Proteins

REGISTER

FREE
Start revising A-level & GCSE with 7 million other students
FREE Revision guides, questions banks and resources
UK's biggest revision website
Enrol now

Lipids (/a-level/biology/biological-molecules-and-enzymes/revise-it/lipids)
Enzymes (/a-level/biology/biological-molecules-and-enzymes/revise-it/enzymes)
Dierent proteins can appear very dierent and perform diverse functions (e.g. the watersoluble antibodies involved in the immune system and the water-insoluble keratin of hair,
hooves and feathers). Despite this, each one is made up of amino acid subunits.
There about 20 dierent amino acids that all have a similar chemical structure but behave in
very dierent ways because they have dierent side groups. Hence, stringing them together in
dierent combinations produces very dierent proteins.

Each amino acid has an amino group (NH2) and a carboxylic acid group (COOH). The R
group is a dierent molecule in dierent amino acids which can make them neutral, acidic,
alkaline, aromatic (has a ring structure) or sulphur-containing.
When 2 amino acids are joined together (condensation) the amino group from one and the
acid group from another form a bond, producing one molecule of water. The bond formed is
called a peptide bond.
Hydrolysis is the opposite of condensation and is the breaking of a peptide bond using a
molecule of water.
Primary structure of proteins
Due to the bonding and the shape and chemical nature of dierent amino acids, the shape of a
whole chain of amino acids (a polypeptide or protein) is specic.
This will aect the properties of the protein, just as the type of a necklace depends on the type
of beads and how they are strung together. Therefore, the primary structure depends on the
order and number of amino acids in a particular protein.
For example:Haemoglobin is made up of 4 polypeptide chains, 2 chains and 2 chains, each
with a haem group attached. There are 146 amino acids in each chain. If just one of these is
wrong, serious problems can arise (e.g. sickle cell anaemia). The red blood cells become
distorted, the amount of oxygen they can carry is reduced and blood capillaries can be
blocked, leading to acute pains called crises.
Secondary structure of proteins
This is the basic shape that the chain of amino acids takes on. The 2 most common structures
are the -helix and the -pleated sheet.

are the -helix and the -pleated sheet.

This has a regular coiled structure like a spring, with the R groups pointing towards the outside
of the helix. Hydrogen (H) bonds are relatively weak but because there are so many, the total
binding eect is strong and stable. The helix is exible and elastic.

This is composed of 'side by side' chains connected by H bonds. All the peptide linkages are
involved in inter-chain H bonding so the structure is very stable.
Tertiary structure of proteins
This is the overall 3-D structure of the protein.
The shape of the protein is held together by H bonds between some of the R groups (side
chains) and ionic bonds between positively and negatively charged side chains. These are weak
interactions, but together they help give the protein a stable shape. The protein may be
reinforced by strong covalent bonds called disulphide bridges which form between two amino
acids with sulphur groups on their side chains.
These interactions may be electrostatic attractions between charged groups e.g. NH3+ and O-

These interactions may be electrostatic attractions between charged groups e.g. NH3+ and Oor van der Waal's forces.
Fibrous proteins are made of long molecules arranged to form bres (e.g. in keratin). Several
helices may be wound around each other to form very strong bres. Collagen is another
brous protein, which has a greater tensile strength than steel because it consists of three
polypeptide chains coiled round each other in a triple helix. We are largely held together by
collagen as it is found in bones, cartilage, tendons and ligaments.
Globular proteins are made of chains folded into a compact structure. One of the most
important classes are the enzymes. Although these folds are less regular than in a helix, they
are highly specic and a particular protein will always be folded in the same way. If the
structure is disrupted, the protein ceases to function properly and is said to be denatured. An
example is insulin, a hormone produced by the pancreas and involved in blood sugar
regulation.
A globular protein based mostly on an -helix is haemoglobin.
A globular protein based mostly on a -pleated sheet is the immunoglobulin antibody
molecule.
Quaternary structure of proteins
If a protein is made up of several polypeptide chains, the way they are arranged is called the
quaternary structure. Again, each protein formed has a precise and specic shape (e.g.
haemoglobin)
Prosthetic groups
The majority of proteins are assisted in their functions by a prosthetic group. This may a simple
metal ion such as zinc in the enzyme carboxypeptidase, or it may be a complex organic
molecule, such as the haem group in haemoglobin.
Functions of proteins
1. Virtually all enzymes are proteins.
2. Structural: e.g. collagen and elastin in connective tissue, keratin in skin, hair and nails.
3. Contractile proteins: actin and myosin in muscles allow contraction and therefore
movement.
4. Hormones: many hormones have a protein structure (e.g. insulin, glucagon, growth
hormone).
5. Transport: for example, haemoglobin facilitates the transport of oxygen around the body,
a type of albumin in the blood transports fatty acids.
6. Transport into and out of cells: carrier and channel proteins in the cell membrane
regulate movement across it.
7. Defence: immunoglobulins (antibodies) protect the body against foreign invaders;
brinogen in the blood is vital for the clotting process.
Biochemical test:
The reagent used to test for proteins is called biuret reagent. It can be used as two separate
solutions of copper sulphate and potassium or sodium hydroxide or as a ready-made biuret
solution. In either case, a purple colour indicates a positive result.

Download the iPhone Revision Apps Bundle

(https://itunes.apple.com/gb/app-bundle/s-cool-a-levelsuccess/id1093845470?

mt=8&utm_source=AlevelMPU&utm_medium=footerADALEVEL&utm_campaign=SuperAPPS)

Get 10 of S-cool's powerful revision apps for the price of 1 with theA-level
Super App Bundle.

GetiPhoneApp>>(https://itunes.apple.com/gb/appbundle/scoolalevel
success/id1093845470?
mt=8&utm_source=AlevelMPU&utm_medium=footerADALEVEL&utm_campaign=SuperAPPS)

Lipids (/a-level/biology/biological-molecules-and-enzymes/revise-it/lipids)
Enzymes (/a-level/biology/biological-molecules-and-enzymes/revise-it/enzymes)

Latest Biological Molecules and Enzymes question

Does stainless steel get rid of garlic smells? (/forums/gcse/does-stainless-steel-get-ridgarlic-smells)

Hannah Roberts

Revise quicker
Get revision guides (/content/revision-guide-database)
Get question banks (/content/question-banks)
Ask questions (/forum/question/add)
Tell a friend (and Win) (/content/s-cool-referral)

JOIN NOW FREE (/user/register)

or Sign in (/user/login)

Ask a Question about Biological Molecules and Enzymes (/node/add/forum?

category=278)