Proteins

There are loads o f different proteins with loads o f different functions. But what are proteins? What do they look like?
Well, for your enjoyment, here are the answers to all those questions and many, many more...

Proteins are Made from Long Chains of Amino Acids

1) The monomers of proteins are amino acids.

2) A dipeptide is formed when two amino acids join together.
Grant's cries of "die peptide,
3) A polypeptide is formed when more than two amino acids join together.
die" could be heard for miles
4) Proteins are made up of one or more polypeptides. around. He'd never forgiven it
for sleeping with his wife.

Different Amino Acids Have Different Variable Groups

Amino acids have the same Structure o f an Am ino Acid E.g. Structure o f Alanine
general structure — a carboxyl
R ^ — variable group CH3
group (-COOH), an amine
I I
or amino group (-NH2) and H ,N — C COOH H N - C — COOH
an R group (also known as \ I
carboxyl H u 1 >1, //✓
a variable side group). _^v * ' ' 1 1 1 1 ' 1 1 ' 1 ' 1 1
group - Glycine is the only amino '
group
- acid th a t doesn't h ave
All living things share a bank of only 20 amino acids.
—
The only difference between them is what makes up their R group. - carbon in its side group. ~
= just one hydrogen atom. =
- Its R group
111111/ consists
111111i 1 / 11of1 \\>“
Polypeptides are Formed by Condensation Reactions
Amino acids are linked together by
amino acid 1 amino acid 2 dipeptide
condensation reactions to form polypeptides. R R O. H. R!
H-
A molecule of water is released during the I I condensation
-c- ■CQOH\+ N -c- COOH sfi— C — C O O H
reaction. The bonds formed between amino I I hydrolysis |_)
i =
I
acids are called peptide bonds. The reverse H H H
a molecule of water is formed
reaction happens during digestion. during condensation. peptide bond

Proteins Have Four Structural Levels

Proteins are big, complicated molecules. They're much easier to explain if you describe their structure in
four 'levels'. These levels are a protein's primary, secondary, tertiary and quaternary structures.

Primary Structure — this is the sequence of amino acids in the polypeptide chain.
Secondary Structure — the polypeptide chain doesn't remain flat and straight.
Hydrogen bonds form between the amino acids in the chain.
amino acid
This makes it automatically coil into an alpha (a) helix or fold into a
beta ((3) pleated sheet — this is the secondary structure.
Tertiary Structure — the coiled or folded chain of amino acids is often
coiled and folded further. More bonds form between different parts of the
polypeptide chain, including hydrogen bonds and ionic bonds (attractions
between negative and positive charges on different parts of the molecule).
Disulfide bridges also form whenever two molecules of the amino acid cysteine
come close together — the sulfur atom in one cysteine bonds to the sulfur atom in
the other. For proteins made from a single polypeptide chain, the tertiary structure
forms their final 3D structure.
Quaternary Structure — some proteins are made of several different polypeptide
chains held together by bonds. The quaternary structure
is the way these polypeptide chains are assembled together. For proteins made
from more than one polypeptide chain (e.g. haemoglobin, insulin, collagen), the
quaternary structure is the protein's final 3D structure.
 Proteins
Proteins have a Variety of Functions
There are loads of different proteins found in living organisms. They've all got different structures and shapes,
which makes them specialised to carry out particular jobs. For example:

1) Enzymes — they're usually roughly spherical in shape due to the tight folding of the polypeptide chains.
They're soluble and often have roles in metabolism, e.g. some enzymes break down large food molecules
(digestive enzymes, see pages 66-67) and other enzymes help to synthesise (make) large molecules.

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2) Antibodies — are involved in the immune response. They're made up of two light (short)
polypeptide chains and two heavy (long) polypeptide chains bonded together. Antibodies have
variable regions (see p. 44) — the amino acid sequences in these regions vary greatly. v
y
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3) Transport proteins — e.g. channel proteins are
present in cell membranes (p. 38). Channel proteins
contain hydrophobic (water hating) and hydrophilic
(water loving) amino acids, which cause the protein
to fold up and form a channel. These proteins
transport molecules and ions across membranes.

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4) Structural proteins — are physically strong. They consist of long polypeptide chains
lying parallel to each other with cross-links between them. Structural proteins include
keratin (found in hair and nails) and collagen (found in connective tissue).
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Use the Biuret Test for Proteins

If you needed to find out if a substance, e.g. a food sample,
contained protein you'd use the biuret test.

Negativeresult Positiveresult There are two stages to this test.

test solution,
sodiurr hydroxide
1) The test solution needs to be alkaline, so first you add
and a few drops of sodium hydroxide solution.
^ copper(ll) sulfate 2 ) Then you add some copper(ll) sulfate solution.
,r solution
• If protein is present the solution turns purple.

•
purple colour
, solution staying blue
indicates protein If there's no protein, the solution will stay blue.
indicates no protein
The colours are pale, so you need to look carefully.