1.

BIOMOLECULES
2. TYPES OF BIOMOLECULES
2.1 MICROMOLECULES
2.1.1. AMINO ACID
2.1.2. SUGAR
2.1.3. LIPID
2.1.4. NUCLEOTIDES
2.2. MACROMOLECULES
2.2.1. POLYSACCARIDES
2.2.2. NUCLEIC ACID
2.2.3. PROTEINS
3.MONOMERS
4.METABOLIC BASIS FOR
LIVING
5.THE LIVING STATE
 THIS IS TO CERTIFY THAT SANJAY SONI, A
STUDENT OF CLASS XII SCIENCE HAS
SUCCESFULLY COMPLETED THE RESEARCH
PROJECT ON THE TOPIC “BIOMOLECULES”
UNDER THE GUIDANCE OF MR. R.K
MALVIYA DURING THE ACADEMIC YEAR
2021-2022

_________ ___________ __________

TEACHER EXTERNAL
PRINCIPAL INCHARGE
INCHARGE
I WANT TO EXPRESS MY SINCERE THANKS
TO MY RESPECTED PRINCIPAL
MR.RAKESH TIWARI AND CHEMISTRY
TEACHER MR. R.K MALVIYA 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.
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 biometals,
are present in small amounts.
 MICRO MOLECULES
BIOMOLECULES
MACROMOLECULES

M < 1000 MICROMOLECULE

AMONIO ACID
SUGARS
LIPIDS
NUCLEOTIDES

M>1000 MACROMOLECULE

POLYSACCARIDES
NUCLEIC ACID
PROTEINS
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

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

GLUCOSE: GLACTOSE:

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 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
phosphatenucleotides.
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
intercellulary; dividing the cell.

Purine + pyridimine monomers

Higher nucleotides store energy in their higher energy

P bond
Nicotinamide + riboplavin coenzymes

Coenzymes: non protein organic moiety of

holoenzymes
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 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 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 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 chain) 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.
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 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).
Thousand of chemical compound in a living organism, otherwise
called metabolities or biomolecules are present at concentration
characterstics 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-
equlibrium 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 mechanismfor the production of the

energy. Hence the living state and metabolism are synonomus.
Without metabolism there cannot be living state.