Protein & Lipids

By: Tayyaba Gulistan

 Protein
• Most abundant biological macromolecules
• Great variety; thousands of different kinds may be found in a single
cell
• Genetic information expressed in proteins
• All life constructed from the same ubiquitous set of 20 amino acids
• Wide range of sizes, from relatively small peptides with just a few
amino acid residues to huge polymers with molecular weights in the
millions
• Cells can produce proteins by joining the same 20 amino acids in
many different combinations and sequences.
• E.g. enzymes, hormones, antibodies, transporters, muscle fibers, the
lens protein of the eye
 Amino Acids
• Proteins are polymers of amino acids
• Amino acid residue joined to its neighbor by a specific type of
covalent bond
• Broken down (hydrolyzed) to their constituent amino acids
• Twenty different amino acids are commonly found in proteins
 Amino Acids
Consists of
• central carbon atom, alpha (α) carbon
• Amino group (NH2)
• Carboxyl group (COOH)
• Side chain (R)

• At physiological pH (7.2-7.4) the amino group is typically protonated

and bears a positive charge, while the carboxyl group is typically
deprotonated and bears a negative charge
 Amino Acids
• R group__ determines the identity of the amino acid

• E.g. H atom___ Glycine

• Methyl group CH3___ Alanine

 Amino Acids
• Acidic amino acid
• That have acidic side chain at neutral pH
• 2 acidic amino acids
1. Aspartic acid 2. Glutamic acid

• Basic Amino acid

• That have basic side chain at
neutral pH
• 3 basic amino acids
1. Arginine 2. Lysine
3. Histidine
Classification of amino acids
• Classified into 3 groups
1. ESSENTIAL AMINO ACIDS
• Essential amino acids cannot be made by the body. As a result, they
must come from food.
• The 9 essential amino acids are: histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, threonine, tryptophan, and valine.
2. NONESSENTIAL AMINO ACIDS
• Nonessential means that our bodies produce an amino acid, even if
we do not get it from the food we eat.
• Nonessential amino acids include: alanine, asparagine, aspartic acid,
and glutamic acid.
3. CONDITIONAL AMINO ACIDS
• Conditional amino acids are usually not essential, except in times of
illness and stress.
• Conditional amino acids include: arginine, cysteine, glutamine,
tyrosine, glycine, ornithine, proline, and serine.
 Peptide bond
• The amino acids of a polypeptide are
attached to their neighbors by
covalent bonds known as a peptide
bonds.
• By condensation reaction (water
removal)
• Carboxyl group of the amino acid at
the end of the growing polypeptide
chain reacts with the amino group of
an incoming amino acid
• Few (2-20) amino acids are joined in
this fashion, the structure is called an
oligopeptide.

• When many amino acids are joined,

the product is called a polypeptide.
 Protein Structure
• Four levels of protein structure
• 1. Primary structure
All covalent bonds (mainly peptide
and disulfide bond) linking amino acid
residues in a polypeptide chain

Important element of primary

structure is the sequence of amino acid
residues
2. Secondary structure
• Stable arrangements of amino acid residues giving rise to specific
structural patterns.
• local folded structures that form within a polypeptide due to
interactions between atoms
• Common types of secondary structures are 

1.  α helix 2. β pleated sheet

• Both structures are held in shape by hydrogen bonds, which form
between the carbonyl O of one amino acid and the amino H of
another
3. Tertiary structure

• Three-dimensional folding of a polypeptide

• Due to interactions between the R groups of the amino acids
• hydrogen bonding, ionic bonding, dipole-dipole interactions, and
London dispersion forces 
• Hydrophobic interactions - hydrophobic R groups cluster together on
the inside of the protein, leaving hydrophilic amino acids on the
outside to interact with surrounding water molecules
4. Quaternary structure
• Two or more polypeptide subunits, arrangement in space is referred
to as quaternary structure
• E.g. hemoglobin
• Contain two α and two β polypeptide subunits
• DNA polymerase
• Contain 10 polypeptide subunits
• Interactions, such as hydrogen bonding and London dispersion forces
also hold the subunits together to give quaternary structure
 Lipids
• Greek: lipos, means fat or lard
• are insoluble in water and highly soluble in one or more of
the following solvents: ether, chloroform, benzene and
acetone
• play a wide variety of roles in plant and animal tissues
• Fats and oils are the principal stored forms of energy in
many organisms
 Functions of Lipids
• Lipids are concentrated source of energy. One gram fat gives 9 K calories.

• It serves as a cushion for the vital organs and protects them from external
shocks or injuries.

• Lipids are the structural materials of cells and membranes

• Lipids serves as insulator for our body

• Lipids are the carrier / reservoir of fat soluble vitamins

Types of Lipids
• Lipids consist of two types of molecules
1. glycerol 2. fatty acids

1. Glycerol

• Made up of three carbon atoms.

• Each of these has a hydroxyl group
attached to it.
• Hydrogen atoms occupy the
remaining positions.
2. Fatty Acids

• fatty acids are hydrocarbon derivatives, which are long chain

carboxylic acids containing up to 24 carbon atoms

• the most common fatty acids in plants and animals are the even-
numbered C16 and C18 species such as palmitate and stearate

• fatty acid are classified as saturated (where all the carbon are
saturated with hydrogen) or unsaturated ( which contain one or
more double bonds)
 Triglycerides

• The fats and oils found in animals and plants are triglycerides

• Triglycerides are:
• esters of fatty acids and glycerols
• simple lipids
• The link between the glycerol molecule & each fatty acid is an ‘Ester
Link
• important as the storage form of fat in the human body
 Phospholipids
• In phospholipids one of the fatty acids
of a triglyceride is substituted by a
phosphate group.
• Glycerol having 1 phosphate group
and 2 fatty acids
Formation of a phospholipid
• Hydrogenation of fats and oils:

• The difference between fats and oils is:

fats are solid in room temperature and oils are liquid in room
temperature.

• Hydrogenation is the process of converting liquid oil to

solid fat by adding hydrogen to some of the double bond
of the unsaturated carbon chain in presence of nickel as
catalyst; e.g., Margarine .