 BIOMOLECULES

 3. PROTEINS

 are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid
residues (the monomers).
 A linear chain of amino acid residues is called a polypeptide.
 Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism.


Protein Functions:

 1.Antibodies - are specialized proteins involved in defending the body from antigens (foreign
invaders).

 2. Contractile Proteins - are responsible for movement.

Ex: actin and myosin
 3.Enzymes - are proteins that facilitate biochemical reactions. They are often referred to as catalysts
because they speed up chemical reactions.
 Ex: enzymes lactase and pepsin
Antibodies-defend against bacteria, viruses, and other foreign intruders
actin and myosin- muscle contraction and movement.
enzymes lactase- breaks down the sugar lactose found in milk and pepsin- digestive enzyme that
works in the stomach to break down proteins in food.

 4.Hormonal Proteins - are messenger proteins which help to coordinate certain bodily activities.
Ex. 1. insulin
2. oxytocin
3. somatotropin
 5. Structural Proteins - are fibrous and stringy and provide support.
 Ex. 1. keratin
2. collagen & elastin
insulin - glucose metabolism by controlling the blood-sugar concentration
2. oxytocin - stimulates contractions in females during childbirth
3. somatotropin - a growth hormone that stimulates protein production in muscle cells.

5. 1. keratin- strengthen protective coverings such as skin, hair, quills, feathers, horns, and beaks
2. collagen & elastin- elastin provide support for connective tissues such as tendons and ligaments.

 6. Storage Proteins - store amino acids.

Examples include ovalbumin and ferritin.
 7. Transport Proteins - are carrier proteins which move molecules from one place to
another around the body.
Ex. hemoglobin and cytochromes.
 6. Ovalbumin is found in egg whites and casein is a milk-based protein.
Ferritin stores iron in hemoglobin.
7. Hemoglobin transports oxygen through the blood via red blood cells.
Cytochromes
Protein Structure:

 Most proteins fold into unique 3-dimensional structures.

 The shape into which a protein naturally folds is known as its native conformation.
 If you were to draw the structure of a general 2-amino acid, you would probably draw it like this:

 However, for drawing the structures of proteins, we usually twist it so that the "R" group sticks out at
the side.

 That means that the two simplest amino acids, glycine and alanine, would be shown
as:

 Glycine and alanine can combine together with the elimination of a molecule of water to produce a
dipeptide.
 The linkage shown in blue in the structure of the dipeptide is known as a peptide link.

 If you joined three amino acids together, you would get a tripeptide.
 If you joined lots and lots together (as in a protein chain), you get a polypeptide.
 A protein chain will have somewhere in the range of 50 to 2000 amino acid residues.
 A protein chain .
 The "R" groups come from the 20 amino acids which occur in proteins. The peptide chain is known as
the backbone, and the "R" groups are known as side chains.

Four distinct aspects of a protein's structure:

 1. Primary structure: the amino acid sequence. A protein is a polyamide.

 2. Secondary structure: regularly repeating local structures stabilized by hydrogen
bonds. The most common examples are the α-helix, double or triple helix and β-sheet.
 3. Tertiary structure: The tertiary structure of a protein is a description of the way the
whole chain folds itself into its final 3-dimensional shape. The tertiary structure is what
controls the basic function of the protein.
 4. Quaternary structure: the structure formed by several protein molecules (polypeptide
chains), usually called protein subunits
Linear sequence of amino acids
Polypeptide chain is coiled. Simple alpha helix like a telephone cord.
Double or triple helix – two to three polypeptide chain are coiled.
Ex. Double – keratin ; triple – collagen – forms tendon ligaments and cartilage
3. Bond – hydrogen bond, ionic bond, disulphide bridges


The Mighty 20 Amino Acids

Non - Essential amino acid – 1-8; 15&16; 19

essential Amino acid –the rest


 Amino acids can be called as the building blocks of our life.
 They get combined in an unlimited number of configurations to construct all the required proteins
with which our body is built. There are essentially 20 common amino acids that keep us alive, healthy
and energetic. If deficiency occurs in an
individual amino acid, it may create
serious problem to our health system.

1. Alanine
o It is one of the most significant among the 20 common amino acids. It offers
energy to your system. It releases into the blood stream during exercise time and
induces carbohydrate-consuming effect to the health system.
2. Arginine
o Synthesized normally in the body, arginine is known to be a semi-essential amino
acid. Deficiencies may include poor wound healing, weakness in muscles, hair
loss, irritations in skin, and constipation.
3. Asparagine
o It is needed to maintain homeostatic balance in the nervous system.
4. Aspartic Acid
 Aspartic acid is one of two acidic amino acids. It promotes enzyme activity, maintenance of solubility
in the body, as well as homeostasis in ionic characters of proteins.
5. Cysteine
 It is present only at the rate of 2.8% into proteins but it provides the 3-dimensional stability of the
protein molecule. It also plays a crucial role in the metabolic process of many important enzymes.
6. Glutamic Acid
 It is one of the important amino acid among all 20 common amino acids. It is responsible for
transportation of glutamate and other amino acids to the blood barrier.
7. Glutamine
 Glutamine is able to eliminate excess ammonia from the body system. It enhances immune system.
Apart from that, glutamine possesses anti-anxiety property that permits the mind to be relaxed.
8. Glycine
 Glycine is known as the second most common among the group of amino acids. It helps transforming
harmful toxic substances within the body to a non-toxic form.

9. Histidine
 Histidine is required for infant development. Histidine deficiency may result in eczema, a kind of skin
disease.This results in speech disorders and mental retardations among infants and toddlers.
10. Isoleucine
 This amino acid is particularly important for stimulating the brain in order to produce mental alertness.
11. Leucine
 It is particularly effective in producing other essential biochemical compounds in the body - body energy and
mental alertness.

12. Lysine
 Lysine is one of the most important amino acid among all 20 common amino acids. It functions
against herpes virus in particular by providing body required nutritional supplements.
13. Methionine
 It is an essential amino acid which functions at initiating the translation of messenger RNA.
14. Phenylalanine
 This amino acid profoundly affects brain cells at biochemical level.
15. Proline
 It significantly affects human nutrition. It is believed to act as a source of nitrogen.
16. Serine
 Serine is intimately related to various bodily functions such as fat metabolism, tissue growth,
enhancement of immune system and many more. It is an essential ingredient of brain protein.
17. Threonine
 It helps in maintaining protein balance and also in assisting collagen formation.
18. Tryptophan
 This is particularly needed in the body for the production of vitamin B3.
19. Tyrosine
 This is crucial in building link between dopamine and norepinephrine. It also reduces fat by
suppressing appetite.
20. Valine
 It is effective in promoting tissue growth and maintaining nitrogen balance in the health system.