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.
Fibrous Proteins
Repetitive regular sequences of amino
acids
Actual sequences may vary slightly
between two examples of the same protein
Polypeptide chain forms long parallel
strands
Length of chain may vary in two examples
of the same protein
Stable structure
Insoluble
Support and structural functions
Examples include collagen and keratin
Globular Proteins
Irregular amino acid sequences
Sequence highly specific and never varies
between two examples of the same
protein
Polypeptide chains folded into a spherical
shape
Length always identical in two examples
of the same protein
Relatively unstable structure
Soluble – forms colloidal suspensions
Metabolic functions
Examples include all enzymes, some
hormones (e.g. insulin) and haemoglobin
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.