Lipids (Textbook Pages 6-7)

The term lipid is used to describe a variable assortment of compounds

The most common type are the triglycerides
These come in the form of:
Fats, which are solid at room temperature
Oils, which are liquid at room temperature
Made by the combination of three fatty acid molecules with one glycerol molecule
Fatty acids are organic molecules which all have a –COOH group attached to a
hydrocarbon tail
The tails vary in length, depending on the fatty acids used
Glycerol is a type of alcohol

3 molecules of water
are released – one for
each bond!

Three fatty acid molecules join to glycerol by a

condensation reaction
The bond formed is an ester bond
Fatty acid +glycerol = glyceride
With three fatty acids it’s a triglyceride
Triglycerides are insoluble in water
Soluble in some organic solvents, including ether, chloroform and ethanol
This is due to the long hydrocarbon tail; electrons are evenly distributed therefore they are
non-polar and will not mix with water molecules which are polar
Triglycerides are therefore hydrophobic

Saturated fatty acids contain the

maximum possible amount of hydrogen
in the molecule (no double bonds)
Animal lipids are often saturated and
occur as fats
Unsaturated fatty acids contain double
bonds; single = monounsaturated more
than 1 = polyunsaturated

The double bond causes a kink in the hydrocarbon tail, and make fatty acids and lipids
melt more easily
Plant lipids are often unsaturated and occur as oils, such as olive oil and sunflower oil
 Roles of triglycerides
Excellent energy reserves; more C-H bonds than carbohydrates therefore more energy
dense
In humans, fat stored around the organs, particularly the kidneys, gives protection
Below the skin it acts as an insulator against heat loss
Blubber, a lipid found under the skin in sea mammals like whales
and dolphins, has a similar function but also provides buoyancy

They are sometimes used as a

metabolic source of water in very
dry habitats. For example, the desert
kangaroo rat never drinks water but
survives on metabolic water from its
fat intake. Lipids are converted to
carbon dioxide and water when
oxidised in respiration.
Waxes:
Similar to fats and oils except that the fatty acids are linked to long-chained alcohols
instead of glycerol
They provide a waterproofing layer on the outer surface of most terrestrial (land-
dwelling) animals and plants.
The shiny appearance of many indoor houseplants and of most insects is a result of
this wax

As well as using wax to waterproof their bodies, honey bees use a stiffer wax to make
the honeycombs in which they store food and house their young.
Phospholipids:
One of the three fatty acid molecules is replaced by a phosphate group

The phosphate group is polar and can dissolve in water

The head of the molecule is hydrophilic (water-loving), but the hydrocarbon tails are
hydrophobic (water-hating).
This has significant implications in the structure of cell membranes
Testing for Lipids: Emulsion test
http://brilliantbiologystudent.weebly.com/ethanol-emulsion-test-for-lipids.html

Shake the test substance with ethanol for about a minute so that it dissolves, then pour
the solution into water.
Any lipid will show up as a milky emulsion.
The more lipid there is, the more noticeable the milky colour will be.
 Proteins (Textbook pages 8-9)
Proteins are an extremely important class of molecules in living organisms
More than 50% of the dry mass of most cells is protein
They have many important functions:
Enzymes, e.g. amylase
Transport proteins, e.g. haemoglobin
Contractile proteins, e.g. myosin in muscle
Immunoproteins, e.g. immunoglobulins (antibodies)
Membrane proteins, in the structure and function of cell surface membranes
Structural proteins, e.g. keratin, collagen
Hormones, e.g. insulin
Despite their tremendous range of function, all proteins are made from the same basic
components (monomers). These are amino acids. Each different protein molecule is made
under the direction of its own gene and performs its own precise function. Of particular
importance is the shape of the protein molecule, which is determined by its amino acid
sequence.
Amino acids – general structure of all amino acids:

Central carbon atom

An amine group –NH2
A carboxylic acid group –COOH
A hydrogen atom
The R group – there are many
different kinds. This is where amino
acids differ from each other

The simplest amino acid is glycine, where the R group is a single hydrogen atom.
Amino acid R groups found in naturally occurring proteins:
Two amino acids join by a condensation reaction a form a peptide bond: one loses a
hydroxyl –OH group from its carboxylic acid group, the other loses a hydrogen atom
from its amine group. The new molecule is called a dipeptide. When many are linked
together it’s a polypeptide.
Primary Structure
The sequence in which the amino acids are joined in the polypeptide chain
Secondary Structure
A polypeptide chain often coils into an alpha helix due to hydrogen bonding between the
oxygen atom of the –CO group of one amino acid and the hydrogen of the –NH group of
the amino acid four places ahead.

Alpha helix
Sometimes a much looser, straighter shape is formed, called a beta pleated sheet.
This is a flat sheet formed by a polypeptide that folds back on itself or links to
adjacent polypeptides lying parallel to one another.

Beta pleated sheet

Other proteins show no regular arrangement at all, it depends which R groups are
present and what attractions occur.
Tertiary Structure
Further folding of the polypeptide to give a more complex three-dimensional shape. The
shape is very precise and specific to the function. Some polypeptides have areas of their
tertiary structure composed of both alpha helices and beta pleated sheets
Different parts of the polypeptide are close to each other and stabilise by:
Hydrogen bonds – form between strongly polar groups. They can be broken by high
temperature or pH changes
Disulphide bonds – form between cysteine molecules. Broken by reducing agents
Ionic bonds – form between ionised amine and carboxylic acid groups. Broken by pH
changes
Hydrophobic interactions – form between non-polar R groups
When the bonds are broken the tertiary structure changes and the protein does not
function. It is said to be denatured.
Quaternary Structure
Many proteins are made of two or more polypeptide chains. E.g. haemoglobin molecules
have four polypeptide chains, each with an iron-containing haem group in the centre. The
chains are held together by the same types of bond as in the tertiary structure.
Chromatography is a technique used to separate mixtures into their components.
Separation is dependant on solubility and molecular mass. Paper chromatography can
be used to separate mixtures of amino acids.
http://www.biotopics.co.uk/as/amino_acid_chromatography.html

A spot of solution containing a mixture of amino acids is added to the lower end of a strip of chromatography
paper, then the paper placed in solvent. The solvent moves up the paper by capillary action, carrying solute
molecules with it. As different solute molecules travel at different rates, they are separated from one another.
Amino acids are colourless, so they are stained with ninhydrin to allow them to be seen.