PROTEINS

by Mohamed kasala

Proteins
 Introduction
 Proteins are the most abundant organic molecules of the living system.
They occur in every part of the cell and constitute about 50% of the
cellular dry weight. Proteins form the fundamental of structure and
function of life.
 Protein is the composite term for hundreds of thousands of different
individual proteins present in our diet .
 The word protein is derived from the Greek word (proteios) which means
primary, protein are high molecular weight (5000 to 2500000) substance.
 About half the dry weight of living materials is protein .
Definition
Proteins are macromolecules with a backbone
formed by polymerization of amino acids in
polyamide (peptide bond) structure.
General formula
C400H620N100O120p1S1
Elemental composition of proteins
Proteins are predominantly constituted by five
major elements in the following proportion.
Carbon : 50 – 55%
Hydrogen : 6 – 7.3%
Oxygen : 19 – 24%
Nitrogen : 13 – 19%
Sulfur : 0 – 4%
Structural Differences Between Carbohydrates,
Lipids, and Proteins
 The peptide bond
 A peptide bond (amide bond) is covalent chemical bond
formed between molecules when carboxylic group of
one amino acid react with the amine group of the other
amino acids releasing a molecule of water
 A tripeptide consist of amino acids composed, glycine,
alanine and serine
 Peptidy, polymers
 A few amino acids in a chain are called a poly peptide
 Protein usually composed of 50 to 400 amino acids
Formation of a Dipeptide

Dehydration synthesis
Functions of protein in the body
 Proteins serve multiple functions in cells and tissues. The function
of a protein is determined by the amino acid sequence
 Proteins can fulfill a variety of functions in the body:
 Building material: many proteins have an important structural role
inside and outside the cell. The main structural protein and most
abundant protein in the body is collagen. Skin, tendons, cartilage,
bone, and connective tissue contain a lot of collagen
 Enzymes: enzymes are proteins that speed up a biochemical
reaction.
 Transporters: transporters assist with import or export of different
molecules across the cell membrane.
 Hormones: hormones are messengers that circulate in the blood.
They are released from a particular tissue into the bloodstream to
signal to distant tissues. For example, insulin is released by the
pancreas and travels to muscle and fat tissue to promote glucose
uptake. Chemically, hormones are either polypeptides or steroids.
 Antibodies: antibodies circulate in the body and are
involved in immune defense against pathogens such as
bacteria and viruses. They are also referred to as
immunoglobulin's and are secreted by plasma cells.
 Regulation of fluid balance: proteins play an important
role in making sure that water in the body is appropriately
distributed across the bloodstream (intravascular
compartment), the space between cells (intercellular
compartment), and inside cells (intracellular compartment).
Protein structure
 Proteins come in many different sizes and shapes.
 For example, cytochrome c, a protein that transfers
electrons, has only one polypeptide chain of 104 amino
acids. Yet myosin, the protein that makes muscles
contract, has two polypeptide chains with some 2,000
amino acids each, connected by four smaller chains. It is
called a multimeric protein.
 No matter their size, all proteins have a primary,
secondary, and tertiary structure. Some also have
quaternary structure.
Structure of proteins
Proteins exhibit four levels of organization
1: Primary structure: -
 Is the sequence in which amino acids are arranged in a
proteins
 The amino acids sequence of protein determines the
function of protein even a change of just one amino acids
in sequence drastically alters properties of the entire
protein molecule
For example
 The hemoglobin molecules has 574 amino
acids units changing one specific amino acids
in the sequence result in defection hemoglobin
found in protein suffering from sickle –
cellaneamia
Val-Hist-Leuc-Thr-Pro-Glu-Glu-Lys
Normal hemoglobin’s

Val-Hist-Leuc-Thr-Pro-Glu-Val-Lys
sickle cell hemoglobin’s
2: Secondary structure
The secondary structure of proteins is the hydrogen-bonded
arrangement of the backbone of the protein, the polypeptide chain.
 Secondary structure determines the coiling of the polypeptides
chain into a helical structure because of folding or twisting two
types
a. Alpha Helix
Three dimensional arrangement of amino acids with the poly
peptide chain held by H bonds between H of N-H group and the O
of the C=O the fourth amino acids long the chain looks like a coiled
( telephone card)
b. Beta Pleated sheet
Poly peptide chains are arranged side by side hydrogen bonds forms
between chains R group of extend above and below the sheet
3: Tertiary structure
 Once it has started folding, the protein eventually
tightens into a specific three-dimensional shape, called its
tertiary structure.
 The three-dimensional arrangement of protein structure
is referred to as tertiary structure.
 Just like humans have unique sets of fingerprints,
every protein has a unique tertiary structure, which is
responsible for its properties and function.
There are three kinds of bonds involved in tertiary
protein structure:
1.Hydrogen bond 2. Disulphide bond
3.Ionic interaction 4. Hydrophobic interaction
4: Quaternary structure
Proteins that have more than one polypeptide chain require
a higher level of organization.
for example hemoglobin carries oxygen in blood four
polypeptide chains each chain has a hemi group to bind
oxygen
Classification of proteins
Classification as per composition
Proteins are classified into three groups as per the
composition
A. Simple proteins :
Yields only amino acids and no other major organic or in
organic, hydrolysis product.
B. Conjugated proteins:
Yields amino acids and other organic and organic
components e.g.
- Lipoproteins: protein containing lipids
- Glycoprotein’s: protein containing carbohydrates
-Phosphoproteins: protein containing phosphorous
-- Mettaloproteins: protein containing metal ions Fe+2
C. Derived proteins:
Classification as per biological function e.g.
- Enzymes the body catalyst
- Hormones such as growth hormones, insulin and others
- Storage proteins such as albumin in egg
- transport protein those that carry things from one place to
an other
- Protective protein such as immunoglobins
A. Simple proteins :
classification per solubility
(Fibrous proteins and globular proteins)
The fibrous proteins are insoluble water and include the
following
Collagens in bone, teeth, tendons, skin.
Elastins found in ligaments, the walls of blood.
Keratins in hair, wool, animal hooves, nails.
 Myosin’s in muscles
 Globular proteins are soluble in water or water with 5%
NaCl and include the following
-albumins in egg white and blood .
-globulins that are part of body defense mechanism against
The proteins speak :
“We are the basis of structure and function of
life; Composed of twenty amino acids, the
building blocks; Organized into primary,
secondary, tertiary and quaternary structure;
Classified as simple, conjugated and derived
proteins.”
Denaturation of proteins
Denaturation of protein it is lose native physics and chemical and
biological properties since the bonds that’s stabilized the protein is
broken down.
Factors that effects denaturation
Physical factors such as temperature, pressure, ionizing radiation
causes the protein to lose its biological activity.
Chemical factors such as acids , alkalis , organic solvent , detergents
(cleaning agents) , and heavy metal salts(Hg , Cu , Ba , Zn , Cd)
 
Reactions of proteins
Ninhydrin reaction
Ammonia, many amines, peptides, and any protein will give a blue
purple color when boiled with ninhydrin a benzene type compound.
Proteins +ninhydrin =blue color +CHO + CO2
Best Sources of Protein
 Eating Too Much Protein
 Risk of heart disease
 Risk of kidney stones
 Risk of calcium loss from bones
 Risk of colon cancer
 Displacement of other nutrient-rich, disease
preventing foods
 Eating Too Little Protein
 Protein-energy malnutrition (PEM)
– Protein is used for energy rather than its other
functions in the body
– Other important nutrients are in short supply
– More prevalent in infants and children
 17,000 children die each day as a result
 Summary

1. Proteins are nitrogen containing, most abundant

organic macromolecules widely distributed in animals
and plants.
2. Proteins are polymers composed of L-amino acids.
They are 20 in number and classified into different
groups based on their structure, chemical nature,
nutritional requirement
3.Amino acids possess two functional groups namely
carboxyl ( COOH) and amino ( NH2).
4.The structure of protein is divided into four levels of
organization. The primary structure represents the linear
sequence of amino acids. The twisting and spatial
arrangement of polypeptide chain is the secondary structure.
Tertiary structure constitutes the three dimensional structure
of a functional protein. The assembly of similar or dissimilar
polypeptide subunits comprises quaternary structure.
5. Proteins are classified into three major groups. Simple
proteins contain only amino acid residues (e.g. albumin).
Conjugated proteins contain a non-protein moiety known as
prosthetic group, besides the amino acids (e.g.
glycoproteins). Derived proteins are obtained by
degradation of simple or conjugated proteins.