BY MISS CHANDA

Student should be able to:

➢ describe the structure of amino acid and
proteins
➢ demonstrate the bond found in proteins
➢ relate how amino acids form proteins
➢ explain the different levels of structure in
proteins and the various bonds at each level
➢ identify and illustrate the 20 amino acids and
their varying nature
➢ understand the roles of proteins and their
functions in biological systems
 Proteins are composed primarily of carbon, hydrogen,
nitrogen,and oxygen. However, some contain sulfur.
 They are all composed of structural monomers called amino
acids.
 They form the structural and functional moterial of various cells
and tissues
 Their differences from organism to organism is due to
differences in the DNA which contains the instructions for their
formation giving rise to differences such as varying Eye color,
Blood type etc
 They account for over 50% of dry cell mass
 Structure: Building structural components of organisms
( collagen, elastin, keratin, microtubules, microfilaments)
 Regulation of metabolic processes: Hormones (insulin)
 Carrying out of metabolic processes: biological catalysts
Enzymes
 Transport Proteins: Carrier proteins, Protein pumps,
Transport of materials through membrane phospholipid
layers
 Self and non-self cell recognition: Major histocompatibility
complexes (Tissue rejection, immune responses).
 Membrane receptors: Hormone receptors
and neurotransmitter receptors.

 Defense:antibodies

 Nutrition/storage proteins: ovalbumin in

eggs

-the functions of proteins depends on the

amino acid content and the sequence of the
amino acids
➢ Amino acids the contain an amine (-NH2) group and a
carboxylic group as part of their composition.
➢ They have a central carbon with the amine group, a
carboxyl group, a hydrogen, and a variable group (R
group) attached to it.
➢ The variable group is what is different from amino acid to
amino acid and it is what give the amino acid its identity.
➢ There are twenty different variable groups, therefore there
are twenty different amino acids.
 A peptide bond is the bond that is created
when two amino acids are covalently bonded
together.
 The carboxyl group of the first is bonded to the
amine group of the second.
 This is carried out by a dehydration synthesis
reaction with the loss of a water molecule.
 This forms a dipeptide (a peptide containing
two amino acid molecules).
 A polypeptide/protein consists of several
amino acids linked by peptide bonds
➢ Proteins are very complex molecules and
their shape or structure determines their
function.
➢ There are 4 levels of structure:
a. Primary Level
b. Secondary Level
c. Tertiary Level
d. Quaternary Level
➢ If any level of structure is changed it can
create faulty or nonfunctioning proteins
 The Primary Level is the linear sequence of amino
acids linked by peptide bonds
 determined by the number of amino acids, the type
of amino acids, and the sequence of the amino
acids in the polypeptide chain.
 The Secondary Level is due to interactions
between amino acids in the chain
 usually due to hydrogen bonding between
oxygen and hydrogen atoms in different
amino acids chains
 Two general forms are taken:
1. Alpha helix, a spiral structure, common
in globular proteins such as hemoglobin
and myoglobin, OR
2. a Beta pleated sheet structure, common
in structural proteins.
➢ The Tertiary Level is due to the “folding
over” of the alpha helical or beta pleated
sheet structure on itself.
➢ This configuration is due again to
hydrogen bonding, hydrophobic
interactions, ionic bonding interactions, and
the interaction of sulfur groups on the
variable groups of some amino acids
forming weak interactions called disulfide
bridges.
 Two broad classes of proteins termed
globular proteins and fibrous proteins exhibit
secondary structure and tertiary structure
 Globular proteins are compactly folded and
coiled, whereas fibrous proteins are more
filamentous or elongated.
➢ Proteins such as myoglobin contain
hydrophobic amino acids and water soluble
polar amino acids
➢ The hydrophobic amino acids usually fold
inside the structure of the protein
 The Quaternary Level of structure is due to the
interactions of more than one polypeptide chain to
form the complete, functional protein.
 The chains are held together by a variety of bonds
similar to those in the tertiary structure
 Hemoglobin and antibodies exhibit this level of
structure.
 Breakdown occurs in the stomach and small
intestines
 by a process called Proteolysis
 HCl in the stomach denatures protein
structure
 Pepsin enzyme hydrolyses proteins to smaller
polypeptides and some free amino acids
 Pancreatic enzymes such as trypsin,
chymotrypsin, elastase and carboxypeptidase
further break down proteins into simple
amino acids in small intestines
 The simple amino acids are then transported
from the small intestines across the intestinal
wall to the liver for protein synthesis and
back to the blood stream
 Excess amino acids are converted to glucose
or ketones that are then decomposed into
hydrocarbons and nitrogenous waste
excreted by kidneys
 Results in the unfolding and disorganisation
of the protein structure which are not
accompanied by hydrolysis of peptide bonds
 Proteins can be denatured by heat, strong
acids and bases, detergents and ions of heavy
metals such as lead and mercury
 Rarely reversible, most denaturation is
permanent
 Denatured proteins are often insoluble and
therefore form precipitate in solution