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Delhi Public Secondary School

Robertsganj, Sonbhadra
INVESTIGATORY REPORT
Name- Adarsh Singh
Class- XII PCB
Topic- Biomolecules
Subject- Chemistry
Submitted To- Priti Ma’am

External’s Internal’s Principal’s


Sign Sign Sign
TOPIC :
BIOMOLECULES

“THER E ARE AS MANY ATOMS IN A


SINGLE AMOLECULE OF A DNA AS
THERE ARE STARS IN A TYPICAL
GALAXY.WE ARE, EACH OF US, A
LITTLE UNIVERSE “
CONTENTS
1. CERTIFICATE
2. ACKNOWLEDGEMENT
3. BIOMOLECULES
4. TYPES OF BIOMOLECULES
4.1 MICROMOLECULES
4.1.1. AMINO ACID
4.1.2. SUGAR
4.1.3. LIPID
4.1.4. NUCLEOTIDES
4.2. MACROMOLECULES
4.2.1. POLYSACCARIDES
4.2.2. NUCLEIC ACID
4.2.3. PROTEINS
5.MONOMERS
6.METABOLIC BASIS FOR LIVING
7.THE LIVING STATE
8.IMPORTANT QUESTION AND
CONCEPT OF BIOMOLECULES
CERTIFICATE
THIS IS TO CERTIFY Adarsh
Singh A STUDENT OF CLASS
XiI SCIENCE HAS
SUCCESFULLY COMPLETED
THE RESEARCH PROJECT ON
THE TOPIC BIOMOLECULES
UNDER THE GUIDANCE OF
MRS Priti Mishra DURING THE
ACADEMIC YEAR 2023-24.

external Internal principal


sign Sign Sign
ACKNOWLEDGEMENT

I WANT TO EXPRESS MY SINCERE THANKS


TO MY Respected CHEMISTRY TEACHER MRS
Priti Mishra FOR GIVING ME A CHANCE TO
RESEARCH ON THE TOPIC BIOMOLECULES
AND IT HAS BEEN MY PLEASURE DOING SO.
THIS HAS ADDED MANY POINTS TO MY
KNOWLEDGE ABOUT CHEMISTRY AND ITS
PRACTICAL APPLICATION. I ALSO THANK
THEM FOR THEIR SUPPORT AND VALUABLE
GUIDANCE WHICH HAS SEEEMED GREAT
CONTRIBUTION IN COMPLETION OF MY
RESEARCH WORK AS A PROJECT.
BIOMO
LECUL
A biomolecule or biological molecule is a loosely used
term for molecules or more commonly ions that are present
in organisms. Biomolecules including
large macromolecules (or polyanions) such
as proteins, carbohydrates, lipids, and nucleic acids, as well
as small molecules such as primary metabolites, secondary
metabolites, and natural products.

Biology and its subsets of biochemistry and molecular


biology study biomolecules and their reactions. Most
biomolecules are organic compounds, and just
four elements—oxygen, carbon, hydrogen, and nitrogen—
make up 96% of the human body's
mass. But many other elements, such as the various bio
metals, are present in small amounts.
TYPES OF BIOMOLECULES
MICRO MOLECULES
BIOMOLECULES
MACROMOLECULES
M < 1000 MICROMOLECULE
AMONIO ACID
SUGARS
LIPIDS
NUCLEOTIDES
M>1000 MACROMOLECULE
POLYSACCARIDES
NUCLEIC ACID
PROTEINS
MICROMOLECULE
AMONIO ACID

Amino acid contain both amino and carboxylic


acid functional groups. (In biochemistry, the term amino
acid is used when referring to those amino acids in which
the amino and carboxylate functionalities are attached to
the same carbon, plus proline which is not actually an
amino acid).
Modified amino acids are sometimes observed in proteins;
this is usually the result of enzymatic modification
after translation (protein synthesis). For example,
phosphorylation of serine by kinases and
dephosphorylation by phosphatases is an important control
mechanism in the cell cycle. Only two amino acids other
than the standard twenty are known to be incorporated into
proteins during translation, in certain organisms:
 Selenocysteine is incorporated into some proteins at a
UGA codon, which is normally a stop codon.
 Pyrrolysine is incorporated into some proteins at a

UAG codon. For instance, in some methanogens in


enzymes that are used to produce methane.
Besides those used in protein synthesis, other biologically
important amino acids include carnitine (used in lipid
transport within a cell), ornithine, GABA and taurine.

AROMATIC AMONIO ACID


SUGAR
MONOSHACCARIDES:
Simplest sugar, which cannot ne hydrolysed
further into smaller sugars
 Composed of 3-7 C atoms:
 Triose (3C)
 Tetrose (4C)
 Pentose (5C)
 Hexose (6C)
 Heptose (7C)

GLUCOSE:

GLACTOSE:
LIPID
For lipids present in biological membranes, the
Lipids (oleaginous) are chiefly fatty acid esters, and are the
basic building blocks of biological membranes. Another
biological role is energy storage (e.g., triglycerides). Most
lipids consist of a polar or hydrophilic head (typically
glycerol) and one to three nonpolar or hydrophobic fatty
acid tails, and therefore they are amphiphilic. Fatty acids
consist of unbranched chains of carbon atoms that are
connected by single bonds alone (saturated fatty acids) or
by both single and double bonds (unsaturated fatty acids).
The chains are usually 14-24 carbon groups long, but it is
always an even number.
hydrophilic head is from one of three classes:
 Glycolipids, whose heads contain

an oligosaccharide with 1-15 saccharide residues.


 Phospholipids, whose heads contain a positively

charged group that is linked to the tail by a negatively


charged phosphate group.
 Sterols, whose heads contain a planar steroid ring, for

example, cholesterol.
Other lipids
include prostaglandins and leukotrienes which are both 20-
carbon fatty acyl units synthesized from arachidonic acid.
They are also known as fatty acids
NUCLEOTIDES
Nucleotides are organic molecules that serve as
the monomer units for forming the nucleic
acid polymers deoxyribonucleic acid (DNA)
and ribonucleic acid (RNA), both of which are
essential biomolecules in all life-forms on Earth.
Nucleotides are the building blocks of nucleic acids; they
are composed of three subunit molecules: a nitrogenous
base a five-carbon sugar (ribose or deoxyribose), and at
least one phosphate group. They are also known
as phosphate nucleotides.
A nucleoside is a nitrogenous base and a 5-carbon sugar.
Thus, a nucleoside plus a phosphate group yields a
nucleotide.
Nucleotides also play a central role in life-form
metabolism at the fundamental, cellular level. They carry
packets of chemical energy—in the form of the nucleoside
triphosphates ATP, GTP, CTP and UTP—throughout the
cell to the many cellular functions that demand energy,
which include synthesizing amino acids, proteins and cell
membranes and parts; moving the cell and moving cell
parts, both internally and intercellularly; dividing the cell.
Purine + pyrimidine monomers

Higher nucleotides store energy in their higher energy P


bond
Nicotinamide + riboflavin coenzymes
Coenzymes: non protein organic moiety of holoenzymes

MACROMOLECULE
Polysaccharides
Polysaccharides are polymerized monosaccharides, or
complex carbohydrates. They have multiple simple sugars.
Examples are starch, cellulose, and glycogen. They are
generally large and often have a complex branched
connectivity. Because of their size, polysaccharides are not
water-soluble, but their many hydroxy groups become
hydrated individually when exposed to water, and some
polysaccharides form thick colloidal dispersions when
heated in water. Shorter polysaccharides, with 3 - 10
monomers, are called oligosaccharides. A fluorescent
indicator-displacement molecular imprinting sensor was
developed for discriminating saccharides. It successfully
discriminated three brands of orange juice beverage. The
change in fluorescence intensity of the sensing films
resulting is directly related to the saccharide concentration.

Nucleic acid
Nucleic acids are biopolymers, or large biomolecules,
essential to all known forms of life. They are composed
of monomers, which are nucleotides made of three
components: a 5-carbon sugar, a phosphate group and
a nitrogenous base. If the sugar is a simple ribose,
the polymer is RNA (ribonucleic acid); if the sugar is
derived from ribose as deoxyribose, the polymer
is DNA (deoxyribonucleic acid).
Nucleic acids are the most important of all biomolecules.
They are found in abundance in all living things, where
they function to create and encode and then store
information in the nucleus of every living cell of every life-
form organism on Earth. In turn, they function to transmit
and express that information inside and outside the cell
nucleus—to the interior operations of the cell and
ultimately to the next generation of each living organism.
The encoded information is contained and conveyed via
the nucleic acid sequence, which provides the 'ladder-step'
ordering of nucleotides within the molecules of RNA and
DNA.

DNA AND RNA STRUCTURE


DNA structure is dominated by the well-known double
helix formed by Watson-Crick base-pairing of C with G
and A with T. This is known as B-form DNA, and is
overwhelmingly the most favourable and common state of
DNA; its highly specific and stable base-pairing is the
basis of reliable genetic information storage. DNA can
sometimes occur as single strands (often needing to be
stabilized by single-strand binding proteins) or as A-
form or Z-form helices, and occasionally in more complex
3D structures such as the crossover at Holliday
junctions during DNA replication.

Stereo 3D image of a group I intron ribozyme gray lines


show base pairs; ribbon arrows show double-helix regions,
blue to red from 5' to 3' end; white ribbon is an RNA
product.
RNA, in contrast, forms large and complex 3D tertiary
structures reminiscent of proteins, as well as the loose
single strands with locally folded regions that
constitute messenger RNA molecules. Those RNA
structures contain many stretches of A-form double helix,
connected into definite 3D arrangements by single-
stranded loops, bulges, and junctions. Examples are RNA,
ribosomes, ribozymes, and riboswitches. These complex
structures are facilitated by the fact that RNA backbone
has less local flexibility than DNA but a large set of
distinct conformations, apparently because of both positive
and negative interactions of the extra OH on the
ribose. Structured RNA molecules can do highly specific
binding of other molecules and can themselves be
recognized specifically; in addition, they can perform
enzymatic catalysis (when they are known as "ribozymes",
as initially discovered by Tom Cech and colleagues.

PROTEINS
Proteins are large biomolecules, or macromolecules,
consisting of one or more long chains of amino
acid residues. Proteins perform a vast array of functions
within organisms, including catalysing metabolic
reactions, DNA replication, responding to stimuli,
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 three-dimensional
structure that determines its activity.

STRUCTURE OF PROTEIN
The particular series of amino acids that form a protein is
known as that protein's primary structure. This sequence is
determined by the genetic makeup of the individual. It
specifies the order of side-chain groups along the linear
polypeptide "backbone".
Proteins have two types of well-classified, frequently
occurring elements of local structure defined by a
particular pattern of hydrogen bonds along the
backbone: alpha helix and beta sheet. Their number and
arrangement is called the secondary structure of the
protein. Alpha helices are regular spirals stabilized by
hydrogen bonds between the backbone CO group
(carbonyl) of one amino acid residue and the backbone NH
group (amide) of the i+4 residue. The spiral has about 3.6
amino acids per turn, and the amino acid side chains stick
out from the cylinder of the helix. Beta pleated sheets are
formed by backbone hydrogen bonds between individual
beta strands each of which is in an "extended", or fully
stretched-out, conformation.

When two or more polypeptide chains (either of identical


or of different sequence) cluster to form a
protein, quaternary structure of protein is formed.
Quaternary structure is an attribute of polymeric (same-
sequence chains) or heteromeric (different-sequence
chains) proteins like hemoglobin, which consists of two
"alpha" and two "beta" polypeptide chains.

Apoenzymes
An apoenzyme (or, generally, an apoprotein) is the protein
without any small-molecule cofactors, substrates, or
inhibitors bound. It is often important as an inactive
storage, transport, or secretory form of a protein. This is
required, for instance, to protect the secretory cell from the
activity of that protein. Apoenzymes becomes active
enzymes on addition of a cofactor. Cofactors can be either
inorganic (e.g., metal ions and iron-sulfur clusters) or
organic compounds, (e.g., flavin and heme). Organic
cofactors can be either prosthetic groups, which are tightly
bound to an enzyme, or coenzymes, which are released
from the enzyme's active site during the reaction.

Isoenzymes
Isoenzymes, or isozymes, are multiple forms of an enzyme,
with slightly different protein sequence and closely similar
but usually not identical functions. They are either
products of different genes, or else different products
of alternative splicing. They may either be produced in
different organs or cell types to perform the same function,
or several isoenzymes may be produced in the same cell
type under differential regulation to suit the needs of
changing development or environment. The relative levels
of isoenzymes in blood can be used to diagnose problems
in the organ of secretion.

MONOMERS
A monomer is a molecule that, as a unit, binds chemically
or supramolecularly to other molecules to form
a supramolecular polymer. Large numbers of monomer
units combine to form polymers in a process
called polymerization. Molecules of a small number of
monomer units (up to a few dozen) are called oligomers.
The term "monomeric protein" may also be used to
describe one of the proteins making up a multiprotein
complex.
Biopolymer groupings, and the types of monomers that
create them.
 For lipids (Diglycerides, triglycerides), the monomers

are glycerol and fatty acids.


 For proteins (Polypeptides), the monomers are amino

acids.
 For Nucleic acids (DNA/RNA), the monomers

are nucleotides, each of which is made of a pentose


sugar, a nitrogenous base and a phosphate group.
 For carbohydrates (Polysaccharides specifically and

disaccharides—depends), the monomers


are monosaccharides.
METABOLIC BASIS FOR
LIVING
Metabolic pathways can lead to a more complex structure
from a simpler structure (for example, acetic acid becomes
cholesterol) or lead to a simpler structure from a complex
structure (for example, glucose becomes lactic acid in our
skeletal muscle). The former cases are called biosynthetic
pathways or anabolic pathways. The latter constitute
degradation and hence are called catabolic pathways.
Anabolic pathways, as expected, consume energy.
Assembly of a protein from amino acids requires energy
input. On the other hand, catabolic pathways lead to the
release of energy. For example, when glucose is degraded
to lactic acid in our skeletal muscle, energy is liberated.
This metabolic pathway from glucose to lactic acid which
occurs in 10 metabolic steps is called glycolysis. Living
organisms have learnt to trap this energy liberated during
degradation and store it in the form of chemical bonds. As
and when needed, this bond energy is utilized for
biosynthetic, osmotic and mechanical work that we
perform. The most important form of energy currency in
living systems is the bond energy in a chemical
called adenosine triphosphate (ATP).

THE LIVING STATE


 Thousands of chemical compounds in a living
organism, otherwise called metabolites or
biomolecules are present at concentration
characteristics of each of them. For example, the blood
concentration of glucose in a normal healthy
individual is 4.5-5.0 mm while that hormone would be
nanograms/ml.
 The most important fact of biological system is that all
living organism exist in a steady-stale characterised by
concentration of each of these molecule
 These biomolecules are in metabolic flux
 Any chemical or physical process move
simultaneously to equilibrium. The steady state is non-
equilibrium state. one should remember from the
physics that system at equilibrium cannot perform
work. As living organisms work continuously, they
cannot afford to each equilibrium. Hence the living
state is the non-equilibrium sready state to be able to
perform work; living process is a constant effort to
prevent falling into equilibrium. This is achieved by
energy input.
 Metabolism provide a mechanism for the production
of the energy. Hence the living state and metabolism
are synonymous. Without metabolism there cannot be
living state.
Bibliography
The Websites that helped me to
complete this Project: -

⦁ www.youtube.com
⦁ www.wikipedia.com
⦁ www.embibe.com

The Books that helped me to


complete this Project: -

⦁ NCERT Textbook of Chemistry part


II (Class XII)
⦁ Modern ABC+ of Chemistry (Class XII)

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