Chemistry

assignment
TOPIC :

BIOMOLECULES
“THERE 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 “

BY: Uvan Vijaya Balaji.V

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
ACKNOWLEDGEMENT

I WANT TO EXPRESS MY SINCERE THANKS

TO MY RESPECTED PRINCIPAL MADAM AND
CHEMISTRY TEACHER MRS SAPNA SINGH
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.

TYPES OF BIOMOLECULES
MICRO MOLECULES
BIOMOLECULES
MACROMOLECULES
M < 1000 MICROMOLECULE
AMONIO ACID
SUGARS
LIPIDS
NUCLEOTIDES
M>1000 MACROMOLECULE
POLYSACCARIDES
NUCLEIC ACID
PROTEINS

MICROMOLECULE
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 ne hydrolysed
further into smaller sugars
 Composed of 3-7 C atoms:
 Triose (3C)
 Tetrose (4C)
 Pentose (5C)
 Hexose (6C)
 Heptose (7C)

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
intercellularly; 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
MACROMOLECULE
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 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 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-equlibrium 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.
QUESTION 1 –
Why are biomolecules essential to life?
ANSWER-
Biomolecules are organic molecules especially
macromolecules like carbohydrates, proteins
in living organisms. All living forms bacteria, algae, plant
and animals are made of similar macromolecules that are
responsible for life. All the carbon compounds we get
from living tissues can be called biomolecules.

QUESTION 2-
What is the structure of a biomolecule?
ANSWER-
Biomolecular structure is the intricate folded, three-
dimensional shape that is formed by a molecule of
protein, DNA, or RNA, and that is important to its function.

QUESTION 3-
What is the function of a biomolecule?
ANSWER-
Proteins make up the majority of biomolecules present in
a cell. These molecules have enormous variation. Proteins
are responsible for many enzymatic functions in the cell
and play an important structural role . Proteins are
composed of subunits called amino acids .
QUESTIONS 4-
What is the purpose of biomolecules?
ANSWER
Proteins carry out specific functions inside cells, and they act
as enzymes to catalyze reactions all over the body. ...
Proteins are typically large molecules that can be built up
from chains of amino acids called polypeptides. Nucleic acids
are central to the function of living cells.

QUESTION 5-
What are the biomolecules made of?
ANSWER
Biomolecules are made of building-block monomers. A
monomer is a small molecule that can be combined
chemically with other monomers to form larger molecules.
Monomers are made up of relatively simple elements. The
most abundant elements in biological monomers
are carbon, hydrogen, and oxygen

QUESTION 6-
Why biological molecules are important?
ANSWER-
Most biological molecules have a core made of carbon
and hydrogen. Molecules differ in structure and function, in
part, because of different functional groups. The major
classes of biological molecules that are important for all
living things are carbohydrates, lipids, proteins, and nucleic
acids.
QUESTION 7-
Is water a biomolecule?
ANSWER-
A biomolecule is a chemical compound that naturally
occurs in living organisms. ... As clear from above, the
essential constituent of bio-molecules are carbon and
hydrogen, and water does not contain carbon ,hence, it can
not be considered as a bio-molecule.

QUESTION 8-
What type of biomolecule is an enzyme?
ANSWER-
Enzymes are usually proteins, and they act
as catalysts for reactions. The proteins vary from enzyme
to enzyme, depending on the location and function. They
are always in globular form, to allow for easy
accommodation for the substrate and active sites.
THANK YOU