CHAPTER 02 BIOLOGICAL MOLECULES BIOLOGICAL MOLECULES OR BIOCHEMICALES

The compounds are produced by living organisms are called biochemicals OR. All molecules / chemicals functional in living organisms, especially the organic ones, are known as bimolecular or bio chemicals. The sum total of different types of biochemical in a cell is called cellular pool which consists of in organic and organic chemicals. Cellular molecules exist in two phase. Aqueous (true and colloidal solution) and non-aqueous (chemicals as constituents of cellular structure like membrane cell wall) phases. The cell maintain their specific cellular pool with the help of selective permeable plasma membrane.

INTRODUCTION OF BIOCHEMISTRY OR CHEMISTRY OF LIFE

The branch of biology which explain the bio chemical basis of life, or study about biochemical and chemical processes in life.

Importance
1. It provides information about all the processes carried out in the living organisms as structure formation protein synthesis and control of all the mechanisms. 2. It provides information about abnormal mechanisms which lead to diseases. It helps in development of medicines. 3. Recently biochemical concepts and powerful techniques have enabled us to investigate and understand some challenging and fundamental problems in embryology, medicines, cancer and memory. Therefore it is essential to understand chemical principal and structures of bimolecular involved in cell.

CHEMICAL COMPOSITION OF CELL

The all living bodies are structurally composed of cells and living cell contains a living material called protoplasm.

Protoplasm
It is crystalloid-colloidal seat of all life activities. Chemically it contains 70 to 90 % water and remaining mass (dry wt: of cell) mainly consists of organic compounds.

ELEMENTS OR BUILDING BLOCKS OF ANIMAL BODY

The elements are classified into three groups. i. Major or principal elements carbon, hydrogen oxygen and nitrogen. These account for 97% of cellular material. ii. Minor elements ca, k, Na, Mg, Fe, S, P, CL, and Iodine. These account for 2% of cellular material. iii. True Elements Cu, Co, Mn, Zine, Silicon boron and fluorine. These account for 1% of cellular material. From above three groups only six elements carbon hydrogen, oxygen, nitrogen, phosphorous and sulphur make up about 98-99% of the biochemicals.

SOME PROPERTIES AND FUNCTIONS OF THESE SIX ELEMENTS

Elements Atomic No/WT
6/12

Molecular from of Utilization

Co2

Functions
Basic elements of organic compounds fixed during photosynthesis During photosynthesis used as reducing agent Use in aerobic Used in amino acid for protein synthesis, nucleic acids, hormones coenzymes Components of nucleic acid, ATP, phospholipids co-enzymes, NAD NADP etc Components of proteins and coenzymes

% by wt: in human body

18.5-19

Carbon (C)

Hydrogen (H)

1/1

H2O

9.5-10

Oxygen (O)

8/16

O2

65%

Nitrogen (N)

7/14

No3-1, NH4+1

3.3

Phosphorous

15/31

H2 Po4, HPo4-2

1.0

Sulphur

16/32

SO4

-2

CELLULAR POOL

IN ORGANIC MOLECULES
1. 2. 3. Occur in aqueous phase Small sized simple molecule of low molecular wt: Do not contain carbon as basic element or in which hydrogen is not directly bonded with carbons as Co2, Co, H2O 1. 2.

ORGANIC MOLECULES
Occur in aqueous and non aqueous phase Large sized complex molecular weight. molecules of high

3.

Contains carbon as basic element bounded covalently with hydrogen atom as glucose

WATER : (CHARACTERISTICS)
Water is most abundant component in the living cell. It constitutes 70-90% of the body of living beings. It is vital for the existence of life. In human, about two thirds of the body is water, of which 55% is found inside of cells (intracellular). The remaining 45% is found as extracellular water fluid in the blood, lymph and the tissue fluid. The chemical formula of water is H2, which is made up of one atom of oxygen and two atoms of hydrogen. The hydrogen and oxygen connected covalent bonds. The angle between the two hydrogen atoms is about 104.50. The water is polar (charged) molecule. The oxygen atom tends to attract the electrons to a greater extent than the hydrogen and therefore has a small negative charge (6-) while the hydrogen and shows a positive charge (8+). The separation of electrical charge is called a dipole which gives the water molecules its very important properties. Also the oxygen atom to attract the hydrogen atoms of other water molecules and this result in the formation of a weak bond called hydrogen bond.

BIOLOGICALLY
Important properties of water or significance of water in living organisms. 1. Behave as best solvent dues to polar nature of water molecules many ionic substance, polar substances dissociate in ions and dissolve in water. 2. Slow to absorb and release heat or water has high specific heat. The specific heat capacity of a substance is a measure of the amount of energy needed to rise the temperature of 1gm of that substance by 1C0. The specific heat capacity of water is high it takes a lot of energy to warm up. This thermal stability provides a constant environment for the various biochemical processes. 3. Water has high heat of vaporization. Due to hydrogen bonding which holds the water molecules together, liquid water requires higher amount of heat energy to change into vapors. 4. An amphoteric molecule: Water molecule is amphoteric because it acts both as an acid and a base. As acid it gives up electron to H+ ion. As base it gains electron to form O-H ions H2O H+ +O-H This ability of water molecules means that it is a perfect medium for the biochemical reactions occurring in cells. 5. It act as buffer (A buffer group of substance that maintains the pH of solution). 6. Co-hesive force in water molecules. Force of attraction between similar molecules is called co-hesive force. Due to the presence of hydrogen bonds in water the adhesion and cohesion force of water is high. 7. Water has the maximum density at 40C. 8. Water serves as habitat for many organisms.

-g

+g H
104.5 A0 120

Organic Molecules

Monomers (one molecule of Organic compound) 1. 2. 3. 4. Monosachuhrides Amino acids Fatty acids glycerol Nucleotides

Polymer (many molecules of organic Compound Poly sauharides Proteins Lipids Nucleic acids

SYNTHESIS OF LARGE MOLECULES BY CONDENSATION

Macromolecules are constructed from monomomers by a process called condensation dehydration synthesis because water is removed (dehydration) and bond is made (synthesis). It always takes place by proper enzyme and energy expense. At the time of joining of two monomers (condensation) a hydroxyl (-OH) group is removed from one monomers and a hydrogen (-H) is removed from monomers.

Monomer

OH

Monomer

OH

H2O

Monomer

Monomer

OH

CONDENSATION (DEHYDRATION)

HYDROLYSIS (Breaking of large molecules)

(water + breaking) It is reverse of the condensation. A process during which polymers are broken down into their sub units (monomers) by the addition of H2O is called hydrolysis. During this process a H2O molecule breaks into H+ and OH- ions with help of enzyme, where as OH group attaches to one monomers and H attaches to the others. When a bond is broken, energy is released and made available. H
Monomers Monomers OH H+

-OH
H2O

Monomers

OH H

Monomers

OH

HYDROLYSIS (HYDRATION)

TOOLPORTANCE OF CARBON (Tetravalent in nature)

The carbon is light element with 6 atomic numbers. It contains 4e- (electron) in its outer most shell and requires 4 more e (electron) to complete its outer most shell. For this purpose, it forms 4 covalent bonds with other four carbon or different atoms.

BONDING OF CARBON
Carbon can form four covalent bonds with other carbon atoms, that results in formation of skeleton and fundamental frame work of carbon in organic molecules.

P=6 N=6

Carbon containing back bone may be linear, branched or cycle by single covalent bond. H H H H H C C C C H

Melanie (4 covalent bonds with H)

H

Linear

H H

H H H H H

C H

H H C H

H (Branched) Four methyl group with carbon

Cyclic (Four carbons in cyclic way)

Carbon can be linked with other carbon by double or triple covalent bonds.
H C H Double Covalent Bond C H Triple Covalent Bond H H C C H

CHEMICAL BOND
Bond the link between two atoms. CHEMICAL BOND It is the attractive force which combines atoms together. Chemical bonds are to two main types. IONIC BOND This bond is formed due to loss or gain (electrostatic bond) of electrons as in NacL. COVALENT BOND This bond is formed by the mutual sharing of electrons between two atoms. In organic compounds covalent bonds are formed between elements. These bond store energy . TYPES OF COVALENT BOND (a) Single covalent bond. This bond is formed by the mutual sharing of one electron pairs between the atoms. CH3 CH3 Ethane.

(b) Double covalent bond: this bond is formed by the mutual sharing of two electron pairs between two atoms.
H C H C H H Ethane

(C) Triple Covalent bond this bond is formed by the mutual sharing of three electrons pairs b/w two atoms. H C C H Ethyne

Polar Covalent bond

Electron shared unequally Formed b/w any two atoms That are unlike.

Non- Polar Covalent bond

Electron shared equally Formed b/w any two atoms that are alike.

(C

O)

H2 (H

H)

(O

O)

Polar Bond Non- Polar Bond

FUNCTIONAL GROUP In organic molecules some of the hydrogen atoms are replaced by certain group of atoms that at as unit and give their properties to the organic molecules. These groups are called functional groups. Examples: Methyl-CH3 Alcohol Hydroxyl group. -OH Carboxylic acid / carboxyl. R-COOH Aldehyde R
R H C=O (R-CHO)

Ketoone

C=O (-C=O)

Amino group Sulfhydril Phosphate

NH2 C-S (- S H) - Po4

BONDS BETWEEN FUNCTIONAL GROUPS

1. ESTERBOND This bond is formed between the COOH (or acid) and OH by releasing water by condensation process.
O C Acid OH + H Alcohol O O C O + H2O

Ester Bond

2. AMID BOND It formed between acid and amine group by release of water due to condensation process.
O C Acid OH + H N CH3 H Amine O C N CH3 H Amide Bond + H2O

3. GLYCOSIDIC BONDS These are formed between aldose or ketoses group of carbohydrate with alcoholic or nitrogen group of another organic compound. Glycosidic bonds are two types, oxygen containing and nitrogen containing C-O-C or C-N-C. These bonds are communally formed during condensation of monosaccharides to form oligosaccharide and polysaccharides.
H CH2OH OH OH OH O H H O CH2OH

BIOLOGICAL MOLECULES
Biological molecules can be divided into following four main classes. 1. Proteins 2. Carbohydrate 3. Lipids 4. Nucleic acids

1. PROTEINS (Proteos= 1st Rank by Berzelius in 1838)

Protein can be defined as the polymers of amino acids, where amino acids link together in a decimate manner to perform a particular function. These are most abundant organic compounds in cells and constitute about more than 50% of dry weight. In 1883 a Duct chemist G.J Murlder recognized cell of the importance of protein as a vital compound which carry out virtually all of the cells activities. Proteins are complex organic compounds having C,H, O and N as elements but some time they contain P and S also. Due to presence of N they are called nitrogenous compounds. Proteins are building blocks of tissues many parts of living body such as hair, skin, nails and feathers are proteins. The eggs, meat, fish, milk and pluses are major sources of proteins. Amino acids are building block of proteins.

A- AMINO ACIDS
Building blocks of proteins discovered by Emil Fisher in 1902. The amino acids are monomers of proteins. These amino acids are linked together by specialized bond or linkage call peptide linkage. There are about 20 difference amino acids are known to make structure of proteins. They cytoplasm matrix is called amino acids pool:

STRUCTURE OF AMINO ACID

The amino acids contain at least one basic amino group (-NH2) and one acidic carboxylic group (-COOH); The carbon next to the carboxylic group is called the O carbon R represents side chain that is different for each amino acid. R can be simple as hydrogen in glycine, CH3 in alanine CH2OH in serine. General structural formula of amino acid.

 In different proteins the number and sequence of amino acids are different as 39 amino acid in ACTH, 51 in insulin and 574 in Hemoglobin. Essential amino acids Not produced by animal body. Non essential amino acids can be produced by body Non protein amino acids not include in protein structure ornithine citrulive

B- LINKAGE OF AMINO ACIDS:

Or how are proteins produced? Proteins are produced by condensation reactions between amino acids. A peptide bond is formed b/w two amino acids when amino group of one amino acid is linked with the carboxylic group of other amino acids with the releasing of H2O molecule.

CHAINS OF AMINO ACIDS

1. 2. 3. 4. Dipeptide (two amino acids) Tripeptied (3 amino acids) Oligopeplide (2-10 amino acids) Polypeptide (poly = many + peptide) more than 10 amino acids.

C- STRUCTURE OF PROTEINS
There are four structure levels of proteins. STRUCTURAL SEQUENCE OF LEVEL AMINO ACIDS Linear or straight of 1.Primary level amino acids. 2.Secondary level Spirally coiled results in a helix, beta sheet Secondary structure becomes folding and twisting Two or more poly peptides chains are in folding TYPES OF BOND Peptide bonds b/w amino acids Hydrogen bond sulphide bond b/w cystine amino acids Peptide, Hydrogen ionic and disulphide bonds Hydrogen ionic bonds B/W amino acids EXAMPLES Insulin Keratin hairs silk protein Lysozyme globular proteins Hemoglobin

3.Tertiary level

4.Quaternary level

FUNCTION OF PROTEINS
The proteins synthesized by the body mostly perform all activities of cell. The important as follows; 1. 2. 3. 4. 5. The structural proteins are form part of cellular structure ex. Keratin, collagen action. The transport proteins are help in the transport of specific substance ex. Hb. Protein act as antibodies, antigens fibrins (defense the body). As enzymes accelerate the rate of metabolic reactions. As hormones, growth factors and gene activators the proteins regulate metabolic activities. 6. The proteins maintain the acid base and proper fluid balance. DEF: 2 CARBOHYDRATE (CARBO=CARBON + HYDRATE=WATER)

Prlyhydroxyaldehyde or ketenes (hydrate of carbon) It is a group of organic compounds having C, O and H in which hydrogen and oxygen are mostly found in the same ratio as in water 2:1 and are this called hydrate carbons. These are found in all living cells both as building material and storage substances. They are found about 1% by weight and principle source of energy i.e. lg of glucose fields 4.9 kcal of energy. Green plants synthesise carbohydrates by process of photosynthesis. Carbohydrates are may be classified on the basis of number as follows. 1. Monocharides 2. Oliyosaealides 3. Polysaeearhide

A- MONOSACCHARIDES (GR-MONO=ONE + SACCHARON = SUGAR)

These are small simplest, carbohydrate monomers they cannot hydrolyses into simple sugars. They have a general formula of Cn (H2O)n Cn H2nOn All monosaccharide are white crystalline solids with sweet in taste and soluble in water eg. Glucose fructose and gala tore. Based on the number of carbon atoms, they are classified into: trioses, teroses, pentoses, hexoses and hepotoses. NAME Trisoe Tetrose Pentose Hexose Heptose FORMULA C3H6O3 C4H8O4 C5H10O5 C6H12O6 C7H14O7 EXAMPLE Glycerose (Glyceraldehyde) Dihydroxyacetone Eryt1hrose Erylhrulose Ribose, Deoxyribose Glucose, Fructose, Galactose Gluco heptose

Some common example of hexoses are; Glucose fructose, Galactose. 1. Glucose (Group Sugar) Founde in ripefruits, sweet corn and honey, in starch and in sugarcane with furctore. It also called blood sugar because it is the common respiratory substrate. It is dextrose (rotate polarized light to right) D.

2. Fructose (Fruit sugar). It is sweetest of sugars and found in honey all fruits, except grapes. It is laevulose (rotates polarized) 3. Galactose : it is found largely in combine to left L d state in the lactose (milk). 4. Dextrins: A polymer of D-glucose which is intermediate in complexity between starch and maltose. 5. Dextran: Any of several polysaccharide. That yield glucose unit on hydrolysis. OLIGOSACCHARIDES (OLIGO=FEW+SACCHARON = SUGAR) The oligosaccharides are small sugars formed by the condensation of 2-10 monosaccharides. Some oligosaccharides attached to membrane protein and lipids to form glycocalyx (sugar coating). They function in recognition, antigen specificity and attachment difference in human blood due to these small sugars. The oligosaccharide which contains 3-10 monosaccharide are communally called Dextrin. Depending upon the number of monosaccharide, the oligosaccharides further classified as follows; Disaccharides trisaccharides,.. Commonally accruing oligosaccharids are the disaccharides . i. Sucrose (cane sugar or commercial sugar) (non reducing sugar). Glucose + Fructose sucrose + H2O it is found in cane sugar and beet root. ii. Lactose: (Milk sugar) It is formed by condensation of glucose and Galactose it is reducing sugar. Glucose + Galactose lactose + H2O When milk sours, the lactose is converted to lactic acid. iii. Maltose (Malt sugar is reducing sugar) It is formed by the condensation between C1 and C4 of two glucose molecules. Glucose + Glucose Maltose + H2O It does not occur abundantly in nature. It can be extracted from malt, which prepared from sprouting barely. POLYSACCHARIDES (Gr. Poly= many + saccharin + sugar) These are complex, Long chain carbohydrate with high molecular weight. These are formed by condensation of a number of monosaccharides. Polysaccharides are usually tasteless insoluble without osmotic effect. Structurally these are of two types. a. Homopolysaccharides (made of only one type of monomer) eg. Starch, glycogen, cellulose (made of glucose). b. Heteropolysaccharids (made of more than one unites type of monomers. Eg. Chitin, Agar, Functionally polysaccharides are of three types (a) Storage (b) structure and (c) mucoplysaccharides i. Starch (C14H18O10). It is most important storage food material of higher plants, found in cereals, legumes, potatoes and vegetables.

 ii. iii.

Structurally, starch occur into simple sugar by hydrolysis and then oxidized to produce energy to be used in the metabolism of other bimolecules. Glycogen The glycogen called animal starch because it is reserve food stored in liver and muscles of animals. It is found in bacteria and fungi It is stored in granular form. Its structure similar to starch It formed by condensation of many glucose molecules. All the time of need glycongen hydrolyses into glucose units Structural Polysaccharides It is fibrous polysaccharide (gelucosan Homopolysaccharides) that forms the structural component of plant cell wall. It is most abundant polysaccharide (produced by plants) on earth. A micro fibril of cellulose is contain about 2000 molecules. In human diet cellulose provides roughage that stimulates peristalsis and bowel movements. It is raw material for paper fiber e-t-c.

(a) Cellulose

(b) Chitin It is the scold most abundant organic material. It is structural polysaccharide found in the cell walls of fungi and join the skeleton of arthropods (insects). The monomer of this macro molecule is nitrogen containing acetyl glucosamine, which is derived monosaccharide. It is soft and leathery, becomes hard by deposition of Ca+.

Mucoplysaccharides
They are slimy, acidic Heteropolysaccharids formed of sugar derivities, Galactose etc EX: Pectin

Pectin
They are mucoplysaccharides that occur in plant cell walls. They are polymers of galacturonic acid. The calcium petate, magnesium petate is a major part of middle lamella.

FUNCTIONS OF CARBOHYDRATE
(1) (2) (3) (4) Carbohydrates are potential source of energy. Act as storage food molecules. Work as excellent building, protective and supporting structure. They also form complex conjugated molecules.

LIPIDS (BLOOR, 1943)

(a) (b) (c)
Bloor in 1943 proposed the term lipid (lipase = fat) for those naturally occurring compounds which are insoluble in water but soluble in organic solvent. They are compounds of C, H and O where ratio of O is less than as in carbohydrate. Lipid can be classified into the given types.

Simple Lipid : Acyleglycerole (fats and oil) waxes Compound Lipid: Phospholipids, Glycolipid, Lipid proteins. Derived Lipid: Trepans, sterols, carotenoids. SIMPLE LIPIDS (a) Acyleglycerole (Triglycerole) (Neutral or true fat)
These are esters of three molecules of fatty acids and one molecule of (trihydric alcohol) glycerol. These are found in both animals and plants provide energy for metabolic activities. These are very rich in chemical energy. (Twice than carbohydrate). It is estimated that a person of average size contains 16 kg of fat which is equivalent to 144000 kcal THERE ARE TWO TYPES OF ACYLGLYCEROL SATURATED (FATS) FATTY ACIDS Posses only single bonds between carbon atoms. Solid at ordinary temperature. Found in animals High melting point Cannot undergo the process of hydrogenation (add of H) Ex. Stearin (C57 H110 O6) in beef, butter, ghee. Short chain of fatty acids. UNSATURATED FATTY ACIDS (OILS) Posses one or more double bonds between C atoms. Liquid at ordinary room temp: Found in plants Lower melting point Readily undergoes the processes of hydrogenation (oils Hard fat). Lanolin (C57 H104 O6) in cotton seed.

1. 2. 3. 4. 5. 6.

WAXES

They are ester of long chain Fatty acids with long chain Monohydric alcohols e.g Bees wax CH3 (CH2) COO (CH2)29 CH3. It is water resistant and water proof. Waxes are found as protective coating on stems, stalks, leaves petals, fruits, skins, animal skins, fur and feathers. Wax present in blood is cholesterol palpitate.

Ear wax (cermun) ear glanced lanolin (skin wax) in animals paraffin wax petroleum stearic acids candles.

COMPOUND LIPID
Phospholipids It is compound triglyceride, in which one fatty acid is replaced by a phosphate group. It is most important lipid that constituents cell membranes. The phospholipids molecule consists of two ends, one is hydrophilic (water loving) end the tail. The phospholipids regulate the plasma membrane permeability and transport processes.
Choline POLAR HEAD Phosphate Glycolipid (a) Cerobrosida (b) Gangliosida (c) Spehingolipid Spingosive (amino myelin sheath alcohol) lipoproteins Egg yolk

BACK BONE

Glycerol

NON POLAR TAIL

Fatty acid

Fatty acid

DERIVED LIPID
Some of the lipids that not contain fatty acids in their constituents Ex. Terpenoids.

TERPENOIDS
This important class of lipids built up of isoprenoid units , (C5, H8). The isoprene is hydrocarbon that has five carbons atoms arranged in branched chain. Isoprene CH3 C 1. CH = CH2

CH2 They help in oxidation and reduction processes. As trepans some are components of essential oils of. As cholesterol, they are found in cell-membranes plants. As pigments found in plants and animals. Some important classes are terpenes, steroids, carotenoids. TERPENES This group based only on isoprenoid unit (C5H8). Small size terpenes are volatile in nature, produce special fragrance. Some of these are used in perfumes. E-g. Myrccne from oil of bay, geran oil from peppermint. Larger terpenes can be found in steroids, and chlorophyll. In nature they are utilize in the synthesis of rubber and latex

2.

STEROIDS (STEROLS) These are fused ring system called steroid nucleus. The system is made of three cyclohexane rings (A,B,C) and one (D) cyclopentane ring. These are with high molecular weight Example: cholesterol

3.

IMPORTANCE OF CHOLESTEROL In the body of organism. Help to form vitamin D in the skin. It is the precursor of steroid hormones like progesterone estrogens and testosterone and cortisol. Help to forms components of lipoproteins: LDL, HDL. Is the constituent of plasma membrane? CAROTENOIDS They are pigment producing compounds in plants and animals. Carotenoids consist of fatty acid likes carbon chain, which are conjugated by double bonds carring bmembered carbon ring at each end.

These produce pigments like red (lycopene in tomato) carotene (in carrot) orange yellow, xanthophylls (02 containing) cream, green and brown colors in plants. In the animals cells, carotenoids serve as precursors for vitamin-A

FUNCTIONS OF LIPIDS
FUNCTION 1. Storage 2. Protective 3. Structural 4. Informational 5. Pigments 6. Cofactors in bio reaction TYPE Triayleglycerols Waxes Phospholipids Steroid hormones Carotenoids Carotenoids steroids EXAMPLE Adipose tissues of animals Surfaces of animals, above ground surfaces in plants Components of all membranes Sex hormones, moulting hormones in insects. Plants, animals Vitamin A, D, E

4. NUCLEIC ACIDS These are bio polymers if nucleotides with higher molecular wt: Discovered by a 22 years old Swiss physician and chemist, fried rich Meischer in 1868. He isolated a substance from the nuclei of pus cells, which was quite different from other bimolecules and named it as nuclein later due to acidic properties, the Altman renamed as nuclei acid. In 1889. Nucleic acids are present in all livings things from virus to man, in Free State or bound to proteins as nucleoproteins. The nucleic acids are the long chains of polynucleotides in which nucleotides are linked to each other.

CHEMICAL COMPOSITION
Chemically nucleic acids are composed of nucleotides. The nucleotide is a molecule (monomer) consists of following three parts. i. Pentose sugar (Ribose C5 H10 O5 or Deoxyribose C5 H10 O4). ii. Phosphoric acid (H3 Po4) (common in all nucleotides with 5th C). iii. A nitrogen base (Nitrogen containing compound). NITROGEN BASES: There are two types of nitrogen bases. PURINES PXRIMIDINES 1. Have nine membraned double Have six membered single ring. ring 2. In Purines Nitrogen atoms are Nitrogen atoms are placed at 1, 3 placed at 1,3,7 and 9 positions positions. 3. Example adenine (A) Thymine T cytosine C Uracil U Guanine (C) Formation of nucleotides in two steps 1st Step Nitrogenous base + pentose sugar Nucleoside Adenine + (NlC), Ribose (adenosine) 2nd Step Nucleoside + Phosphoric acid Nucleotide Adenosine + P (with C of sugar) AMP

TYPES OF NUCLEOTIDES
1. Mononucleotide: The mononucleotide exists singly in the cell or as part of other molecules. These are not part of DNA or RNA, some have extra phosphates (ATP). The ATP (adenosine tri-phosphate) most important, unstable molecule and carries energy from place to place within cell (currency of cell). ATP synthesized from ADP (adenosine diphosphate and Pi by capturing energy during photosynthesis. During conversion of ATP into ADP the free energy releases about (31.81k or 7.3kcal / mole energy) that utilized in energy demanding reactions. 2. Dinucleotides Sometimes two nucleotides are covalently bounded together to form compounds are called Dinucleotides. Certain B- complex vitamins like Nicotine amide and Riboflavin function as important co-enzymes and take part in oxidation (removal of e, H) reduction (add;

of e, H) reactions. These vitamins also behave like nitrogenous bases and form nudeotides. The NAD is co-enzyme activates the dehydrigenase. NAD:
Nicotine amide + Ribose + Phosphate + Phosphate + Ribose + Adenine

3. Polynucleotides The nucleic acids are polynucleotides, perform important role In living organisms they are store houses and transmitters of genetic information generation to generation. They are two kinds of nucleic acids DNA and RNA.

DIFFERENCE B/W DNA AND RNA

TYPE I II III STRAND SUGAR N. BASES DNA Double Stranded Deoxyribose C5 H10 O4 Adenine (A) Guanine (G) Cytosine (C) Thymine (T) Mainly in nucleus of eukaryotic, nucleotide region of prokaryotic, mitochondria Nuclear DNA, Nake DNA organellar DNA Genetic material in most organisms RNA Single Stranded except RNA Nucleotide contains ribose C5 H10O5 Adenine (A) Guanine (G) Cytosine (C) Uracil (U) 90% in cytoplasm, 10% in nucleus r RNA (80%) t RNA (15%) smallest m RNA (5% longest) Information carriers, genetic material in some viruses and some plants.

IV

LOCATION

KINDS

VI

FUNCTION

EXPLAIN THAT DNA ACTS AS HEREDITARY MATERIAL

DNA is a constituent of genes. The genes contain hereditary characteristic, which are transferred into new cells or new generation, so DNA is considered as hereditary material. GRIFFTH proved DNA as genetic material by transformation process in bacteria. In this process the living bacteria can get genetic material (DNA) from dead bacteria and virulent bacteria. It shows that DNA acts as genetic material. Another proof of DNA as genetic material was present by Hershey and Chase. According to their experiment it is proved that the genetic material (DNA) of one bacterial cell can be transferred into another bacteria cell by bacteriophage virus.

DNA BEHAVES AS GENETIC MATERIAL

DNA is polynuccteolide. It consists of Deoxyribose sugar, phosphate group, and four types of nitrogen bases. Sugar and phosphate do not play any role in the formation of genetic code. The four nitrogen bases are present in specific manner. These are able to encode much information. These four nitrogen bases can form many combinations of genetic codes for 20 different amino acids. The four types of nucleotides can be arranged in straight manner along a strand of DNA. Each chromosome of plant and animal cell contains billions of nucleotides, so numerous informations can be encoded in the form of genetic codes.

RNA ACTS AS A CARRIER OF INFORMATION

Ribonucleic acid (RNA) acts as carrier information from DNA to ribosome for protein synthesis. The genetic information are transferred from DNA to m. RNA and then to the cytoplasm for protein synthesis in two steps. (1) Transcription (2) Translation TRASCRIPTION 1st step in protein synthesis, takes place in the nucleus. In the process the DNA produces single stranded RNA molecules from its one strand. This mRNA carries the message out of the nucleus to ribosome in the cytoplasm. This message indicates the formation of a particular type of protein. The mRNA is attached to the ribosome which is a site of protein synthesis. TRANSLATION In this step two types of RNA, tRNA, and r-RNA take part r-RNA (ribosomal RNA) is attached to the ribosome t-RNA (transfer RNA) is present in cytoplasm. It transfers specific amino acids to the ribosome so help to translate the informations of mRNA into the arrangement of amino acids to prepare a particular type of protein. r fig-2.12 page 36
r-RNA -70-80% of total RNA of cell mRNA- 5% long RNA of cell t-RNA 15% smallest RNA of cell

A.

B.

CONJUGATED MOLECULS AND THEIR TYPES These are formed when bimolecules of two different groups combine with each other acting as unit molecules. Types, Glycolipid , Glycoproteins, Nucleoproteins and lipoprotein.

1. Glycolipids or cerebrosides (one sugar at one fatty) These are conjugate of lipids and carbohydrates acid also contains some nitrogenous compound. Examples (i) Cerebrosides (in myelin sheath of nerve) form while matter is brain. (ii) Gangliosides (in grey matter of brain) (iii) Sulpholipid in chloroplast of plants 2. Glycoprotein or Mucoids (carbohydrate + proteins) These are formed when a molecule of carbohydrate combine with a protein molecules. Most of the oligo and polysaccharides in animals and plants cell are linked covalently to protein molecules. These contain small amount of carbohydrate i.e less than 4% e.g. Albumin of egg, Gonadotrophic hormone e.t.c. Functions. (i) As antibodies in the membrane of RBCs. (ii) As cell membrane protein hormones receptors for. 3. Nucleoproteins (Nucleic acids + proteins) Found in nucleus where protein conjugated with nucleic acid. These are weakly acidic and soluble in water. 4. Lipoproteins (Lipid + proteins) (Egg yolk rich in lipoproteins) These are conjugates of lipids and proteins, the lipid is lecithin & cholesterol function Transportation of lipid in blood plasma (LDL, HDL) Component of membrance of mitochondria ER and nucleus Lamellar lipoprotein system occur in myelin sheath of nerves, photoreceptive structure in chloroplast and the membrane of bacteria.

CHAPTER # 03
INTRODUCTION A cell is a site for various biochemical activities. New tissues are constantly being made, old tissue are being replaces, energy conversion processes and disposal of waste substance occurs antinuosly. These biochemical processes do not happen spontaneously. Catalysts are required for bringing about these reactions. In living organisms, the catalysts are enzymes or biocatalysts. DEFINITION These are the organic proleineous substance which catalyses (speed up) chemical reactions in the living organisms. These increase the rate of reaction but are not consumed in the process. Enzyme (En= in + zyme = yeast) word used by fried rich Wilhelm Kuhne in 1878. Most of the enzymes are proteins. During the 1980s, however Thomas Cech and Sidney alt man discovered that certain molecules of ribonucleic and also function as enzymes, called Ribozymes. RIBOZYMES These are molecules of RNA that catatyse reactions on the phosphodiester bond of other RNA. Enzymes speed up chemical reactions, often very dramatically few examples are follows. 1. 2H2O2 catalase 40 millions one second 2H2O + O2 2. Co2 + H2O carbonic anhydrase one million CO2 in second H2CO3 ENERGY OF ACTIVATION The chemical reactions (Endergonic reaction) do not takes spontaneously. An external supply of energy is required to initiate a reaction called activation energy (Ea) or the energy that must be added, to cause molecules to react with one another is called the energy of activation. Activation energy increase the Kinetic Energy of molecules and increase the chances of collisions.

Enzymes work by lowering the activation energy needed for a reaction and speed up the reaction. This is done by bringing the reactant molecules together. CHARCTERSTICS OF ENZYME

The enzymes are biocatalysts produced in the protoplasm of cell. The basic properties are: Most of the enzymes are proteinaceous in nature (except Ribozymes). They are big molecules of globular proteins with higher mol: wt: they consists of only proteins (simple Enzymes) or may contain a non protein part (holo enzyme). They react with both acidic and alkaline substances due to the presence of protein as their major part. Enzymes generally act within living cell (endoenzymes) but sometimes they act out side of cell (exoenzymes). They are specific in their action and nature. Enzymes are required in very small quantities to bringing about a change in large amounts of substances to products.

Enzymes activities can be accelerated by certain ions or salts called activators e.g. Mn, Ni, Mg, Cl, etc. Enzymes activities can be inhibited by certain factors called inhibitors e.g. temperature, pH. The enzymes are not consumed during the reaction. They remain unaffected and can be used again and again.

MODE OF ACTION OF ENZYME

Action of enzyme is related to its structure which is complex and three dimensional. Each enzyme has a dimple or groove of a specific shape called the active site into which substrate can fit. Enzymes action occur int two steps. Step No. 1 Enzyme substrate complex occurs E + S ES (enzyme substance complex) (Enzyme) (Substrate) Step No. 2 ES E + P Product

THEORIES ABOUT THE MADE OF ACTION OF ENZYMES

There are two theories that explain the mode of action of enzyme A. LOCK AND KEY THEORY This theory proposed by Email Fischer in (1898) and later improved by Paul Filder and D.D Woods. They proposed that a particular enzyme acts on a particular substrate like particular lock can be unlocked by a particular key. This theory depends upon physical contact between substrate and enzyme molecules. The active site of each enzyme has distinct shape and distribution of charge which is complementary to its substrate, and helps in the catalytic action. Sometimes other molecules are connected with active site sometimes other molecules are connected with active site but there is bond formation and no chemical reaction.

B. INDUCE FIT MODEL OR THEORY This theory proposed by D.E Koshland in 1959. It is the modification of the lock and key theory. According to this theory when substrate combines with an enzyme, it includes changes in the enzyme structure (active site). This change enables the enzyme to perform its catalytic activity more effectively.

TYPES OF ENZYMES
Enzymes are of two types on the basic of their composition. a. Simple enzyme or proteozyme These enzymes composed wholly of protein. Eg. Amylase pepsin. b. Holoenzyme or conjugated enzyme or complex enzyme. These enzymes composed of proteins and non protein part for performing catalytic activities. Holoenzyme word used by Euler in (1932) for conjugated enzymes that showing complete activity. In Holoenzyme the protein part is called apoenzyme and non protein part called prosthetic group or co factors. On the basis of nature of prosthetic group, conjugated enzyme, are of two types. 1. Metal Activated enzymes- co factor is metal ion or e.g Mg++, Fe+++, Ca++, Zn++, K+, Mn++. 2. Co-enzymes co-factor is organic compound, loosely attached with enzyme. If organic compound is covalently attached the co-factor is called prosthetic group.
Holo enzyme

Protein part Apo-enzyme

Non-Protein part cofactor, prosthetic group

In-organic metal (activators) Metal activated enzymes Covalent Bond Prosthetic Group

Organic compound

Non-Covalent Bond Co-enzyme