GOOD MORNING

Dr. SHAIKH ANALHAQ A.

1ST YEAR
POSTGRADUATE
DEPT. OF
ORTHODONTICS
BASICS OF PROTEINS
Proteins are polymers of L--
amino acids, which are bonded
by peptide bonds.
Proteins are made of 20 amino
acids linked by peptide bonds

Polypeptide backbone is the

repeating sequence of the N-C-C-
N-C-C in the peptide bond

The side chain or R group is not

part of the backbone or the
peptide bond
Amino acid: Basic unit of protein

NH3 +
C COO -

Carboxylic acid
Amino
group
group
H
An amino
acid
 20 Amino acids

Nonpolar,
Glycine
hydrophobic
(G)

Polar,
uncharged

Polar, charged
 Alcohol dehydrogenase oxidizes alcohols to aldehydes or ketones

Proteins play key roles in a living system

Three examples of
protein functions Alcohol
Catalysis: dehydrogenas
e oxidizes
Almost all chemical alcohols to
reactions in a living cell aldehydes or
are catalyzed by protein ketones
enzymes.
Transport:
Haemoglobin
Some proteins carries
transports various oxygen
substances, such as
oxygen, ions, and so on.
Insulin
Information transfer: controls the
For example, hormones. amount of
sugar in the
blood
General properties of protein
Taste- Tasteless. Hydrolytic or derived
products are bitter.
Odor- odorless. On heat drying burning
odor.

Viscosity- It depends upon the pH,

concentration, size and shape of the
molecule.

Shape- There is a wide variation In the

protein shape. It may be globular, oval,
fibrous or elongated .
Elemental composition of
protein
5 major elements
Carbon- 50-55%

Hydrogen- 6-7.3%

Oxygen- 19-24%

Nitrogen- 13-19%

Sulfur- 0-4%
Classification of proteins
Based on chemical composition:
Simple proteins: Contain amino
acids(E.g: Serum albumin, serum
globulins, keratin etc)
Conjugated proteins or compound
proteins: Conjugated groups + amino
acids (E.g.: Egg albumin, hemoglobin,
immunoglobulins etc.)
Derived proteins: Partial hydrolysis of
simple or compound proteins.(E.g:
Gelatin, proteoses & peptones etc.)
Based on shape:
Globular proteins: Spherical or
oval
E.g.: Hemoglobin, Albumin, and
Enzymes.
Fibrous proteins: Elongated and
fiber-like structures.
E.g.: Keratin, Collagen etc.
Based on biological function:
Catalytic proteins
E.g.: Hexokinase, Amylase etc.
Defence proteins
E.g.: Immunoglobulins as
antibodies
Structural proteins
E.g.: Keratin, Collagen
 Hormonal proteins
E.g.: Growth hormone, Insulin etc.
Contractile proteins
E.g.: Actin, Myosin and
Tropomyosin .
Transport proteins
E.g.: Serum albumin
Storage proteins
E.g.: Ferritin
Visual proteins
E.g.: Rhodopsin & Iodopsin
 Membrane proteins
E.g.: Sodium potassium pump
Hemostatic proteins
E.g.: Fibrinogen, Prothrombin.
Buffer proteins
E.g.: Plasma proteins, Hemoglobin
Respiratory proteins
E.g.: Hemoglobin, Myoglobin
Receptor proteins
E.g.: Insulin receptors, Glucagon
receptors, Steroid hormone receptors etc.
Protein structure:
Made up of one or more polypeptide
chains.

Proteins with a single polypeptide

chain- monomeric proteins.

Proteins with more than one

oligomeric proteins.

Each polypeptide chain in an oligomeric

protein is called subunit or monomer.
 Examples for oligomeric proteins are
hemoglobin, lactate dehydrogenase.
Structural organisation of proteins

1. Primary structure

2. Secondary structure

3. Tertiary structure

4. Quaternary structure
Hierarchical nature of protein structure

Primary structure (Amino acid sequence)

Secondary structure -helix, -sheet

Tertiary structure Three-dimensional
structure formed by assembly of
secondary structures

Quaternary structure Structure
formed by more than one polypeptide
chains
Primary Structure

It
is the amino
acid sequence
(1940) that
exclusively
determines the
3D structure of a
protein
20 amino acids
modifications do
occur post
translationally
 Secondary structure

Regular patterns of hydrogen bonding in

proteins result in two patterns that emerge
in nearly every protein structure known:
the -helix and the
-sheet.

Thelocation of direction of these periodic,

repeating structures is known as the
secondary structure of the protein.
-helix -sheet

Secondary structures, -
helix and -sheet, have
regular hydrogen-
bonding patterns.
 - pleated sheet
-helix is the is an extended
most common structure.
secondary
structure found
in proteins. - pleated
structure is
Mostcommonly stsbilized by
seen in globular hydrogen
protein. bonding.
Tertiary structure
Tertiary structure of protein refer to
the further folding of secondary
structure of polypeptide chain giving
the compact three dimensional
conformation.

Tertiary structure results in the

orientation of hydrophobic side chain
towards the water free interior and the
hydrophilic polar groups towards the
surface of the protein.
Quaternary structure
Protein having more than one
polypeptide chain show more
level of higher structure called
the quaternary structure.

Quaternary structure refer to the

spatial arrangement of the
subunits of an oligomeric
protein.
Denaturation of
proteins
The process of disorganization of
native protein structure is called
Denaturation.

Denaturation involves the loss of

secondary , tertiary and
quaternary structures without
breaking the primary structure.
 Denaturation involves a changes
in physical, chemical and biological
properties of protein .

Decreases the solubility, increase

the precipitiability and increase the
viscosity of proteins.
Protein Energy Malnutrition
(PEM)
Deficiency disease caused in the
infants due to Food Gap between the
intake and requirement.

It affects children under 5 mostly

belonging to the poor underprivileged
communities.

PEM is particularly serious during the

post-weaning stage and is often
associated with infection.
Types
Marasmus

Kwashiorkor

Marasmus Kwashiorkor
Marasmus
It is an overall deficit of food
intake which results from near
starvation from with deficiency of
protein and non-protein nutrients.
Clinical Features
Age 1 and 3 years

Weight loss

Wasting of subcutaneous fat and muscle

Head of the child seems larger than the

body

Very little hair

Ribs of the child are visible

Adomen of the child appears

extended and protruding

Child suffers and is more prone to

infections

Skin has some pigmentation

Kwashiorkor
Kwashiorkor is another form of
PEM, is it uncommon in the
children under one year of age.

It is associated with primary

dietary protein deficiency.
Clinical Feature
Three essential features of
kwashiorkor are

Growth failure

Oedema

Mental changes
Oral Manifestation
Tongue- Bright reddening, loss of papillae.
In kwashiorkor odema of tongue and
may develop scalloping around lateral
margins.

Xerostomia- Mouth becomes dry.

Jaws- Decreased overall growth of jaws.

Teeth- Delayed eruption

Periodontal membrane
Gingiva and periodontal ligament
membrane exhibit varying degree
of degenration.

Maxillofacial gangrene- Severe

infection, spread in mouth from
necrotizing gingivitis.

Extra oral- Bilateral angular

cheilosis, fissuring of lips.
Amylodosis
Itis also called as amyloid
disease.

It is deposition of amyloid in the

tissue.

Type A amyloid is a fibrillar

protein of unknown origin.
Clinical Feature
Commonly affected kidney,
heart, G.I tract, liver, respiratory
tract, skin, eyes, nerves and
spleen.

Fatigue, weakness, ankle edema,

weight loss.

Purpuric spot
Oral Manifestation
There are difficulty in
Chewing
Swallowing
Speech

Tongue Enlarged
Mobility of tongue decreased
Presence of yellowish nodules
Impression from the teeth also visible
Gingiva-
Infiltrated
Bluish color
Spongy
Hypertrophied

Salivary gland-
Xerostomia may result from
salivary gland involvement.
 Bone morphogenic protein
Bone morphogenetic proteins form a unique group
of proteins within the transforming growth factor
superfamily of genes and have a vital role in the
regulation in the bone induction and maintenance.

The activity of bone morphogenetic proteins was

first identified in the 1960s, but the proteins
responsible for bone induction were unknown until
the purification and cloning of human bone
morphogenetic proteins in the 1980s, because of
their osteoinductive potential.

Bonemorphogenetic proteins have gained a lot of

interest as therapeutic agents for treating
periodontal defects.
From the times of Hippocrates it has
been known that bone has considerable
potential for regeneration and repair.

Several decades ago Urist reported the

discovery that BMPs induce cartilage,
bone formation when implanted
intramuscularly in a rodent model.

Bone morphogenetic proteins play

essential role in regulation of bone
formation and repair.
BMPs are frequently referred to
as growth factors, they are now
regarded as differentiation
factors, because BMPs are
involved in morphogenesis and
organogenesis.
Periodontal tissue regeneration
entails the induction of periodontal
ligament, cementum, and alveolar
bone.

several studies have shown

significant regeneration of the
periodontal tissues with the use of
BMP.
References
Nutrition Science by B Srilakshmi
Nutrition and Child Care : A practical
guide by Shanti Ghosh
Textbook of Human Nutrition by
Mahtab S. Bamji, N Pralhad Rao and
Vinodini Reddy.
Textbook of Biochemistry by Prasad
R.M. 2nd edition.
Textbook of Biochemistry by
Satyanarayana.
Textbook of Medical Biochemistry
by S.S Randhawa.

Textbook of Oral Medicine by Anil

Ghoms.

UristMR. Bone: Formation by

autoinduction. Science
1965;150:8939.

Urist MR, Strates. Bone

Morphogenetic proteins. J Dent Res
Subramaniam M Rao. Bone
Morphogenetic Proteins:
Periodontal Regeneration, 2014,
November 21 IP: 117.208.128.69.

Jaebum L, Andreas S, Cristiano S,

Wikesjo ME. Periodontal
Regeneration: Focus on Growth
and Differentiation Factors. Dent
Clin N Am 2010;54:93111.
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