Haem Group

One haem group is


contained in each
of the four
subunits of
haemoglobin. The
Iron atom in the
middle is able to
bind with oxygen
to form oxy-
haemoglobin.
Marlborough School
Mr D Eve Science Department
Acknowledgements
• http://www.elmhurst.edu/~chm/vchembook/567tertprotein.html

• http://images.google.co.uk/imgres?imgurl=http://kvhs.nbed.nb.ca/
gallant/biology/tertiary_structure.jpg&imgrefurl=http://kvhs.nbed.
nb.ca/gallant/biology/biology.html&h=600&w=341&sz=82&tbnid
=85_xPGG43P285M:&tbnh=135&tbnw=77&prev=/images%3Fq%
3Dtertiary%2Bstructure%26um%3D1&start=1&sa=X&oi=images
&ct=image&cd=1

• http://dl.clackamas.edu/ch106-08/tertiary.htm

Marlborough School
Mr D Eve Science Department