Unit -2

Biomolecules

biomolecule, also called biological molecule, any of numerous substances that are produced by
cells and living organisms. Biomolecules have a wide range of sizes and structures and perform a
vast array of functions. The four major types of biomolecules are carbohydrates, lipids, nucleic
acids, and proteins.

Among biomolecules, nucleic acids, namely DNA and RNA, have the unique function of
storing an organism’s genetic code—the sequence of nucleotides that determines the amino
acid sequence of proteins, which are of critical importance to life on Earth. There are 20 different
amino acids that can occur within a protein; the order in which they occur plays a fundamental
role in determining protein structure and function. Proteins themselves are major structural
elements of cells. They also serve as transporters, moving nutrients and other molecules in and
out of cells, and as enzymes and catalysts for the vast majority of chemical reactions that take
place in living organisms. Proteins also form antibodies and hormones, and they
influence gene activity.

Likewise, carbohydrates, which are made up primarily of molecules containing atoms

of carbon, hydrogen, and oxygen, are essential energy sources and structural components of all
life, and they are among the most abundant biomolecules on Earth. They are built from four
types of sugar units—monosaccharides, disaccharides, oligosaccharides, and polysaccharides.
Lipids, another key biomolecule of living organisms, fulfill a variety of roles, including serving
as a source of stored energy and acting as chemical messengers. They also form membranes,
which separate cells from their environments and compartmentalize the cell interior, giving rise
to organelles, such as the nucleus and the mitochondrion, in higher (more complex) organisms.

A diverse range of biomolecules exist, including:

 Small molecules:

o Lipids, fatty acids, glycolipids, sterols, monosaccharides

o Vitamins

o Hormones, neurotransmitters

o Metabolites

 Monomers, oligomers and polymers

Nucleosides and nucleotides

Nucleosides are molecules formed by attaching a nucleobase to a ribose or deoxyribose ring.

Examples of these include cytidine (C), uridine (U), adenosine (A), guanosine (G), and
thymidine (T). Nucleosides can be phosphorylated by specific kinases in the cell, producing
nucleotides. Both DNA and RNA are polymers, consisting of long, linear molecules assembled
by polymerase enzymes from repeating structural units, or monomers, of mononucleotides. DNA
uses the deoxynucleotides C, G, A, and T, while RNA uses the ribonucleotides (which have an
extra hydroxyl(OH) group on the pentose ring) C, G, A, and U. Modified bases are fairly
common (such as with methyl groups on the base ring), as found in ribosomal RNA or transfer
RNAs or for discriminating the new from old strands of DNA after replication.[6]

Each nucleotide is made of an acyclic nitrogenous base, a pentose and one to three phosphate
groups. They contain carbon, nitrogen, oxygen, hydrogen and phosphorus. They serve as sources
of chemical energy (adenosine triphosphate and guanosine triphosphate), participate in cellular
signaling (cyclic guanosine monophosphate and cyclic adenosine monophosphate), and are
incorporated into important cofactors of enzymatic reactions (coenzyme A, flavin adenine
dinucleotide, flavin mononucleotide, and nicotinamide adenine dinucleotide phosphate).

Monomeric unit and polymeric structure

Lipids, Polysaccharides, Proteins and Polynucleotides are the major groups

of macromolecules that are found in all living organisms. These giant molecules carry out all the
vital functions needed by cells. Macromolecules are involved in processes such as food
digestion, information storage, energy manipulation and metabolism. They are complex, huge
associations of molecular subunits that appear impossibly difficult to understand. Fortunately
they are all built using the same construction principle.

Monomers & Polymers Monomers are small molecules, mostly organic, that can join
with other similar molecules to form very large molecules, or
polymers. All monomers have the capacity to form chemical
bonds to at least two other monomer molecules.

monomers
Polymers are a class of
synthetic substances
composed of multiples of
simpler units called
monomers. Polymers are
chains with an
unspecified number of
monomeric units.

Homopolymers are polymers made by joining together monomers of the same chemical
composition or structure.

Heteropolymers are
polymers composed of
more than one kind of
monomer

Carbohydrate

is a biomolecule consisting of carbon (C), hydrogen (H) and oxygen (O) atoms, usually with a
hydrogen–oxygen atom ratio of 2:1 (as in water) and thus with the empirical
formula Cm(H2O)n (where m may or may not be different from n). However, not all
carbohydrates conform to this precise stoichiometric definition (e.g., uronic acids, deoxy-sugars
such as fucose), nor are all chemicals that do conform to this definition automatically classified
as carbohydrates (e.g. formaldehyde and acetic acid).

The term is most common in biochemistry, where it is a synonym of saccharide, a group that
includes sugars, starch, and cellulose. The saccharides are divided into four chemical
groups: monosaccharides, disaccharides, oligosaccharides, and polysaccharides.
Monosaccharides and disaccharides, the smallest (lower molecular weight) carbohydrates, are
commonly referred to as sugars. Carbohydrates perform numerous roles in living organisms.
Polysaccharides serve for the storage of energy (e.g. starch and glycogen) and as structural
components (e.g. cellulose in plants and chitin in arthropods). The 5-carbon
monosaccharide ribose is an important component of coenzymes (e.g. ATP, FAD and NAD) and
the backbone of the genetic molecule known as RNA. The related deoxyribose is a component of
DNA. Saccharides and their derivatives include many other important biomolecules that play key
roles in the immune system, fertilization, preventing pathogenesis, blood clotting,
and development. Cellulose, a polysaccharide found in the cell walls of all plants, is one of the
main components of insoluble dietary fiber. Although it is not digestible in humans (ruminates
generally, and some insects -- notably termites, have more complex digestions and can digest
cellulose), cellulose and insoluble dietary fiber generally help maintain a healthy digestive
system[4] by facilitating movement through the large colon (ie, defecation). Other
polysaccharides contained in dietary fiber include resistant starch and inulin, which feed some
bacteria in the microbiota of the large intestine, and are metabolized by these bacteria to
yield short-chain fatty acids

Structure

Natural saccharides are generally built of simple carbohydrates called monosaccharides with
general formula (CH2O)n where n is three or more. A typical monosaccharide has the structure
H–(CHOH)x(C=O)–(CHOH)y–H, that is, an aldehyde or ketone with many hydroxyl groups
added, usually one on each carbon atom that is not part of the aldehyde or ketone functional
group. Examples of monosaccharides are glucose, fructose, and glyceraldehydes. However, some
biological substances commonly called "monosaccharides" do not conform to this formula
(e.g. uronic acids and deoxy-sugars such as fucose) and there are many chemicals that do
conform to this formula but are not considered to be monosaccharides (e.g. formaldehyde CH 2O
and inositol (CH2O)6)

The major dietary carbohydrates

class
Subgroup Components
(degree of polymerization)

Monosaccharides Glucose, galactose, fructose, xylose

Sugars (1–2) Disaccharides Sucrose, lactose, maltose, isomaltulose, trehalose

Polyols Sorbitol, mannitol

Malto-
Maltodextrins
oligosaccharides
Oligosaccharides (3–9)
Other
Raffinose, stachyose, fructo-oligosaccharides
oligosaccharides

Starch Amylose, amylopectin, modified starches

Polysaccharides (>9)
Non-starch Glycogen, Cellulose, Hemicellulose, Pectins, Hyd
polysaccharides rocolloids

Monosaccharides

Monosaccharides are the simplest carbohydrates in that they cannot be hydrolyzed to smaller
carbohydrates. They are aldehydes or ketones with two or more hydroxyl groups. The
general chemical formula of an unmodified monosaccharide is (C•H2O)n, literally a "carbon
hydrate". Monosaccharides are important fuel molecules as well as building blocks for nucleic
acids. The smallest monosaccharides, for which n=3, are dihydroxyacetone and D- and L-
glyceraldehydes.
Disaccharides

Two joined monosaccharides are called a disaccharide and these are the simplest
polysaccharides. Examples include sucrose and lactose. They are composed of two
monosaccharide units bound together by a covalent bond known as a glycosidic linkage formed
via a dehydration reaction, resulting in the loss of a hydrogen atom from one monosaccharide
and a hydroxyl group from the other. The formula of unmodified disaccharides is C12H22O11.
Although there are numerous kinds of disaccharides, a handful of disaccharides are particularly
notable.

Sucrose, pictured to the right, is the most abundant disaccharide, and the main form in which
carbohydrates are transported in plants. It is composed of one D-glucose molecule and one D-
fructose molecule. The systematic name for sucrose, O-α-D-glucopyranosyl-(1→2)-D-
fructofuranoside, indicates four things:

 Its monosaccharides: glucose and fructose

 Their ring types: glucose is a pyranose and fructose is a furanose

 How they are linked together: the oxygen on carbon number 1 (C1) of α-D-glucose is
linked to the C2 of D-fructose.

 The -oside suffix indicates that the anomeric carbon of both monosaccharides participates
in the glycosidic bond.

Lactose, a disaccharide composed of one D-galactose molecule and one D-glucose molecule,
occurs naturally in mammalian milk. The systematic name for lactose is O-β-D-
galactopyranosyl-(1→4)-D-glucopyranose. Other notable disaccharides include maltose (two D-
glucoses linked α-1,4) and cellobiose (two D-glucoses linked β-1,4). Disaccharides can be
classified into two types: reducing and non-reducing disaccharides. If the functional group is
present in bonding with another sugar unit, it is called a reducing disaccharide or biose.
Starch

Starch or amylum is a polymeric carbohydrate consisting of numerous glucose units joined

by glycosidic bonds. This polysaccharide is produced by most green plants for energy storage.
Worldwide, it is the most common carbohydrate in human diets, and is contained in large
amounts in staple foods like wheat, potatoes, maize (corn), rice, and cassava (manioc).

Pure starch is a white, tasteless and odorless powder that is insoluble in cold water or alcohol. It
consists of two types of molecules: the linear and helical amylose and the branched amylopectin.
Depending on the plant, starch generally contains 20 to 25% amylose and 75 to 80% amylopectin
by weight. Glycogen, the glucose store of animals, is a more highly branched version of
amylopectin. While amylose was thought to be completely unbranched, it is now known that some of its
molecules contain a few branch points. [35] Amylose is a much smaller molecule than amylopectin. About
one quarter of the mass of starch granules in plants consist of amylose, although there are about 150 times
more amylose than amylopectin molecules.

Starch molecules arrange themselves in the plant in semi-crystalline granules. Each plant species
has a unique starch granular size: rice starch is relatively small (about 2 μm) while potato
starches have larger granules (up to 100 μm).

Some cultivated plant varieties have pure amylopectin starch without amylose, known as waxy
starches. The most used is waxy maize, others are glutinous rice and waxy potato starch. Waxy
starches have less retrogradation, resulting in a more stable paste. High amylose
starch, amylomaize, is cultivated for the use of its gel strength and for use as a resistant starch (a
starch that resists digestion) in food products.

Synthetic amylose made from cellulose has a well-controlled degree of polymerization.

Therefore, it can be used as a potential drug deliver carrier.
 Starch structure

Cellulose

Cellulose is an organic compound with the formula (C6H10O5)n a polysaccharide consisting of a

linear chain of several hundred to many thousands of β(1→4) linked D-glucose units. Cellulose
is an important structural component of the primary cell wall of green plants, many forms
of algae and the oomycetes. Some species of bacteria secrete it to form biofilms. Cellulose is the
most abundant organic polymer on Earth. The cellulose content of cotton fiber is 90%, that
of wood is 40–50%, and that of dried hemp is approximately 57%. Cellulose is mainly used to
produce paperboard and paper. Smaller quantities are converted into a wide variety of derivative
products such as cellophane and rayon.
Amino acid

Amino acids are organic compounds that contain amino and carboxylate functional groups, along
with a side chain (R group) specific to each amino acid The elements present in every amino acid
are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N); in addition sulfur (S) is present in
the side chains of cysteine and methionine, and selenium (Se) in the less common amino
acid selenocysteine. More than 500 naturally occurring amino acids are known to constitute
monomer units of peptides, including proteins, as of 2020(though only 20 appear in the genetic
code, plus selenocysteine, which is encoded in a special way).

Proteins

Proteins are large, complex molecules that play many critical roles in the body. They do most of
the work in cells and are required for the structure, function, and regulation of the body’s tissues
and organs.

Proteins are made up of hundreds or thousands of smaller units called amino acids, which are
attached to one another in long chains. There are 20 different types of amino acids that can be
combined to make a protein. The sequence of amino acids determines each protein’s unique 3-
dimensional structure and its specific function. Amino acids are coded by combinations of three
DNA building blocks (nucleotides), determined by the sequence of genes.

Proteins can be described according to their large range of functions in the body, listed in
alphabetical order:

Examples of protein functions

Function Description Example

Antibody Antibodies bind to specific foreign particles, such as viruses and Immunoglobulin G
bacteria, to help protect the body. (IgG)

Enzyme Enzymes carry out almost all of the thousands of chemical Phenylalanine
reactions that take place in cells. They also assist with the hydroxylase
formation of new molecules by reading the genetic information
stored in DNA.

Messenger Messenger proteins, such as some types of hormones, transmit Growth hormone
signals to coordinate biological processes between different cells,
tissues, and organs.

Structural These proteins provide structure and support for cells. On a larger Actin
component scale, they also allow the body to move.

Transport/storage These proteins bind and carry atoms and small molecules within Ferritin
cells and throughout the body.

Nucleotides

Nucleotides are organic molecules consisting of a nucleoside and a phosphate. They serve
as monomeric units of the nucleic acid polymers – deoxyribonucleic acid (DNA) and ribonucleic
acid (RNA), both of which are essential biomolecules within all life-forms on Earth. Nucleotides
are obtained in the diet and are also synthesized from common nutrients by the liver.
Nucleotides are composed of three subunit molecules: a nucleobase, a five-carbon
sugar (ribose or deoxyribose), and a phosphate group consisting of one to three phosphates. The
four nucleobases in DNA are guanine, adenine, cytosine and thymine; in RNA, uracil is used in
place of thymine.

Nucleotides also play a central role in metabolism at a fundamental, cellular level. They provide
chemical energy—in the form of the nucleoside triphosphates, adenosine
triphosphate (ATP), guanosine triphosphate (GTP), cytidine triphosphate (CTP) and uridine
triphosphate (UTP)—throughout the cell for the many cellular functions that demand energy,
including: amino acid, protein and cell membrane synthesis, moving the cell and cell parts (both
internally and intercellularly), cell division, etc.[2] In addition, nucleotides participate in cell
signaling (cyclic guanosine monophosphate or cGMP and cyclic adenosine monophosphate or
cAMP), and are incorporated into important cofactors of enzymatic reactions (e.g. coenzyme
A, FAD, FMN, NAD, and NADP+).

A nucleotide is regarded as the basic building block of nucleic acid (e.g. DNA and RNA). A
nucleic acid, in turn, is one of the major groups of biomolecules (the others are carbohydrates,
proteins, and amino acids). Nucleic acids are involved in the preservation, replication, and
expression of hereditary information. Nucleotides also provide chemical energy in the form of
their nucleoside triphosphates. Additionally, they participate in cell signaling and form a second
messenger in cellular processes. A nucleotide is an organic compound made up of three subunits:
a nitrogenous base, a five-carbon sugar, and a phosphate group. The sugar component may either
be ribose or deoxyribose. Ribose is the sugar component of the nucleotides that make up RNA.
The deoxyribose sugar is the sugar component of DNA. Each phosphate group connects the
sugar rings of two adjacent nucleotide monomers. The phosphate groups and the sugar moieties
form the backbone of nucleic acid. In DNA, the orientation of the two strands is in opposite
directions. This is to allow complementary base pairing between nucleobase constituents. Apart
from the long chain of nucleic acids, nucleotides also occur in cyclic forms. Cyclic nucleotides
form when the phosphate group is linked twice to the sugar moiety, particularly to the two
hydroxyl groups of the constituent sugar.

Apart from the role of nucleotides as subunits of nucleic acids, they are also energy carriers.
They carry chemical energy that the cell uses to fuel various cell activities. Adenosine
triphosphate (ATP) is by far the most widely used.

The fundamental nucleotides are divided into purines and pyrimidines based on the structure of
the nitrogenous base. The purine bases include adenine and guanine while the pyrimidine bases
are thymine and cytosine, and uracil. In RNA uracil replaces thymine (thymine is produced by
adding methyl to uracil). (Ref. 2)
The nucleobases that make up the nucleic acid are used to distinguish DNA from RNA
molecules. In DNA, thymine complementary pairs with adenine whereas in RNA, uracil matches
with adenine. The pairings of nucleobases C-G and A-T (or A-U in RNA) are referred to as base
complements.

Biological Functions of Nucleotides

Aside from serving as precursors of nucleic acids, nucleotides also serve as

important cofactors in cellular signaling and metabolism. The nucleoside triphosphates, in
particular, carry packets of chemical energy that are used in many cellular activities demanding
energy, e.g. amino acid synthesis, protein synthesis, cell division, internal and intercellular
movements, etc.

DNA

DNA, abbreviation of deoxyribonucleic acid, organic chemical of complex molecular structure

that is found in all prokaryotic and eukaryotic cells and in many viruses. DNA codes genetic
information for the transmission of inherited traits. The chemical DNA was first discovered in
1869, but its role in genetic inheritance was not demonstrated until 1943. In 1953 James
Watson and Francis Crick, aided by the work of biophysicists Rosalind Franklin and Maurice
Wilkins, determined that the structure of DNA is a double-helix polymer, a spiral consisting of
two DNA strands wound around each other. The breakthrough led to significant advances in
scientists’ understanding of DNA replication and hereditary control of cellular activities.

 DNA stands for Deoxyribonucleic Acid which is a molecule that contains the instructions
an organism needs to develop, live and reproduce.

 These instructions are found inside every cell and are passed down from parents to their
children.

 It is a nucleic acid and is one of the four major types of macromolecules that are known
to be essential for all forms of life.

 DNA is found in the nucleus, with a small amount of DNA also present in mitochondria
in the eukaryotes.

 In 1953, James Watson and Francis Crick discovered the structure of DNA.
 The works of Rosalind Franklin lead to Watson and Crick’s discovery. Franklin
first had pointed out that the DNA is made up of two spirals.
 The structure of DNA is a double helix structure because it looks like a twisted
ladder.
  The sides of the ladder are made of alternating sugar (deoxyribose) and phosphate
molecules while the steps of the ladder are made up of a pair of nitrogen bases.
 There are 4 types of nitrogen bases Adenine (A) Thymine (T) Guanine (G)
Cytosine (C) DNA Pairing. The nitrogen bases have a specific pairing pattern.
 This pairing pattern occurs because the amount of adenine equals the amount of
thymine; the amount of guanine equals the amount of cytosine. The pairs are held
together by hydrogen bonds.
 DNA is a double-stranded helix. That is each DNA molecule is comprised of two
biopolymer strands coiling around each other to form a double helix structure.
These two DNA strands are called polynucleotides, as they are made of simpler
monomer units called nucleotides.
 Each strand has a 5′end (with a phosphate group) and a 3′end (with a hydroxyl
group).
 The strands are antiparallel, meaning that one strand runs in a 5′to 3′direction,
while the other strand runs in a 3′ to 5′ direction.
 The two strands are held together by hydrogen bonds and are complimentary to
each other.
 Basically, the DNA is composed of deoxyribonucleotides.
 The deoxyribonucleotides are linked together by 3′ – 5′phosphodiester bonds.
 The nitrogenous bases that compose the deoxyribonucleotides include adenine,
cytosine, thymine, and guanine.
 The complimentary of the strands are due to the nature of the nitrogenous bases.
The base adenine always interacts with a thymine (A-T) on the opposite strand via
two hydrogen bonds and cytosine always interacts with guanine (C-G) via three
hydrogen bonds on the opposite strand.
 The shape of the helix is stabilized by hydrogen bonding and hydrophobic
interactions between bases.
 The diameter of double helix is 2nm and the double helical structure repeats at an
interval of 3.4nm which corresponds to ten base pairs.
Properties of DNA

 DNA helices can be right handed or left handed. But the B – conformation of
DNA having the right handed helices is the most stable.

 On heating the two strands of DNA separate from each other and on cooling these again
hybridize.

 The temperature at which the two strands separate completely is known as melting
temperature (Tm). Melting temperature is specific for each specific sequence.

 The B sample of DNA having higher melting point must have more C-G content because
C-G pair has 3 hydrogen bonds.
 The sequence of bases along the DNA molecule encodes for the sequence of amino acids
in every protein in all organisms.

Types of DNA

Eukaryotic organisms such as animals, plants and fungi, store the majority of their DNA
inside the cell nucleus and some of their DNA in organelles such as mitochondria.

Based on the location DNA may be:

Nuclear DNA

 Located within the nucleus of eukaryote cells.

 Usually has two copies per cell.

 The structure of nuclear DNA chromosomes is linear with open ends and includes
46 chromosomes containing 3 billion nucleotides.

 Nuclear DNA is diploid, ordinarily inheriting the DNA from two parents. The mutation
rate for nuclear DNA is less than 0.3%.

Mitochondrial DNA

 Mitochondrial DNA is located in the mitochondria.

 Contains 100-1,000 copies per cell.

 Mitochondrial DNA chromosomes usually have closed, circular structures, and contain
for example 16,569 nucleotides in human.

 Mitochondrial DNA is haploid, coming only from the mother.

 The mutation rate for mitochondrial DNA is generally higher than nuclear DNA.

Functions of DNA

DNA has a crucial role as genetic material in most living organisms. It carries genetic
information from cell to cell and from generation to generation.

Thus its major functions include:

 Storing genetic information

 Directing protein synthesis

 Determining genetic coding

  Directly responsible for metabolic activities, evolution, heredity, and differentiation.

RNA

RNA, abbreviation of ribonucleic acid, complex compound of high molecular weight that
functions in cellular protein synthesis and replaces DNA (deoxyribonucleic acid) as a carrier
of genetic codes in some viruses. RNA consists of ribose nucleotides (nitrogenous bases
appended to a ribose sugar) attached by phosphodiester bonds, forming strands of varying
lengths. The nitrogenous bases in RNA are adenine, guanine, cytosine, and uracil, which
replaces thymine in DNA. The ribose sugar of RNA is a cyclical structure consisting of
five carbons and one oxygen. The presence of a chemically reactive hydroxyl (−OH) group
attached to the second carbon group in the ribose sugar molecule makes RNA prone
to hydrolysis. This chemical lability of RNA, compared with DNA, which does not have a
reactive −OH group in the same position on the sugar moiety (deoxyribose), is thought to be one
reason why DNA evolved to be the preferred carrier of genetic information in most organisms.
The structure of the RNA molecule was described by R.W. Holley in 1965.

RNA structure

RNA typically is a single-stranded biopolymer. However, the presence of self-complementary

sequences in the RNA strand leads to intrachain base-pairing and folding of the ribonucleotide
chain into complex structural forms consisting of bulges and helices. The three-dimensional
structure of RNA is critical to its stability and function, allowing the ribose sugar and the
nitrogenous bases to be modified in numerous different ways by cellular enzymes that attach
chemical groups (e.g., methyl groups) to the chain. Such modifications enable the formation
of chemical bonds between distant regions in the RNA strand, leading to complex contortions in
the RNA chain, which further stabilizes the RNA structure. Molecules with weak structural
modifications and stabilization may be readily destroyed. As an example, in an initiator transfer
RNA (tRNA) molecule that lacks a methyl group (tRNAiMet), modification at position 58 of the
tRNA chain renders the molecule unstable and hence nonfunctional; the nonfunctional chain is
destroyed by cellular tRNA quality control mechanisms.

RNAs can also form complexes with molecules known as ribonucleoproteins (RNPs). The RNA
portion of at least one cellular RNP has been shown to act as a biological catalyst, a function
previously ascribed only to proteins.

Types and functions of RNA

Of the many types of RNA, the three most well-known and most commonly studied
are messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA), which are
present in all organisms. These and other types of RNAs primarily carry out biochemical
reactions, similar to enzymes. Some, however, also have complex regulatory functions in cells.
Owing to their involvement in many regulatory processes, to their abundance, and to
their diverse functions, RNAs play important roles in both normal cellular processes and
diseases. In protein synthesis, mRNA carries genetic codes from the DNA in
the nucleus to ribosomes, the sites of protein translation in the cytoplasm. Ribosomes are
composed of rRNA and protein. The ribosome protein subunits are encoded by rRNA and are
synthesized in the nucleolus. Once fully assembled, they move to the cytoplasm, where, as key
regulators of translation, they “read” the code carried by mRNA. A sequence of three
nitrogenous bases in mRNA specifies incorporation of a specific amino acid in the sequence that
makes up the protein. Molecules of tRNA (sometimes also called soluble, or activator, RNA),
which contain fewer than 100 nucleotides, bring the specified amino acids to the ribosomes,
where they are linked to form proteins.

Lipid

lipid, any of a diverse group of organic compounds including fats, oils, hormones, and certain
components of membranes that are grouped together because they do not interact appreciably
with water. One type of lipid, the triglycerides, is sequestered as fat in adipose cells, which serve
as the energy-storage depot for organisms and also provide thermal insulation. Some lipids such
as steroid hormones serve as chemical messengers between cells, tissues, and organs, and others
communicate signals between biochemical systems within a single cell. The membranes of cells
and organelles (structures within cells) are microscopically thin structures formed from two
layers of phospholipid molecules. Membranes function to separate individual cells from
their environments and to compartmentalize the cell interior into structures that carry out special
functions. So important is this compartmentalizing function that membranes, and the lipids that
form them, must have been essential to the origin of life itself. Water is the biological milieu—
the substance that makes life possible—and almost all the molecular components of living cells,
whether they be found in animals, plants, or microorganisms, are soluble in water. Molecules
such as proteins, nucleic acids, and carbohydrates have an affinity for water and are
called hydrophilic (“water-loving”). Lipids, however, are hydrophobic (“water-fearing”). Some
lipids are amphipathic—part of their structure is hydrophilic and another part, usually a larger
section, is hydrophobic. Amphipathic lipids exhibit a unique behaviour in water: they
spontaneously form ordered molecular aggregates, with their hydrophilic ends on the outside, in
contact with the water, and their hydrophobic parts on the inside, shielded from the water. This
property is key to their role as the fundamental components of cellular and organelle membranes.

Although biological lipids are not large macromolecular polymers (e.g., proteins, nucleic acids,
and polysaccharides), many are formed by the chemical linking of several
small constituent molecules. Many of these molecular building blocks are similar, or
homologous, in structure. The homologies allow lipids to be classified into a few major groups:
fatty acids, fatty acid derivatives, cholesterol and its derivatives, and lipoproteins. This article
covers the major groups and explains how these molecules function as energy-storage molecules,
chemical messengers, and structural components of cells.
Fatty acids

Fatty acids rarely occur as free molecules in nature but are usually found as components of many
complex lipid molecules such as fats (energy-storage compounds) and phospholipids (the
primary lipid components of cellular membranes). This section describes the structure and
physical and chemical properties of fatty acids. It also explains how living organisms obtain fatty
acids, both from their diets and through metabolic breakdown of stored fats.

Structure

Biological fatty acids, members of the class of compounds known as carboxylic acids, are
composed of a hydrocarbon chain with one terminal carboxyl group (COOH). The fragment of
a carboxylic acid not including the hydroxyl (OH) group is called an acyl group. Under
physiological conditions in water, this acidic group usually has lost a hydrogen ion (H+) to form
a negatively charged carboxylate group (COO−). Most biological fatty acids contain an even
number of carbon atoms because the biosynthetic pathway common to all organisms involves
chemically linking two-carbon units together (although relatively small amounts of odd-number
fatty acids do occur in some organisms). Although the molecule as a whole is water-insoluble by
virtue of its hydrophobic hydrocarbon chain, the negatively charged carboxylate is hydrophilic.
This common form for biological lipids—one that contains well-separated hydrophobic and
hydrophilic parts—is called amphipathic.

Saturated fatty acids

The simplest fatty acids are unbranched, linear chains of CH 2 groups linked by carbon-carbon
single bonds with one terminal carboxylic acid group. The term saturated indicates that the
maximum possible number of hydrogen atoms are bonded to each carbon in the molecule. Many
saturated fatty acids have a trivial or common name as well as a chemically descriptive
systematic name. The systematic names are based on numbering the carbon atoms, beginning
with the acidic carbon. The table gives the names and typical biological sources of the most
common saturated fatty acids. Although the chains are usually between 12 and 24 carbons long,
several shorter-chain fatty acids are biochemically important. For instance, butyric acid (C4) and
caproic acid (C6) are lipids found in milk. Palm kernel oil, an important dietary source of fat in
certain areas of the world, is rich in fatty acids that contain 8 and 10 carbons (C 8 and C10).

Unsaturated fatty acids

Unsaturated fatty acids have one or more carbon-carbon double bonds. The
term unsaturated indicates that fewer than the maximum possible number of hydrogen atoms are
bonded to each carbon in the molecule. The number of double bonds is indicated by the generic
name—monounsaturated for molecules with one double bond or polyunsaturated for molecules
with two or more double bonds. Oleic acid is an example of a monounsaturated fatty acid.
Common representative monounsaturated fatty acids together with their names and typical
sources are listed in the table. The prefix cis-9 in the systematic name of palmitoleic acid denotes
that the position of the double bond is between carbons 9 and 10. Two possible
conformations, cis and trans, can be taken by the two CH2 groups immediately adjacent to the
double-bonded carbons. In the cis configuration, the one occurring in all biological unsaturated
fatty acids, the two adjacent carbons lie on the same side of the double-bonded carbons. In
the trans configuration, the two adjacent carbons lie on opposite sides of the double-bonded
carbons.

Physical properties

Pure fatty acids form crystals that consist of stacked layers of molecules, with each layer the
thickness of two extended molecules. The molecules in a layer are arranged so that the
hydrophobic (water-fearing) hydrocarbon chains form the interior of the layer and the
hydrophilic (water-loving) carboxylic acid groups form the two faces. For a specific fatty acid
the details of the molecular packing may vary, giving rise to different crystal forms known as
polymorphs.

Protein structure –primary , secondary , tertiary and quaternary structure

protein, highly complex substance that is present in all living organisms. Proteins are of great
nutritional value and are directly involved in the chemical processes essential for life. The
importance of proteins was recognized by chemists in the early 19th century, including Swedish
chemist Jöns Jacob Berzelius, who in 1838 coined the term protein, a word derived from the
Greek prōteios, meaning “holding first place.” Proteins are species-specific; that is, the proteins
of one species differ from those of another species. They are also organ-specific; for instance,
within a single organism, muscle proteins differ from those of the brain and liver. A
protein molecule is very large compared with molecules of sugar or salt and consists of
many amino acids joined together to form long chains, much as beads are arranged on a string.
There are about 20 different amino acids that occur naturally in proteins. Proteins of similar
function have similar amino acid composition and sequence. Although it is not yet possible to
explain all of the functions of a protein from its amino acid sequence, established correlations
between structure and function can be attributed to the properties of the amino acids that
compose proteins.

General structure and properties of proteins

The amino acid composition of proteins

The common property of all proteins is that they consist of long chains of α-amino (alpha amino)
acids. The general structure of α-amino acids is shown in . The α-amino acids are so called
because the α-carbon atom in the molecule carries an amino group (―NH2); the α-carbon atom
also carries a carboxyl group (―COOH).
are linked to each other by peptide bonds between the amino group of one amino acid and the
carboxyl group of its neighbour.

Amino acid sequence in protein molecules

Since each protein molecule consists of a long chain of amino acid residues, linked to each other
by peptide bonds, the hydrolytic cleavage of all peptide bonds is a prerequisite for the
quantitative determination of the amino acid residues. Hydrolysis is most frequently
accomplished by boiling the protein with concentrated hydrochloric acid. The quantitative
determination of the amino acids is based on the discovery that amino acids can be separated
from each other by chromatography on filter paper and made visible by spraying the paper with
ninhydrin. The amino acids of the protein hydrolysate are separated from each other by passing
the hydrolysate through a column of adsorbents, which adsorb the amino acids with
different affinities and, on washing the column with buffer solutions, release them in a definite
order. The amount of each of the amino acids can be determined by the intensity of the colour
reaction with ninhydrin.

Levels of structural organization in proteins

Primary structure

Analytical and synthetic procedures reveal only the primary structure of the proteins—that is, the
amino acid sequence of the peptide chains. They do not reveal information about
the conformation (arrangement in space) of the peptide chain—that is, whether the peptide chain
is present as a long straight thread or is irregularly coiled and folded into a globule.
The configuration, or conformation, of a protein is determined by mutual attraction or repulsion
of polar or nonpolar groups in the side chains (R groups) of the amino acids. The former have
positive or negative charges in their side chains; the latter repel water but attract each other.
Some parts of a peptide chain containing 100 to 200 amino acids may form a loop, or helix;
others may be straight or form irregular coils.

The terms secondary, tertiary, and quaternary structure are frequently applied to the
configuration of the peptide chain of a protein. A nomenclature committee of the International
Union of Biochemistry (IUB) has defined these terms as follows: The primary structure of a
protein is determined by its amino acid sequence without any regard for the arrangement of the
peptide chain in space. The secondary structure is determined by the spatial arrangement of the
main peptide chain without any regard for the conformation of side chains or other segments of
the main chain. The tertiary structure is determined by both the side chains and
other adjacent segments of the main chain, without regard for neighbouring peptide chains.
Finally, the term quaternary structure is used for the arrangement of identical or different
subunits of a large protein in which each subunit is a separate peptide chain.

Secondary structure
The nitrogen and carbon atoms of a peptide chain cannot lie on a straight line, because of the
magnitude of the bond angles between adjacent atoms of the chain; the bond angle is about 110°.
Each of the nitrogen and carbon atoms can rotate to a certain extent, however, so that the chain
has a limited flexibility. Because all of the amino acids, except glycine, are asymmetric L-amino
acids, the peptide chain tends to assume an asymmetric helical shape; some of the fibrous
proteins consist of elongated helices around a straight screw axis. Such structural features result
from properties common to all peptide chains. The product of their effects is the secondary
structure of the protein.

Tertiary structure

The tertiary structure is the product of the interaction between the side chains (R) of the amino
acids composing the protein. Some of them contain positively or negatively charged groups,
others are polar, and still others are nonpolar. The number of carbon atoms in the side chain
varies from zero in glycine to nine in tryptophan. Positively and negatively charged side chains
have the tendency to attract each other; side chains with identical charges repel each other. The
bonds formed by the forces between the negatively charged side chains of aspartic or glutamic
acid on the one hand, and the positively charged side chains of lysine or arginine on the other
hand, are called salt bridges. Mutual attraction of adjacent peptide chains also results from the
formation of numerous hydrogen bonds. Hydrogen bonds form as a result of the attraction
between the nitrogen-bound hydrogen atom (the imide hydrogen) and the unshared pair
of electrons of the oxygen atom in the double bonded carbon–oxygen group (the carbonyl
group). The result is a slight displacement of the imide hydrogen toward the oxygen atom of the
carbonyl group. Although the hydrogen bond is much weaker than a covalent bond (i.e., the type
of bond between two carbon atoms, which equally share the pair of bonding electrons between
them), the large number of imide and carbonyl groups in peptide chains results in the formation
of numerous hydrogen bonds. Another type of attraction is that between nonpolar side chains
of valine, leucine, isoleucine, and phenylalanine; the attraction results in the displacement
of water molecules and is called hydrophobic interaction.

Quaternary structure

The nature of the quaternary structure is demonstrated by the structure of hemoglobin.

Each molecule of human hemoglobin consists of four peptide chains, two α-chains and two β-
chains; i.e., it is a tetramer. The four subunits are linked to each other by hydrogen bonds and
hydrophobic interaction. Because the four subunits are so closely linked, the hemoglobin
tetramer is called a molecule, even though no covalent bonds occur between the peptide chains
of the four subunits. In other proteins, the subunits are bound to each other by covalent bonds
(disulfide bridges).
Proteins as enzymes, transporters , receptors and structural elements:

Protein functions include structural support, storage, transport, cellular communications,

movement, and defense against foreign substances

1 Function: Transport of substances Examples: Hemoglobin, the iron-containing protein of

vertebrate blood, transports oxygen from the lungs to other parts of the body. Other
proteins transport molecules across cell membranes.

2. Enzymatic proteins Function: Selective acceleration of chemical reactions

Example: Digestive enzymes catalyze the hydrolysis of bonds in food molecules.

Enzymes are a type of protein that acts as a catalyst to speed up chemical reactions

3. Storage proteins Ovalbumin Amino acids for embryo Function: Storage of amino acids
Examples: Casein, the protein of milk, is the major source of amino acids for baby
mammals. Plants have storage proteins in their seeds. Ovalbumin is the protein of egg
white, used as an amino acid source for the developing embryo.
4. Hormonal proteins Function: Coordination of an organismʼs activities Example: Insulin,
a hormone secreted by the pancreas, causes other tissues to take up glucose, thus regulating
blood sugar concentration

5. Function: Movement Examples: Motor proteins are responsible for the undulations of
cilia and flagella. Actin and myosin proteins are responsible for the contraction of muscles.

6. Defensive proteins Virus Antibodies Bacterium Function: Protection against disease

Example: Antibodies inactivate and help destroy viruses and bacteria.

7. Receptor proteins Function: Response of cell to chemical stimuli Example: Receptors

built into the membrane of a nerve cell detect signaling molecules released by other nerve
cells.

8. Structural proteins Function: Support Examples: Keratin is the protein of hair, horns,
feathers, and other skin appendages. Insects and spiders use silk fibers to make their
cocoons and webs, respectively. Collagen and elastin proteins provide a fibrous framework
in animal connective tissues.

Enzymes classification and mechanism of action

“Enzymes can be defined as biological polymers that catalyze biochemical reactions.”

An enzyme is a protein or RNA produced by living cells, which is highly specific and highly
catalytic to its substrates. Enzymes are a very important type of macromolecular biological
catalysts. Due to the action of enzymes, chemical reactions in organisms can also be carried out
efficiently and specifically under mild conditions.

Enzyme Structure

Enzymes are a linear chain of amino acids, which give rise to a three-dimensional structure. The
sequence of amino acids specifies the structure, which in turn identifies the catalytic activity of
the enzyme. Upon heating, enzyme’s structure denatures, resulting in a loss of enzyme activity,
that typically is associated with temperature.

Compared to its substrates, enzymes are typically large with varying sizes, ranging from 62
amino acid residues to an average of 2500 residues found in fatty acid synthase. Only a small
section of the structure is involved in catalysis and is situated next to the binding sites. The
catalytic site and binding site together constitute the enzyme’s active site. A small number of
ribozymes exist which serve as an RNA-based biological catalyst. It reacts in complex with
proteins.
Enzymes Classification

Class 1. Oxidoreductases.

To this class belong all enzymes catalysing oxidoreduction reactions. The substrate that is
oxidized is regarded as hydrogen donor. The systematic name is based on donor:acceptor
oxidoreductase. The common name will be dehydrogenase, wherever this is possible; as an
alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor.

These catalyze oxidation and reduction reactions, e.g. pyruvate dehydrogenase, catalysing the
oxidation of pyruvate to acetyl coenzyme A.

Class 2. Transferases.

Transferases are enzymes transferring a group, e.g. a methyl group or a glycosyl group, from one
compound (generally regarded as donor) to another compound (generally regarded as acceptor).
The systematic names are formed according to the scheme donor:acceptor grouptransferase.
The common names are normally formed according to acceptor grouptransferase or donor
grouptransferase. In many cases, the donor is a cofactor (coenzyme) charged with the group to
be transferred.

These catalyze transferring of the chemical group from one to another compound. An example is
a transaminase, which transfers an amino group from one molecule to another.

Class 3. Hydrolases.

These enzymes catalyse the hydrolytic cleavage of C-O, C-N, C-C and some other bonds,
including phosphoric anhydride bonds. Although the systematic name always
includes hydrolase, the common name is, in many cases, formed by the name of the substrate
with the suffix -ase. It is understood that the name of the substrate with this suffix means a
hydrolytic enzyme.

A number of hydrolases acting on ester, glycosyl, peptide, amide or other bonds are known to
catalyse not only hydrolytic removal of a particular group from their substrates, but likewise the
transfer of this group to suitable acceptor molecules. In principle, all hydrolytic enzymes might
be classified as transferases, since hydrolysis itself can be regarded as transfer of a specific group
to water as the acceptor. Yet, in most cases, the reaction with water as the acceptor was
discovered earlier and is considered as the main physiological function of the enzyme. This is
why such enzymes are classified as hydrolases rather than as transferases.

They catalyze the hydrolysis of a bond. For example, the enzyme pepsin hydrolyzes peptide
bonds in proteins.

Class 4. Lyases.

Lyases are enzymes cleaving C-C, C-O, C-N, and other bonds by elimination, leaving double
bonds or rings, or conversely adding groups to double bonds. The systematic name is formed
according to the pattern substrate group-lyase. The hyphen is an important part of the name, and
to avoid confusion should not be omitted, e.g. hydro-lyase not 'hydrolyase'. In the common
names, expressions like decarboxylase, aldolase, dehydratase (in case of elimination of CO2,
aldehyde, or water) are used

Class 5. Isomerases.

These enzymes catalyse geometric or structural changes within one molecule. According to the
type of isomerism, they may be called racemases, epimerases, cis-trans-isomerases, isomerases,
tautomerases, mutases or cycloisomerases.

Class 6. Ligases.

Ligases are enzymes catalysing the joining together of two molecules coupled with the
hydrolysis of a diphosphate bond in ATP or a similar triphosphate. The systematic names are
formed on the system X:Y ligase (ADP-forming). For example, DNA ligase catalyzes the joining
of two fragments of DNA by forming a phosphodiester bond.

Types Biochemical Property

The enzyme Oxidoreductase catalyzes the oxidation reaction where the electrons
Oxidoreductases
tend to travel from one form of a molecule to the other.
 The Transferases enzymes help in the transportation of the functional group among
Transferases
acceptors and donor molecules.

Hydrolases are hydrolytic enzymes, which catalyze the hydrolysis reaction by

Hydrolases
adding water to cleave the bond and hydrolyze it.

Adds water, carbon dioxide or ammonia across double bonds or eliminate these to
Lyases
create double bonds.

The Isomerases enzymes catalyze the structural shifts present in a molecule, thus
Isomerases
causing the change in the shape of the molecule.

Ligases The Ligases enzymes are known to charge the catalysis of a ligation process.

Mechanism of Enzyme Reaction

Any two molecules have to collide for the reaction to occur along with the right orientation and a
sufficient amount of energy. The energy between these molecules needs to overcome the barrier
in the reaction. This energy is called activation energy.

Enzymes are said to possess an active site. The active site is a part of the molecule that has a
definite shape and the functional group for the binding of reactant molecules. The molecule that
binds to the enzyme is referred to as the substrate group. The substrate and the enzyme form an
intermediate reaction with low activation energy without any catalysts.

reactant(1)+reactant(2)→product

reactant(1)+enzyme→intermediate

intermediate+reactant(2)→product+enzyme

The basic mechanism of enzyme action is to catalyze the chemical reactions, which begins with
the binding of the substrate with the active site of the enzyme. This active site is a specific area
that combines with the substrate.

Enzyme-Substrate Interactions

Enzymes are the biocatalysts with high molecular weight proteinous compound. It enhances the
reactions which occur in the body during various life processes. It helps the substrate by
providing the surface for the reaction to occur. The enzyme comprises hollow spaces occupying
groups such as -SH, -COOH, and others on the outer surface. The substrate which has an
opposite charge of the enzyme fits into these spaces, just like a key fits into a lock. This substrate
binding site is called the active site of an enzyme (E).

The favourable model of enzyme-substrate interaction is called the induced-fit model. This
model states that the interaction between substrate and enzyme is weak, and these weak
interactions induce conformational changes rapidly and strengthen binding and bring catalytic
sites close enough to substrate bonds.

RNA catalysis

Ribozymes (ribonucleic acid enzymes) are RNA molecules that have the ability to catalyze
specific biochemical reactions, including RNA splicing in gene expression, similar to the action
of protein enzymes. The 1982 discovery of ribozymes demonstrated that RNA can be both
genetic material (like DNA) and a biological catalyst (like protein enzymes), and contributed to
the RNA world hypothesis, which suggests that RNA may have been important in the evolution
of prebiotic self-replicating systems.[1] The most common activities of natural or in vitro-evolved
ribozymes are the cleavage or ligation of RNA and DNA and peptide bond formation.[2] Within
the ribosome, ribozymes function as part of the large subunit ribosomal RNA to link amino acids
during protein synthesis. They also participate in a variety of RNA processing reactions,
including RNA splicing, viral replication, and transfer RNA biosynthesis. Examples of
ribozymes include the hammerhead ribozyme, the VS ribozyme, Leadzyme and the hairpin
ribozyme.

Before the discovery of ribozymes, enzymes, which are defined as catalytic proteins,[5] were the
only known biological catalysts. In 1967, Carl Woese, Francis Crick, and Leslie Orgel were the
first to suggest that RNA could act as a catalyst. In 1989, Thomas R. Cech and Sidney
Altman shared the Nobel Prize in chemistry for their "discovery of catalytic properties of RNA.

Activities of Ribozymes :

Although ribozymes are quite rare in most cells, their roles are sometimes essential to life. For
example, the functional part of the ribosome, the biological machine that translates RNA into
proteins, is fundamentally a ribozyme, composed of RNA tertiary structural motifs that are often
coordinated to metal ions such as Mg2+ as cofactors.[14] In a model system, there is no
requirement for divalent cations in a five-nucleotide RNA catalyzing trans-phenylalanation of a
four-nucleotide substrate with 3 base pairs complementary with the catalyst, where the
catalyst/substrate were devised by truncation of the C3 ribozyme. [15]

The best-studied ribozymes are probably those that cut themselves or other RNAs, as in the
original discovery by Cech[16] and Altman.[17] However, ribozymes can be designed to catalyze a
range of reactions (see below), many of which may occur in life but have not been discovered in
cells.[18]

RNA may catalyze folding of the pathological protein conformation of a prion in a manner
similar to that of a chaperonin.

Enzyme kinetic and kinetic parameters

Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme
kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are
investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of
this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier
(inhibitor or activator) might affect the rate.

An enzyme (E) is typically a protein molecule that promotes a reaction of another molecule,
its substrate (S). This binds to the active site of the enzyme to produce an enzyme-substrate
complex ES, and is transformed into an enzyme-product complex EP and from there to product
P, via a transition state ES*. The series of steps is known as the mechanism:

E + S ⇄ ES ⇄ ES* ⇄ EP ⇄ E + P

Michaelis–Menten kinetics

Michaelis–Menten kinetics is one of the best-known models of enzyme kinetics. It is named after
German biochemist Leonor Michaelis and Canadian physician Maud Menten.
This equation is called the Michaelis–Menten equation. Here, Vmax represents the maximum
rate achieved by the system, happening at saturating substrate concentration for a given enzyme
concentration. The value of the Michaelis constant Km is numerically equal to the substrate
concentration at which the reaction rate is half of Vmax.

Lock and key hypothesis

Definition

The lock and key model also called Fisher's theory is one of two models which describe the
enzyme-substrate interaction. The lock and key model assumes that the active site of the enzyme
and the substrate are equal shaped. It supposes that the substrate fits perfectly into the active site
of the enzyme.

Characteristics

A substrate is bond to the active site of the Enzyme by weak non-covalent bonds:

 hydrogen bonds

 hydrophobic interaction

 ionic interactions

 Van-der-Waals force

Enzymes can be defined as biological polymers that catalyze biochemical reactions. Enzymes are
a linear chain of amino acids that generate the three-dimensional structure. The sequence of
amino acids enumerates the structure, which in turn identifies the catalytic activity of the
enzyme. The structure of the enzyme denatures when heated, leading to loss of enzyme activity,
which is typically connected to the temperature. Enzymes enhance the rate of reactions. Enzymes
bind to a given substrate material to produce the desired product. When the enzyme binds to
substrate, it forms an intermediate complex before the final product is formed. The reaction takes
place in two ways as given below,

Step1: Combining of enzyme and the reactant/substrate.

E + S → [ES]

Step 2: Disintegration of the complex molecule to give the product.

[ES]→ E + P

Thus, the whole catalyst action of enzymes is summarized as:

E + S → [ES] → [EP] → E + P

Fischer has developed a Lock and Key theory to describe the mode of action of the enzyme.
According to this principle, if the right key fits inside the right lock, the lock will be opened
otherwise it will not. Likewise, if the right enzyme fits into the right substrate, the drug will
form, otherwise, it won’t. Enzyme shape provides surface configurations that can fit with the
other molecules. The molecules on which the enzymes act are known as substrates of enzymes.
Substrates that have the correct geometric shape can fit within the active site of the enzyme. The
active site of the enzyme is highly specific about the surface of its substrates. The enzyme and
substrate fit like a lock and key, making it a lock and key enzyme action model. Sometimes,
however, certain molecules close to the substrate may also interact with an enzyme’s active site.
The molecule completes with the substrate and can either slow down or stop the reaction. Such
substance is called the competitive inhibitor because it acts to prevent a product from being
created.

Induced fit model

The induced fit model is a model for enzyme-substrate interaction. It describes that only the
proper substrate is capable of inducing the proper alignment of the active site that will enable the
enzyme to perform its catalytic function. It also suggests that the active site continues to change
until the substrate is completely bound to it, at which point the final shape and charge is
determined.
The induced fit model suggested by Daniel Koshland in 1958. It is the more accepted model for
enzyme-substrate complex than the lock-and-key model. In the lock-and-key model, the
interaction of the substrate and the enzyme is likened to a key (the substrate) that is highly
specific to the lock (the active site of the enzyme).