PROTEINS

FOLDED POLYPEPTIDES
 Try This!

 1. Proteins are composed of which group

of elements?
A. CHOP
B. CHO
C. CHOS
D. CHON
 2. The building blocks of proteins are the _

A. Fatty acids
B. Amino acids
C. Nucleotides
D. phospholipid
 3. Amino acids are linked together by
_____ bond to form protein molecule.

A. hydrogen bond
B. glycosidic bond
C. peptide bond
D. phospodiester bond
 4. This protein structure refers to the linear
sequence of amino acids in a polypeptide
chain.
A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure
 5. Proteins are also classified based on
functions. Which of the following is a
transport protein?
A. lipase
B. hemoglobin
C. actin
D. insulin
Composed of Carbon, Hydrogen, Oxygen, &
Nitrogen (CHON)

 Proteins help build and repair tissues and

muscles
 Amino acids are the building
blocks/monomers of proteins. There are
20 Amino acids.
 Of the 20, there are 9 essential amino
acids
Essential Amino acids are those that the body
can not produce and are therefore taken from the
foods that we eat
 The 9 Essential Amino Acids:
 Histidine, Isoleucine, Leucine, Lysine,
Methionine, Phenylalanine, threonine,
trytophan, and valine
 Complete proteins – contain adequate
proportion of all nine (9) essential amino acids
necessary for the dietary needs of humans and
other animals. (Animal proteins, Soya)
The 20 Amino Acids
 Charged: Arginine (Arg), Lysine (Lys), Aspartic Acid
(Asp), Glutamic Acid ( Glu)

 Polar: Glutamine (Gln), Asparagine (Asn), Histidine

(His), Serine (Ser), Threonine (Thr), Tyrosine (Tyr),
Csyteine (Cys), Methionine (Met), Trytophan (Trp)

 Hydrophobic: Alanine (Ala), Isoleucine (Ile), Leucine

(Leu), Phenylalanine (Phe), Valine (Val), Proline (Pro),
Glycine (Gly)
Functions of amino acids
 Arginine – is converted into nitric oxide which helps blood vessels
to relax and expand.
 Lysine – concentrated in muscle tissue and helps in the absorption
of calcium from the intestinal tract, promotes bone growth.
 Aspartic Acid – Major role in metabolism, plays a role in hormone
production and for normal nervous system function
 Glutamic acid – important for protein synthesis
 Glutamine –for biosynthesis of proteins
 Asparagine – involved in nerve and brain tissue function


 Histidine – for growth and tissue repair
 Serine- needed for fat metabolism, muscle growth
 Threonine – for normal growth, maintain protein balance
 Tyrosine – used in protein supplements to treat the
inherited diesease phenylketonuria
 Cysteine- sulfur-containing, important structural and
functional components of proteins and enzymes
 Methionine- prevent liver damage
 Trytophan- for normal growth of infants and nitrogen
balance in adults
 Alanine-involved in metabolism of trytophan and
pyridoxine
 Isoleucine-increase endurance, repair muscle
tissue
 Leucine- for protein synthesis
 Phenylalanine- makes the body healthy
 Valine – for protein synthesis
 PROTEIN STRUCTURE
 The basic functioning of cells is entirely dependent
upon the structure of their proteins

 The gene, or sequence of DNA, determines the

unique sequence of amino acids in each peptide
chain.

 A change in nucleotide sequence of the gene's

coding region may lead to a different amino acid
being added to the growing polypeptide
chain, causing a change in protein
structure and therefore a change in function
PRIMARY STRUCTURE
 The primary structure of a protein refers to the
sequence of amino acids in the polypeptide
chain.

 The primary structure is held together by

peptide bonds that are made during the
process of protein biosynthesis

 An average protein has 300 amino acids

SECONDARY STRUCTURE
It is due to the interactions, like coiling
or folding, of a polypeptide chain,
using weak hydrogen bonds, that
gives protein its 3D shape.
 2 TYPES OF SECONDARY STRUCTURE
 1. Alpha helix structure – resembles a coiled spring and is
secured by hydrogen bonding in the polypeptide chain.
 The length of the helix is determined by certain amino acids
that will not participate in these structures
(e.g. proline)

© Dr Gary Kaiser
2. Beta pleated
sheet
Appears to be folded or
pleated held together by
hydrogen bond between
polypeptide units that lie
adjacent to one another

Alpha Helix structure of DNA is more stable

than Beta pleated Sheet structure. It is stabilized by the
regular formation of hydrogen bonds.
TERTIARY STRUCTURE
 The comprehensive 3D
structure of the polypeptide
chain of a protein.
 Several types of bonds and Secondary structures
forces hold a protein in its fold on themselves to
tertiary structure namely form the tertiary
hydrophobic interactions, structure of the
hydrogen bond, ionic
bond, disulfide bridge protein.
(cysteine-cysteine bond),
van der Waals forces
(distance-dependent)

© Anne-Marie Ternes
 Chain B of Protein Kinase C

© Max Planck Institute for Molecular Genetics

MIL1 protein
QUATERNARY STRUCTURE
Some proteins are
made of several
polypeptide subunits

(e.g. hemoglobin)
It contains 4 subunits;
2 alpha and beta
subunits
Protein Kinase C
© Max Planck Institute for Molecular Genetics
 3 CLASSES OF PROTEINS BASED ON
STRUCTURE

Fibrous proteins
Are typically elongated and insoluble
Involved in structure: tendons, ligaments, blood clots
(e.g. collagen in connective tissues like tendons and
ligaments, keratin in hair, nails, feathers, horns, claws,
fibrin in blood clots)
Contractile proteins in movement: muscle,
microtubules, cytoskeleton, mitotic spindle, cilia, and
flagella like actin and myosin
Globular proteins

 Are generally compact, soluble, and

spherical in shape
 most proteins which move around (e.g.
ovalbumin in egg, casein in milk)
 Proteins with binding sites:
enzymes, hemoglobin, immunoglobulins
(antibodies), membrane receptor proteins
 Intermediate Proteins
 AreIntermediate filaments (IFs),
microfilaments (MFs), and
microtubules (MTs) are the key
structural proteins that form the
cytoskeleton.
Classes of Proteins Based on
Composition

e.g. Albumins, globulins, collagen

e.g. glycoproteins, nucleoproteins, lipoproteins, phoshoproteins

Proteins classified by function
 CATALYTIC: enzymes (amylase, glucase, lipase, pepsin,
trypsin, ATPase, sucrase, )
 STORAGE: ovalbumin (in eggs), casein (in milk), zein (in
maize)
 TRANSPORT: hemoglobin, carrier proteins in cell membrane
 COMMUNICATION: hormones (e.g. insulin, glucagon, FSH,
growth hormone, neurotransmitters)
 CONTRACTILE: actin, myosin, dynein (in microtubules)
 PROTECTIVE: Immunoglobulin (antibodies), fibrinogen, fibrin
(blood clotting factors)
 TOXINS: snake venom
 STRUCTURAL: cell membrane proteins, keratin (hair),
collagen, fibroin in silk
Level of malnutrition
 KWASHIORKOR (Ga language of Ghana) “the sickness
the baby gets when the new baby comes”; also called
“disease of a deposed child”)
 due to inadequate protein intake
 Also known as edematous malnutrition
 Fluid retention (edema),enlarged liver,

 MARASMUS – worse condition than kwashiorkor

 - severe form of protein-energy malnutrition
- loss of body fat & muscle
- worst result of Anorexia nervosa (eating disorder)
Let’s Check!!!
 1. Give the general function of protein
 2. Elements that make up proteins
 3. Building blocks of proteins
 4. Describe essential amino acids. There
are how many essential amino acids.
 5. Describe complete proteins
 6. What bond joins amino acids together to
form polypeptide chain/protein molecule?
 7. Why is protein structure important?
 8. Classify the following proteins accdg. to
structure?
 A. enzymes
 B. collagen
 C. keratin
 D. hemoglobin
 9. Classifying proteins based on functions
CATALYTIC, STORAGE, TRANSPORT, COMMUNICATION,
CONTRACTILE, PROTECTIVE, TOXINS, STRUCTURAL,

1. Actin
2. Ovalbumin
3. insulin
4. antibodies
5. pepsin
6. hemoglobin
7. collagen
 TASK
 Explain how the following are important in the
given areas. Cite specific example of proteins
involved and describe its participation.
 (1) Proteins used for the treatment of certain
conditions/diseases.
 (2) Proteins help us resist infection
 (3) Proteins help in chemical reactions in the
body
 COMPOSITION BUILDING TYPES OR FUNCTIONS
BIOMOLECULE BLOCKS EXAMPLES
         
 
1. Carbohydrates  

         

2. PROTEINS
 

         

3. LIPIDS
 

         

4. NUCLEIC
ACIDS