amino acid (acidic, basic, neutral and

•
•
CHEMISTRY OF LIPIDS
AMINO ACIDS & PROTEINS
•
nonpolar).
Functions of amino acids

• Protein synthesis, energy reserves,

What are the chemical composition hormones (thyroxin)
of proteins?
• 20 different amino acids used in
• Amino acids protein synthesis though others do

• amino group, carboxyl group, occur in nature

hydrogen and a variable side group • Essential amino acids cannot be

(residue) each joined to a central synthesised by the organism and
carbon atom must form part of their diet.

• Basic Structure of proteins – • Essential Amino Acids

Amino Acids
• Proteins are made up of chains of
small molecules called amino acids.
• There are 20 different amino acids
but each has the same basic
structure.
• C = carbon atom
• There are over 20 different amino
acids.
• 8 are Essential Amino Acids that
cannot be made by the body and
must be eaten.
• There are 2 extra essential amino
acids for children.

• H= Hydrogen atom • The rest are Non-Essential Amino

Acids these can be made by the
• NH2 = Amino group (basic) body
• COOH = Carboxyl group (acidic) • Essential and Nonessential Amino
• R = Variable group, changes for every
Acids
amino
• For example in the amino acid
• Essential Amino acids cannot be
made by the body and must be
Glycine the R group = H (one
obtained from food
Hydrogen Atom)

• Types of amino acids

• Vincent’s
•
• Amino end and carboxyl end can be •
Lovely
Mother
ionised NH3+ and COO- to give acidic
and basic characteristics • Took
• At pH 7 both groups are ionised • Him
• The residues are side chains which • To
give the individual properties to the
• London PROLAMINES: Soluble in
• In alcohol
FIBROUS GLOBULAR
• a gliadin in wheat
• Pram Collagen albumin

• PROTEIN CLASSIFICATION • Properties of Protein

• SIMPLE CONJUGATED
• Denaturation
DERIVED
• • Solubility
• Maillard reaction
These proteins are
formed due
•
to a chemical or
enzyme action on a • Elasticity
• Foam Formation
•
protein : i.e: Rennin
acts on
•
caesinogen and
• Gel Formation
makes caesin
•
PROTEIN + NON-
PROTEIN
Protein + Lipid =
Lipoprotein (lecithin)
• Properties of Protein

•
Protein + Phosphate
= Phosphoprotein (caesin) Denaturation
Protein + nucleic
acid = Nucleoprotein (DNA)
Protein + Colour • change in the nature of the
Pigment = Chromoprotein protein
(Haemoglobin)

ANIMAL PLANT
• The protein chain unfolds,
causing a change to the structure
Classified Classified
GLUTENINS : Soluble in acids &
alkali
according according
• caused by

to shape
Glutenin in wheat
to solubility
• a) heat,
• b) chemicals and
 • c) agitation • Properties of Protein

• It is often an irreversible
• Solubility
process
• Properties of Protein • Proteins are generally insoluble in
• Denaturation
water

• Heat
• There are two exceptions – egg
white in cold water & connective
• Most proteins coagulate/set when tissue, which is converted to
heated. gelatine in hot water
• E.g. Egg white coagulates at
60˚C; egg yolk coagulates in the • Maillard reaction
stomach at 68˚C
• also known as non-enzymic
• Chemicals browning.

• Acids, alkali, alcohol & • It occurs when food is roasted,

enzymes cause changes to the baked or grilled
protein structure
• Amino Acid + Carbohydrates +
• E.g. Lemon juice added to milk Dry heat = Brown Color
causes the milk protein
caesinogen to curdle
• Examples include roast potatoes,
toast
•
•
E.g. Enzyme rennin coagulates
milk protein caesinogen in the Elasticity
stomach
• Properties of Protein
• Certain proteins have an
elastic property
• Denaturation
• e.g. Gluten, the protein found
• Agitation
in flour, enables bread to rise
during cooking
•
•
This is also known as
mechanical action Foam Formation

• It involves whipping or
whisking the protein
• When egg white is whisked, air
bubbles are formed as the
• This results in the protein chain
protein chains unravel
unfolding & partial coagulation
 • Whisking also produces heat,
which slightly sets the egg
white
• This foam will collapse after a
while, unless it is subjected to
heat
• This property is used to make
meringues
• Gel formation
• Collagen, when heated, forms
gelatine
• Gelatine can absorb large
amounts of water and, when
heated, forms a sol
• On cooling, this becomes solid
•
& a gel is formed
A gel is a semi-solid viscous
solution
• All gels have a three-
dimensional network whereby
water becomes trapped. This
property is used in making
cheesecakes and soufflés
Gelatine
Heat is applied
As the protein
Uncoils water
becomes trapped
Sol
Pro gel
Water
Protein Matrix – the mixture has set – it
has become a gel
• Biological Functions of Protein
• Biological Functions of Protein
• Deamination
• This is the process by which excess
protein is used for energy.
• Left over amino acids are brought to
the liver
• The NH2 group is broken off, changed
to ammonia, then to urea and then
excreted.
• The rest of the molecule is converted
to glucose and used for releasing
energy.
• Biological Value of Protein
• The Biological Value of a protein is a
measure of the quality of the protein
and is expressed as a %.
• It is decided by the number of
essential amino acids a protein
contains in proportion to how much of
them the body needs.
• There are 2 types of protein foods:
(a) High Biological value, contain all
essential Amino Acids, complete
proteins, animal sources.
(b) Low Biological value, lack some
essential amino acids, incomplete
protein, plant sources
• Biological Value of different proteins
• Supplementary Value of Protein
• When low biological value foods, that
lack essential amino acids, are eaten
together they can provide all the
essential amino acid.
• The essential amino acids missing in
one food can be made up for by
 being present in the other food and
visa versa. • Protein structure

• This complementary value of protein • Primary structure

means that vegans can get all the
essential amino acids without eating
• The primary structure of human
cytochrome C
animal food
• Example; Bread is lacking Lysine but • Each letter represents an amino acid
is high in Methionine. Beans are • This protein has 105 amino acids.
lacking Methionine but high in Lysine.
By eating beans on toast both • Protein structure
essential amino acids are included in
the meal.
• 3-D structure of human cytochrome C

• RDA Protein & Energy value

• Protein structure - Primary
RDA • Order and number of amino acids in a
protein chain for example the protein
• 1gram of protein per kilogram of body insulin has over 50 amino acids in its
weight. chain arranged in a definite order.
• Child 30-50g/day
• Teenager 60-80g/day • Protein structure - Secondary
• Adults 50-75g/day • Involves the folding of the protein
• Pregnant or lactating 70-85g/day
chain into a spiral or zig-zag shape
Energy Value • This structure is caused by crosslinks
• 1g of protein gives 4kCal or 17 kJ
that form between different chains or
within the one chain.
energy
• There are different types of cross-
links
(a) Disulfide links which happen

•
•
CHEMISTRY OF LIPIDS
Enzymatic
when 2 Sulphur atoms bond .
(b) Hydrogen bonds where a
Hydrogen atom in one chain bonds
with an Oxygen atom in another
chain.
• Storage
• Hormonal • Protein structure - Tertiary
• Defensive • This refers to the 3 dimensional
• Transport folding of the chain. This structure
can be globular or fibrous. The
• Receptor shapes give certain properties to the
protein
• Structural
• Globular : In these the protein chain • Hemoglobin is a globular protein
is rolled up like a ball of wool. This consisting of four polypeptides: two
structure makes the protein soluble. alpha and two beta chains
This type of protein is found in body
cells, myoglobin in meat, albumin in
egg, haemoglobin in blood.
• Biology/Chemistry of Protein
Structure
• Fibrous: In these the protein chain Primary
takes on a straight, coiled or zig-zag
shape. These shapes make the
protein insoluble and stretchy or Secondary
tough. Gluten in wheat and elastin in
meat have a coiled structure.
Collagen in meat has a zig-zag Tertiary
structure.
• Fibrous proteins Quaternary
• Involved in structure: tendons • Proteins classified by function
ligaments blood clots • CATALYTIC
(e.g. collagen and spiders silk)
• COMMUNICATION
• Contractile proteins in movement:
muscle, microtubules • PROTECTIVE
(cytoskelton, mitotic spindle, cilia,
flagella).
• STRUCTURAL
• Globular proteins
• PIGMENTS
• most proteins which move around
(e.g. albumen, casein in milk) • STORAGE
• Proteins with binding sites: • TRANSPORT
enzymes, hemoglobin,
immunoglobulins, membrane receptor
sites. • CONTRACTILE

• Quaternary structure results when • TOXINS

two or more polypeptide chains form
one macromolecule
• Collagen is a fibrous protein
consisting of three polypeptides
coiled like a rope
• Proteins classified by function
• CATALYTIC: enzymes eg rubisco
• COMMUNICATION: hormones (eg
insulin) and neurotransmitters
• PROTECTIVE: eg immunoglobulin,
fibrinogen, blood clotting factors
• STRUCTURAL: eg collagen, spiders
silk
• PIGMENTS: eg rhodopsin
• STORAGE: eg ovalbumen (in eggs),
casein (in milk)
• TRANSPORT: eg hemoglobin
• CONTRACTILE: eg actin, myosin
• TOXINS: eg snake venom
• PROTEIN FUNCTIONS

• Protein structure determines protein

function

• Denaturation or inhibition which may

change protein structure will change
its function

• Coenzymes and cofactors in general

may enhance the protein's structure.