CERTIFICATE
This certify that Devendra Yadav student of
class 12th B has successfully completed the
research on below mentioned project under
the guidance of Mrs. Divya Jyoti Naghotra
during the year 2016-17 in partial fulfillment
of chemistry practical examination conducted
by AISSCE New Delhi.
Neelam Malviya
[Pricipal]
Sign of
Sub-Teacher
ACKNOWLEDGEMEN
I would like to express my sincere gratitude to
T
my biology teacher Mrs. Divya Jyoti
Naghotra for her vital support guidance and
encouragement without which this project
would not have come forth.
I would also express my gratitude to my
parents and classmates who helped me to
carry out this project work successful and for
their advices and support.
Protiens
1.1-What are protiens?
Proteins large biomolecules, or macromolecules, consisting of
one or more long chains of amino acidresidues. Proteins
perform
vast
array
of
including catalysing
functions
within organisms,
metabolic
replication, responding
to
stimuli,
reactions, DNA
and transporting
molecules from one location to another. Proteins differ from
one another primarily in their sequence of amino acids, which
is dictated by the nucleotide sequence of their genes, and
which usually results in protein folding into a specific threedimensional structure that determines its activity.
A linear chain of amino acid residues is called a polypeptide. A
protein
contains
at
least
one
long
polypeptide.
Short
polypeptides, containing less than 2030 residues, are rarely
considered to be proteins and are commonly called peptides,
or
sometimes oligopeptides.
The
individual
amino
acid
residues are bonded together by peptide bonds and adjacent
amino acid residues. The sequence of amino acid residues in a
protein is defined by the sequence of a gene, which is encoded
in the genetic code. In general, the genetic code specifies 20
standard amino acids; however, in certain organisms the
genetic
code
can
include selenocysteine andin
certain archaeapyrrolysine. Shortly after or even during
synthesis, the residues in a protein are often chemically
modified by post-translational modification, which alters the
physical and chemical properties, folding, stability, activity,
and ultimately, the function of the proteins. Sometimes
proteins have non-peptide groups attached, which can be
called prosthetic groups or cofactors. Proteins can also work
together to achieve a particular function, and they often
associate to form stable protein complexes.
Once formed, proteins only exist for a certain period of time
and are then degraded and recycled by the cell's machinery
through the process of protein turnover. A protein's lifespan is
measured in terms of its half-life and covers a wide range.
They can exist for minutes or years with an average lifespan of
12 days in mammalian cells. Abnormal and or misfolded
proteins are degraded more rapidly either due to being
targeted for destruction or due to being unstable.
Like
other
biological
macromolecules
such
as polysaccharides and nucleic acids, proteins are essential
parts of organisms and participate in virtually every process
within cells.
Many
proteins
are enzymes that catalyse biochemical reactions and are vital
to metabolism. Proteins also have structural or mechanical
functions, such as actin and myosin in muscle and the proteins
in the cytoskeleton, which form a system of scaffolding that
maintains cell shape. Other proteins are important in cell
signaling, immune responses, cell adhesion, and the cell cycle.
In
animals,
proteins
the essential
are
needed
amino
in
the diet to
acids that
provide
cannot
be synthesized. Digestion breaks the proteins down for use in
the metabolism.
Proteins may be purified from other cellular components using
a
variety
of
techniques
such
as ultracentrifugation, precipitation, electrophoresis,
and chromatography; the advent of genetic engineering has
made possible a number of methods to facilitate purification.
Methods commonly used to study protein structure and
function
include immunohistochemistry, site-directed
mutagenesis, X-ray
crystallography, nuclear
magnetic
resonance and mass spectrometry.
1.2 -What are amino amino acids?
Amino
acids are biologically important organic
compounds containing amine (-NH2)
and carboxyl (-
COOH) functional groups, along with a side-chain (R group)
specific to each amino acid.[ The key elements of an amino
acid are carbon, hydrogen, oxygen, and nitrogen, though other
elements are found in the side-chains of certain amino acids.
About 500 amino acids are known (though only 20 appear in
the genetic code) and can be classified in many ways. They
can be classified according to the core structural functional
groups' locations as alpha- (-), beta- (-), gamma- (-) or
delta- (-) amino
acids;
other
categories
relate
to polarity, pH level,
and
(aliphatic, acyclic, aromatic,
side-chain
containing
group
hydroxyl
type
or sulfur,
etc.). In the form of proteins, amino acids comprise the
second-largest
component
human muscles, cells and
amino
acids
perform
(water
is
the
other tissues.
critical
roles
largest)
Outside
in
of
proteins,
processes
such
as neurotransmitter transport and biosynthesis.
1.3 STRUCTURE OF pROTIENS
Most proteins fold into unique 3-dimensional structures. The
shape into which a protein naturally folds is known as
its native conformation. Although many proteins can fold
unassisted, simply through the chemical properties of their
amino acids, others require the aid of molecular chaperones to
fold into their native states. Biochemists often refer to four
distinct aspects of a protein's structure:
Primary structure :- The amino acid sequence. A
protein is a polyamide.
Secondary structure :- Regularly repeating local
structures stabilized by hydrogen bonds. The most common
examples are the -helix, -sheet and turns. Because
secondary structures are local, many regions of different
secondary structure can be present in the same protein
molecule.
Tertiary structure :- The overall shape of a single
protein molecule; the spatial relationship of the secondary
structures to one another. Tertiary structure is generally
stabilized by nonlocal interactions, most commonly the
formation of a hydrophobic core, but also through salt
bridges, hydrogen bonds, disulfide bonds, and
even posttranslational modifications. The term "tertiary
structure" is often used as synonymous with the term fold.
The tertiary structure is what controls the basic function of
the protein.
Quaternary structure:- the structure formed by several
protein molecules (polypeptide chains), usually
called protein subunits in this context, which function as a
single protein complex.
Proteins are not entirely rigid molecules. In addition to these
levels of structure, proteins may shift between several related
structures while they perform their functions. In the context of
these functional rearrangements, these tertiary or quaternary
structures are usually referred to as "conformations", and
transitions between them are called conformational
changes. Such changes are often induced by the binding of
a substrate molecule to an enzyme's active site, or the
physical region of the protein that participates in chemical
catalysis. In solution proteins also undergo variation in
structure through thermal vibration and the collision with other
molecules.
Proteins can be informally divided into three main classes,
which correlate with typical tertiary structures: globular
proteins, fibrous proteins, and membrane proteins. Almost all
globular proteins are soluble and many are enzymes. Fibrous
proteins are often structural, such as collagen, the major
component of connective tissue, or keratin, the protein
component of hair and nails. Membrane proteins often serve
as receptors or provide channels for polar or charged
molecules to pass through the cell membrane.
A special case of intramolecular hydrogen bonds within
proteins, poorly shielded from water attack and hence
promoting their own dehydration, are called dehydrons.
1.4 Types of amino acids
Amino acids are organic compounds which contain at least one
amino group (-NH2) and a carboxy (-COOH) group. In the
human genome, 20 amino acids are created to build proteins
and therefore termed proteinogen. Besides this, there are
approximately 250 amino acids which do not form proteins.
These are used to form sugar for example.
The 20 proteinogen amino acids are also called standard
amino acids, which can be divided into three groups: essential,
semi-essential and non-essential.
Eight amino acids are essential for humans, as the body
cannot produce them by themselves, and they have to be
supplied externally. These are: isoleucine, leucine,
lysine, methionine, phenylalanine, threonine,
tryptophan and valine.
Arginine and histidine form the group of so-called semiessential amino acids. They have to be consumed in the diet
under certain circumstances.
The ten non-essential amino acids are able to be produced in
the body. The following amino acids fall into this category:
alanine, asparagine, aspartic acid, cysteine, glutamine,
glutamic acid, glycine, proline, serin and tyrosine.
It should be noted that the grouping essential and nonessential does not mean that one group more important is
that the other. This is because the division of the two does not
assess whether the body has sufficient supply of the amino
acids in question at its disposal. The protein requirement can
differ greatly from person to person. The amount of semiessential and non-essential amino acids produced by the body
itself depends on many different factors, such as age, mental
and/or physical stress or distress situations. These determine
the various amino acid levels required to stay fit and healthy.
1.5 Diseases caused by deficiency of
proteins
Marasmus
Marasmus is a disease caused by a severe deficiency of
protein and calories that affect infants and very young
children, often resulting in weight loss and dehydration.
Marasmus can develop into starvation and cause fatality
caused by a lack of essential nutrients. People with marasmus
appear bony with little muscle tissue, according to
Food4Africa.
Kwashiorkor
Kwashiorkor is a disease caused by a severe deficiency of
protein in diets that contain calories mostly from
carbohydrates such as yams, rice and bananas. It usually
affects older children. People with kwashiorkor appear puffy in
the abdomen area from retention of fluid, according to the
University of Maryland Medical Center. Common symptoms of
both marasmus and kwashiorkor include fatigue, irritability,
diarrhea, stunted growth and impairment of cognition and
mental health.
Deficiencies of Protein C and Protein S
Deficiencies of protein C and protein S are inherited conditions
that cause abnormal blood clotting, according to Medline Plus.
Deficiency of protein C occurs in about 1 out of 300 people.
Deficiency of protein S affects 1 in 20,000 people. Symptoms
for these deficiencies include redness, pain, tenderness or
swelling in the affected area. People with these protein
deficiencies need to be careful about activities that increase
risk of blood clots, such as prolonged sitting, bed rest, and
long-time travel in cars and airplanes. Research by A. Hooda
published in the "Annals of Indian Academy of Neurology" in
2009 discovered that protein S deficiency causes ischemic
stroke.
Cachexia
Cachexia is a condition that involves protein deficiency,
depletion of skeletal muscle and an increased rate of protein
degradation, according to research by D.P. Kotler published in
the "Annals of Internal Medicine" in 2000. Cachexia causes
weight loss and mortality and is associated with cancer, AIDS,
chronic kidney failure, heat disease, chronic obstructive
pulmonary disease and rheumatoid arthritis, according to J.E.
Morley in the "American Journal of Clinical Nutrition." Patients
with malignant cancer of the stomach, colon, liver, billiary
tract and pancreas experience undernutrition from reduced
intake of protein, calories and micronutrients, and have fatigue
and a negative nitrogen balance as a result of loss of muscle
mass from cachexia, according to J. Ockenga in "Alimentary
Pharmacology and Therapeutics" in 2005.
