Biological Molecules
Biological Molecules
➢ Introduction to Biochemistry
•     Biological molecules are different chemical
      compounds of living beings.
•     Biochemistry is the branch of biology which deals with
      the study of chemical components and chemical
      processes in living organisms.
                             On the basis of
                                                               Minor forming 1% body e.g., S, Mg, etc.
                               presence
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✓ Macro-Organic Molecules
•       Carbohydrates are composed of C, H, O and provide fuel for the metabolic activities of the cell.
        Carbohydrates are present in the cytoplasm of the cells.
•       Proteins are the most abundant organic compounds in protoplasm. Proteins are present in the membranes,
        ribosomes, cytoskeleton and enzymes of the cell.
•       Lipids are heterogenous groups of hydrophobic compounds. Lipids are present in the membranes and
        cytoplasm of the cell
•       Nucleic acids (DNA and RNA) are most essential organic compounds, for living organisms. The nucleic acid
        DNA is present in the chromosome. The nucleic acid RNA is present in the nucleoplasm and cytoplasm.
1. C-H bond            Hydrocarbon (potential source of chemical energy for cellular activities)
2. C-N bond            Peptide bond (forms proteins which are very important due to their diversity in structure and
                       function)
3. C-O bond            Glyosidic bond (provides stability to complex carbohydrate molecules)
                        Condensation                                               Hydrolysis
    •     Condensation is the combination of monomers into •         The hydrolysis is essentially the reverse of
          polymer by the removal of water.                           condensation i.e., the breakdown of a polymer
                                                                     into its monomers by the addition of water.
    •     During condensation, a hydroxyl (OH -) group is •          During hydrolysis, an (OH-) group from water is
          removed from one monomer and a hydrogen (-H)               attached to one monomer and (H) is attached
          is removed from the other to make water and as a           to the other monomer. All digestion reactions
          result a bond is synthesized between the                   are example of hydrolysis.
          monomers.     Condensation    is   also   called
          dehydration synthesis.
➢ Importance of water
•       Water is the most abundant compound in all organisms.
•       It varies from 65 to 89 percent (FTB = 70%, BTB & KPK = 70 to 90%) in different organisms.
•       Human tissues contain about 20 percent water in bone cells and 85 percent (FTB = 85 to 90%) in brain cells.
•       Seeds also contain 20% water.
•       Blood contains 88% water.
•       Cucumber contains 98% water.
•       Jelly fish has exceptionally large amount of water i.e. 99% that’s why its body shows transparency.
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✓ Solvent Properties
•   Due to its polarity, water is an excellent solvent for polar substances and hence called universal solvent.
•   Ionic substances when dissolved in water, dissociate into positive and negative ions.
•   Non-ionic substances having charged groups in their molecules are dispersed in water.
•   It is because of this property of water that almost all reactions in cells occur in aqueous media.
•   Nonpolar organic molecules, such as fats, are insoluble in water and help to maintain membranes which make
    compartments in the cell.
✓ Hydrogen Bonding
•   The polarity of water molecules makes them interact with each other.
•   The charged regions on each molecule are attracted to oppositely charged regions on neighbouring
    molecules, forming weak bonds.
•   Since the positively charged region in this special type of bond is
    always an H atom, the bond is called a hydrogen bond.
•   This bond is often represented by a dotted line because a hydrogen
    bond is easily broken.
•   The presence of hydrogen bonds among water molecules causes it
    to remain in liquid state rather than change to ice or steam.
•   Without hydrogen bonds, water would boil at -80 degree Celsius
    and freeze at -100 degree Celsius.
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✓ Hydrogen Exclusion
•   Hydrophobic exclusion can be defined as reduction of the
    contact area between water and hydrophobic substances
    which are placed in water.
•   Biologically, hydrophobic exclusion plays key roles in
    maintaining the integrity of lipid bilayer membranes.
✓ Ionization of Water
•   The dissociation of a molecule into ions is called ionization.
                                                                      Hydrophobic Exclusion.
•   When water molecule ionizes, it releases an equal number of
    positive hydrogen and negative hydroxyl ions.
•   This reaction is reversible but an equilibrium is maintained.
•   At 25 degree C the concentration of each of H+ and OH - ions in pure
    water is about 10-7 mole/litre.
•   The H+ and OH - ions effect and take part in many chemical reactions that
    occur in the cells.
✓ Protection
•   Water is an effective lubricant that provides protection against the damage resulting from friction.
•   For example, tears protect the surface of eye from the rubbing of eyelids.
•   Water also forms a fluid cushion around organs that helps to protect them from trauma.
•   For example, pleural fluid around lungs, pericardial fluid around heart, CSF around brain.
➢   Carbohydrates
•   Carbohydrates are the most abundant biomolecule in nature.
•   The word carbohydrate literally means hydrated carbons.
•   They are composed of carbon, hydrogen and oxygen and the ratio of hydrogen and oxygen is the same as in
    water i.e. 2:1.
•   Their general formula is Cx(H2O)y where x is the whole number from three to many thousands whereas y may
    be the same or different whole number.
•   Chemically, carbohydrates are defined as “polyhydroxy aldehydes or ketones, or complex substances which
    on hydrolysis yield polyhydroxy aldehyde or ketone subunits.”
•   They are strong reducing agents.
•   The sources of carbohydrates are green living things e.g. plants, cyanobacteria, algae and many bacteria.
•   These are the primary products of photosynthesis.
•   One gram of carbohydrates gives 4.1 kcal of energy.
•   Carbohydrates are commonly known as sugar or saccharides.
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✓ Classification of carbohydrates
Carbohydrates
➢ Monosaccharides
•     Monosaccharides are only true carbohydrates.
•     All carbon atoms in a monosaccharide except one, have a hydroxyl group.
•     The remaining carbon atom is either a part of an aldehyde group or a keto group.
•     Their general formula is CnH2nOn.
✓ Classification of monosaccharides
•     It may be on the basis of functional group or number of carbon atoms.
•     On the basis of functional group, the monosaccharides containing aldehyde are called aldoses while those
      containing ketone are called ketoses.
•     The range of number of carbons in monosaccharides is 3 to 7. Hence,monosaccharides are classified into five
      groups based upon number of carbon atoms i.e., trioses (3C), tetroses (4C), pentoses (5C), hexoses (6C) and
      heptoses (7C).
•     Tetroses are rare in nature and ocuur in some bacteria.
•     Most common are pentose and hexose. Most common hexose is glucose.
Glyceraldehyde
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                         Dihydroxy
                         acetone
✓ Stereomerism in Glucose
•     Stereoisomers are molecules that have the same
      molecular formula and differ only in how atoms are
      arranged in 3D space.
•     Enantiomers is a type of stereoisomers in which
      molecules are non superimposable mirror-images.
•     An example of enantiomer is D and L glucose. D
      sugars are right handed and L-sugars are left handed
      molecules.
✓ Occurrance of Glucose
•     In free state, glucose is present in all fruits, being abundant in An example of enantiomers.
      grapes, figs, and dates.
•     Grapes contain as much as 27% glucose.
•     Our blood normally contains 0.08% glucose. Human blood contains 100 mg of glucose per 100 ml of blood.
      That’s why glucose is known as blood sugar.
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•   In combined form, it is found in many disaccharides and polysaccharides.
•   Starch, cellulose and glycogen yield glucose on complete hydrolysis only.
•   Glucose is naturally produced in green plants through photosynthesis.
•   For the synthesis of 10g of glucose 717.6 kcal of solar energy is used. This energy is stored in the glucose
    molecules as chemical energy and becomes available in all organisms when it is oxidized in the body.
➢ Oligosaccharides
•   These are comparatively less sweet in taste, and less soluble in water.
•   On hydrolysis oligosaccharides yield from two to ten monosaccharides units
•   The ones yielding two monosaccharides are known as disaccharides, those yielding three are known as
    trisaccharides and so on.
➢ Polysaccharides
•   Polysaccharides are the most complex and the most abundant carbohydrates in nature.
•   They are usually branched and tasteless.
•   They are formed by several (more than 10) monosaccharides linked by glycosidic bond.
•   Polysaccharides have high molecular weights and are only sparingly soluble in water.
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✓ Types of Polysaccharides
Polysaccharides can be classified as:
           Homopolysaccharides                                    Heteropolysaccharides
 The polysaccharides which are composed by the          The polysaccharide which are composed by the
 condensation of only one kind of monosaccharides       condensation of different kind of monosaccharides are
 are called homopolysaccharides.                        called heteropolysaccharides.
 e.g., starch, glycogen, cellulose, chitin.             e.g., agar, pectin, peptidoglycan.
Some common homopolysaccharides are discused here
❖ Starch
•  Starch is formed by the condensation of hundreds of a-glucoses.
•  It is called storage carbohydrate of plants. It is mainly stored in root, stem and seeds.
•  It is found in roots, grains, seeds and tubers.
•  Starch is digested in oral cavity and in small intestine by the enzyme amylase. Upon hydrolysis it yields
   maltose first and then maltose is further digested by maltase enzyme and yields glucoses.
• It gives blue colour with iodine solution.
• It is the main souce of carbohydrates in diet for animals.
• There are two types of starches i.e., amylose and amylopectin.
1. Amylose:
• It is un-branched i.e., a linear chain of glucoses in which glucoses are attached together by α-1, 4-glycosidic
   linkages.
• It is soluble in hot water and insoluble in cold water.
2. Amylopectin:
• It has branched structure i.e., a linear chain of glucoses having α-1,4 glycosidic linkages but more chains of
   glucoses in the form of branches are also attached by α-1, 6-glycosidic linkages. (after 20 monomers, there is
   a branch).
• It is completely insoluble in both hot and cold water. Mnemonic: AmylopecTIn = Totally Insoluble
Structure of starches.
❖ Glycogen
• Glycogen is also composed of a-glucoses.
• It is called storage carbohydrate of animals. It is
  found abundantly in liver and muscles, though found
  in all animal cells. It is also found in fungi.
• It is also known as animal's starch.
• The digestion of glycogen is also quite similar to that
  of starch. It yeilds maltose upon initial hydrolysis and
  glucose after complete hydrolysis.
• It gives red colour with iodine solution.
                                                                       Structure of Glycogen
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•    Structure of glycogen resembles with amylopectin starch but glycogen has much more branching than
     amylopectin (after 10 monomers,there is a branch)
•    It is insoluble in water.
❖ Cellulose (Fiber)
•    Cellulose is the most abundant carbohydrate on earth.
•    It is formed by condensation of hundreds of β-glucoses.
•    It is structural carbohydrate of plants because it is the main constituent of their cell wall of plants (and algae
     also).
•    Cotton and paper are pure forms of cellulose.
•    It is not digested by human digestive tract. In herbivores, it is
     digested because of micro-organisms (bacteria, yeast and
     protozoa) in their digestive tract which secrete cellulase for
     digestion of cellulose.
•    Upon intial hydrolysis, it yeilds cellubiose (a disaccharide with
     beta 1,4-glycosidic linkage) and after complete hydrolysis, it
     yeilds glucose.
                                                                                    Structure of cellulose
•    It gives no colour with iodine solution.
•    Cellulose is added to iodine, the colour of iodine solution remains intact that is light orange brown [SZABMU
     MDCAT-I 2024]
•    It is highly insoluble in water.
•    Its structure resembles amylose starch as it is also unbranched but
     it has β-1,4 glycosidic linkages between glucoses.
❖ Chitin
•    Chitin is second most abundant organic molecule on earth.
•    It is a derivative of N-acetyl glucosamine monomers.
•    It is a structural carbohydrate found in cell walls of fungi and in the
     exoskeleton of arthropods.
•    It is also known as fungal cellulose.
•    Like cellulose, chitin is also undigestable.                                       Structure of chitin.
•    It is unbranched and it has β-1,4 glycosidic linkage between its
     monomers.
➢    Proteins
•    Word “protein” has been derived from greek word proteios meaning prime or first.
•    Proteins are the most abundant organic compounds to be found in cells and comprise over 50% of their total
     dry weight.
•    One gram of protein gives 4.6 kcal of energy.
•    All proteins contain C, H, O and N, while some contains P, S. Few proteins have Fe, I and Mg incorporated into
     the molecule.
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✓ Structure and Composition of Proteins
•   Chemically proteins can be defined as polymers of amino acids or polypeptide chains.
•   The number of amino acids varies from a few to 3000 or even more in different proteins.
❖ Amino acids
•   About 170 types of amino acids have been found to occur in cells and
    tissues.
•   Of these, about 25 are constituents of proteins.
•   Most of the proteins are however, made of 20 types of amino acids.
•   All the amino acids have an amino group (-NH₂) and a carboxyl group (-
                                                                                General structure     of   an
    COOH) attached to the same carbon atom also known as alpha carbon.          amino acid
•   The general formula of amino acids is:
•   -R group is a variable group. It may be –H in glycine or –CH3 in alanine.
❖ Peptide linkage
•   Amino acids are linked together to form polypeptides chains.The linkage between the hydroxyl group of
    carboxyl group of one amino acid and the hydrogen of amino group of another amino acid release H₂O and C-
    N link to form a bond called peptide bond.The resultant compound has two amino acid subunits and is a
    dipeptide.
•   A dipeptide has two ends; one is called amino or -N terminal end while other is called carboxylic acid or -C
    terminal end.
•   A new amino acid can be added in this chain from its carboxylic acid or -C terminal end in the same way.
•   Similarly, when several amino acids are linked together by many peptide bonds, the polypeptide chain is
    formed.
➢ Structure of Proteins
There are four levels of organization of a protein molecule.
✓ Primary Structure
•   The primary structure comprises the number and sequence of amino acids in a protein molecule.
•   F. Sanger in 1951 was the first scientist who determined the sequence of amino acids in a protein (insulin).
•   Insulin is composed of 51 amino acids(49 peptide linkages) in two chains. One of the chains had 21 amino
    acids and the other had 30 amino acids and they were held together by disulphide bridges.
•   Similarly, Haemoglobin is composed of 574 amino acids (570 peptide linkages) in four chains, two alpha and
    two beta chains. Each alpha chain contains 141 amino acids, while each beta chain contains 146 amino acids.
•   The size of a protein molecule is determined by the type and number of amino acids comprising that
    particular protein molecule.
•   To calculate the number of possible peptides of a given length from a set of amino acids, you use the
    formula: Number of peptides = (number of amino acids)(length of peptide)
•   For example, Number of different dipeptides from five different amino acids is 52 = 25 dipeptides.
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✓ Secondary structure
•   The polypeptide chains then usually coil into α-helix, or into some other regular configuration which is a
    secondary structure.
• One of the secondary structures, α-helix involves a spiral formation of polypeptide chain.
• It is a very uniform geometric structure with 3.6 amino acids in each turn (36 in 10 turns) of the helix.
In chemistry, select option that there are 27 amino acid units for each turn of the helix.
• The helical structure is kept by the formation of hydrogen bonds among amino acid molecules in successive
    turns of the spiral.
• β-pleated sheet is formed by folding back of the polypeptide.
✓ Tertiary Structure
•   Usually a polypeptide chain bends and folds upon itself forming a globular shape or 3-D structure. This is the
    proteins' tertiary conformation.
•   It is maintained by three types of bonds, namely ionic, hydrogen, and disulfide (-S-S-).
•   Disulphide bridges are present in antibodies and are formed by the presence of cysteine.
•   In aqueous environment the most stable tertiary conformation is that in which hydrophobic amino acids are
    buried inside while the hydrophilic amino acids are on the surface of the molecule.
•   Metal ion coordination can be seen from tertiary structure onwards, e.g Fe2+ as heme group.
✓ Quarternary Structure
• When two or more polypeptide tertiary chains are aggregated and held together by hydrophobic
  interactions, hydrogen and ionic bonds, the specific arrangement is the quaternary structure.
• For e.g, hemoglobin.
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✓ Significance of Sequence of Amino Acids
    4. They are non-crystalline and are elastic in           4. They are crystalline and inelastic.
         nature.                                             5. (mnemonic:GC= Globular Crystalline)
    5. They perform structural roles in cells and            6. They disorganize with changes in the physical and
         organisms.                                              physiological environment.
    Examples                                                 Examples
    Silk fiber (from silk worm, spiders web) Actin and       Enzymes, antibodies, hormones, hemoglobin, myoglobin,
    myosin (in muscle cells)                                 channel proteins, albumen of egg white and proteins of cell
    Fibrin (of blood clot)                                   membranes.
    Keratin (of nails, hair, fur, outer skin) Collagen (in
    skin, ligaments, tendons, bones and in cornea of
    eyes).
Note: Myosin, a fibrous protein has enzymatic activity due to its globular heads.
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✓ Role of Proteins
Some proteins have structural roles while some have functional roles.
• Following is the list of structural proteins.
➢ Lipids
•     Lipid is the collective name for variety of organic compounds such as fats, oils, waxes and fat-like molecules
      (steroids) found in the body.
•     Therefore, it is defined as a heterogeneous group of organic compounds.
•     Most lipids are non-polar and are insoluble in water (hydrophobic) but soluble in organic solvent such as
      acetone, alcohol, and ether etc.
•     Lipids are composed of carbon, hydrogen and oxygen. However, they have relatively less oxygen in proportion
      to carbon and hydrogen.
•     For instance, tristearin is a simple lipid which shows molecular formula as C57H110O6.
•     Due to high contents of carbon and hydrogen, they store double amount of energy than carbohydrates.
•     One gram of lipid gives 9 kcal of energy.
•     Bloor proposed the term Lipid in 1943.
✓ Function of Lipids
•     Lipids are components of cellular membranes (e.g, phospholipids and cholestrol).
•     They act as energy stores (e.g, triglycerides).
•     Some hormones are lipids For e.g., auxins, gibberellins and cytokinins among plant hormones and
      aldosterone and sex hormones among animal hormones.
•     Lipids are also involved in protection, insulation, waterproofing and buoyancy.
•     Waxes, in the exoskeleton of insects. and cutin, an additional protective layer on the cuticle of epidermis of
      some plant organs e.g. leaves, fruits, seeds etc., are some of the main examples.
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➢ Classification of Lipids
•   Lipids have been classified as acylglycerols, waxes, phospholipids, sphingolipids, glycolipids and terpenoid
    lipids.
✓ Acylglycerol
•   The most abundant lipids in living things are acylglycerols.
•   Acylglycerols can be defined as esters of
    glycerol (alcohol) and fatty acids.
• An ester is the compound produced as the
    result of a chemical reaction of an alcohol with
    acid and a water molecule is released such a
    reaction is called esterification.
• Glycerol is a trihydroxy alcohol which contains
    three carbons, each bears an OH group.
• A fatty acid is a type of organic acid containing
    one carboxylic acid group attached to a
    hydrocarbon.
• Fatty acids contain even number of carbons
    from 2 to 30.
• Each fatty acid is represented as R-COOH,                Formation of a triacylglycerol (in the presence
    where R is a hydrocarbon tail.                                        of H+ catalyst) - FTB
      1. When one glycerol molecule combines
          chemically with one fatty acid, a
          monoacylglycerol (monoglyceride)
          is formed.
      2. When two fatty acids combine with
          one glycerol a diacylglycerol is
          formed.
      3. Similarly, three fatty acids + one
          glycerol molecule = triacylglycerol.
• Triacylglycerols are also called neutral
    lipids as all three charge bearing OH
    groups are occupied by three fatty
    acids.
• The most widely spread acylglycerol is
    triacylglycerol.
• In the formation of acylglycerols, OH is
    released from alcohol and H from acid
    which are together released as water
    molecule. (But according to FTB, OH is                In the presence of enzyme catalyst - PTB
    taken from acid and H from alcohol).
Reason: In laboratory/in vitro/chemistry, OH comes from acid because there is H+ catalyst and it is nucleophilic
substitution of carboxylic acid. But in vivo/in cell/in biology, ther reaction is carried out by enzymes and in its
mechanism, enzyme removes OH from alcohol and H from acid.
❖ Fatty Acids Properties
•   About 30 different fatty acids are found.
•   Acetic acid (2C) and butyric acid (4C) are simplest fatty acid.
•   Palmitic acid (16C) and stearic acid (18C) are most common fatty acids.
•   Some properties of fatty acid are increased with an increase in number of carbon atoms, such as melting
    point, solubility in organic solvent and hydrophobic nature.
•   For e.g., Palmitic acid (C16) is much more soluble in organic solvents and has higher melting point than butyric
    acid (C4).
•   Most fatty acids in plants contain 16-18 carbon per molecule
•   In animals the fatty acids are straight chains, while in plants these may be branched or ringed.
•   Fatty acids may be saturated or unsaturated.
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                Saturated fatty acids                                      Unsaturated fatty acids
    1. They contain no double bond.                            1. They contain upto six(1-6) double bonds.
    2. Saturated fatty acids tend to be solid at room          2. Unsaturated fatty acids tend to be liquid at room
        temperature.                                              temperature.
    3. They have higher melting point.                         3. They have lower melting point.
    4. They contain more energy due to more C-H                4. They contain less energy due to less C-H bonds.
        bonds.
    5. They are more common in animal lipids which             5. They are more common in plant lipids which are
        are called fats.                                           called oils.
    Exapmles:                                                  Examples:
    Lauric acid, myristic acid, palmitic acid, stearic acid.   Oleic acid, linoleic acid, linoleneic acid, arachidonic acd.
✓ Waxes
•      Waxes are highly hydrophobic compounds.
•      There are two types of wax.
•      Natural waxes are simple lipids.
•      They are typically esters of long chain fatty acids and long chain alcohols.
•      They are solid at room temperature because they have high melting point.
•      They are stable compound/inert and resistant to degradation and atmospheric oxidation.
•      They are widespread as protective coatings on fruit and leaves and protect plants from water loss and
       abrasive damage.
•      They also provide water barrier for insects, birds and animals like sheep.
•      For example:
        1. bees wax (the most common animal wax and found in honeycomb)
        2. cutin (on leaf surfaces and fruits) of plants)
        3. suberin (in plant roots)
        4. lanolin (found in sheep wool)
•      Synthetic waxes which are generally derived from petroleum or polyethene.
•      For e.g., paraffin wax which is used to make candles.
•      The most common plant wax is epicuticular wax.
✓ Phospholipids
•      These are the most abundant lipids.
•      Phospholipids are derivatives of phosphatidic acid.
•      A phosphatidic acid molecule is most similar to diglyceride that it contains a glycerol, two fatty acids
       esterified with first and second OH groups of glycerol and a phosphate group esterified with third OH group
       of glycerol.
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•   A phospholipid is formed when phosphatidic acid combines with one of the four organic compounds such as :
    1. choline (a nitrogenous base)                                 2. ethanolamine (an amino alcohol)
    3. inositol (an amino alcohol)                                  4. serine (an amino acid).
•   Most common type of phospholipid is phosphatidylcholine also called lecithin in which choline is attached to
    phosphate group of phosphatidic acid.
•   Phospholipids are major compononets of cell membranes in the form lipid bilayer because they are
    amphiphilic.
•   One end of the phospholipid molecule, containing the phosphate group and additional compound (head
    region) is hydrophilic i.e, polar and readily soluble in water.
•   The other end, containing the fatty acid side chain (tail region) is hydrophobic i.e. non-polar.
•   All lipids are hydrophobic except phospholipids head.
•   Phospholipid protein complex are present in milk, blood, cell nucleus and eggs.
✓ Terpenoids
• Terpenoids are a very large and diverse group of organic compounds.
• They are the only polymers among the class of lipids and are non-fatty
  acid lipids.
• The building block of terpenoids is a five-carbon isoprenoid unit.
• Classification of terpenoids: Isoprenoid unit by condensation in
  different ways give rise to compounds such as rubber, carotenoids,
  steroids and terpenes.
✓ Steroids
• Steroids are non-fatty acids lipids of high molecular weight
  which can be crystalline.
• A steroid nucleus consists of 17 carbon atoms arranged in four
  attached rings.
• Three of the rings are six sided, and the fourth is five sided.
• These structures are synthesized from isoprene units.
• Example, cholesterol is the structural component of cell
  membrane and brain tissue.                                                   Steroid Nucleus
• Sex hormones like estrogen, progesterone in female and
  testosterone in male are steroids in nature.
• Vitamin D which regulates calcium metabolism and bile salts which emulsify fats are steroids.
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✓ Prostaglandins
•   The name prostaglandins is derived from prostate gland because it was first isolated from seminal fluid in
    1935.
•   It was believed to be part of prostatic secretions.
•   They are found in every mammalian tissue and act as local hormones.
•   They are derivatives of arachidonic acid.
•   Every prostaglandin contains 20 carbon atoms including a 5-carbon ring.
•   Aspirin like drugs inhibit synthesis of prosatglandin.
➢ Nucleic Acid
•   Nucleic acids were first isolated (in 1869) by a Swiss physician, Fredrick miescher from the nuclei of pus cells
    (white blood cells) and sperm of salmon fish.
•   He named this molecule as nuclein, because it was located in the nucleus.
•   The basic structure and chemical nature of nuclein was determined (in 1920) and was renamed as nucleic acid
    because of its acidic nature.
•   Nucleic acids are of two types, DNA and RNA.
                                 Nucleic Acids
    tRNA transfers Amino          rRNA catalytic part of         mRNA transfers information about amino acid
            acids                     ribosomes                                   sequence
•   DNA occurs in chromosomes, in the nuclei of the cells and in much lesser amounts in mitochondria and
    chloroplasts. RNA is present in the nucleolus, in the ribosomes, in the cytosol and in smaller amounts in other
    parts of the cell.
•   Both are linerar, unbranched polymers of nucleotides.
•   DNA is stable long-term protein and nucleic acid but RNA degrades within 30 minutes in cell.
✓ Constituents of Nucleotide
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•   The partial hydrolysis of nucleic acids yield compounds known as nucleotides or nucleosides.
•   While, complete hydrolysis yields a mixture of bases, pentose sugars and phosphate ions.
•   Nucleotides of DNA are deoxyribonucleotides while that of RNA are ribonucleotides.
•   Both nucleotides consists of three parts
    1. a pentose sugar                                   2. a phosphate
    3. a nitrogen containing ring structure called base.
•   The pentose sugar in deoxyribonucleotides is deoxyribose and in ribonucleotides is ribose.
•   Deoxyribose has same structure as ribose except it has one oxygen removed from OH at carbon 2.
•   Di-deoxyribonucleoside triphosphates are used to terminate DNA synthesis at different sites in Sanger’s
    method.
•   Phosphoric acid is a common component of both
    nucleotides which provides acidic properties to
    DNA and RNA.
•   The nitrogen containing heterocyclic structures
    are called bases because of unshared pair of
    electron on nitrogen atoms, which can thus
    acquire a proton.
•   There are two major classes of nitrogenous
    bases i.e., single six cornered ring, pyrimidine
    and double ring (a 6 cornered ring attached to a
    5 cornered ring)purines.
•   Pyrimidine bases are of three types i.e., cytosine
    (C), thymine (T) and uracil (U). Thymine is only
    found in DNA while the uracil is only found in
    RNA.
•   Purine bases are also two types i.e., adenine (A)
    and guanine (G).
                                           Formation of nucleotide
•   During the formation of a typical nucleotide, firstly nitrogenous base is linked with 1' carbon of pentose sugar.
    Such combination is called nucleoside.
•   The bond that combines the base with sugar is called glycosidic bond (formed between C'1 of pentose sugar
    and N9 of purines or N1 of pyrimidines)
•   When a phosphoric acid is linked with 5' carbon of pentose sugar of a nucleoside, the nucleotide is formed.
•   A nucleotide with one phosphoric acid is called nucleoside monophosphate, with two phosphoric acids is
    called nucleoside diphosphate and with three phosphoric acids is called nucleoside triphosphate.
•   The nucleotides which take part in the formation of DNA or RNA polymer must contain three phosphates but
    during their incorporation into DNA or RNA polymer each nucleotide losses its two terminal phosphates.
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✓ Phosphodiester Linkages
•   The bond formed between phosphoric acids (H3PO4)
    and hydroxyl (OH) groups of pentose sugar is called
    ester linkage.
•   In a polynucleotide chain one phosphoric acid is
    attached to the OH group of carbon no. 3 of pentose
    sugar in front while carbon No 5 of another pentose
    sugar behind it forming phosphodiester linkage(C-
    O-P-O-C) between consecutive nucleotides.
•   When one nucleotide joins to other in formation of
    polynucleotide, the molecule that is released is not
    water but pyrophosphate (two phosphate groups
    bound together). When pyrophosphate is cleaved by
    the addition of water, a great deal of free energy is
                                                                        Phosphodiester Bond
    released.
•   In this way nucleotides begin to link by phosphodiester bonds and a polymer of nucleotides (polynucleotide)
    is formed.
✓ Types of RNA
•   There are three main types of RNA.
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❖ Transfer RNA (tRNA)
• It comprises about 10 to 20% (BTB = 15%) of the cellular RNA.
• Transfer RNA molecules are smallest among RNA, each with a
  chain length of 75 to 90 (BTB = 80) nucleotides.
• A tRNA is a single stranded molecule but it shows a duplex
  appearance at its some regions where complementary bases
  are bonded to one another.
• It shows a flat cloverleaf shape in two dimensional views.
• Its 5' end always terminates in Guanine base while the 3' end
  is     always     terminated    with     base    sequence     of
  CCA.(mnemonic:Come CAt = CCA)
• Amino acid is attached to tRNA at 3 end.
• It transfers amino acid molecules to the ribosomes where
  peptide chains are being synthesized to form proteins.                   Cloverleaf Model of tRNA.
• There is one specific tRNA for cach amino acid. So, the cell will
  have at least 20 kinds of tRNA molecules.
• Sixty tRNA have been identified. However, human cells contain about 45 different kinds of tRNA.
• tRNA has three loops:
  1. Middle loop
  The middle loop in all the tRNA is composed of 7 bases, the middle three of which form the anticodon; it is
  complementary to specific codon of mRNA.
  2. D-loop
  D loop recognizes the activation enzyme.
  3. Theta loop
  Theta loop recognizes the specific place on the ribosome for binding during protein synthesis.
Mnemonic: MA = Middle Anticodon, AD = Activation of enzyme D-loop, TB = Theeta Binds ribosomes
➢ Conjugated Molecules
•   Two different molecules, belonging to different categories, usually combine together to form conjugated
    molecules.
✓ Glycoproteins (Carbohydrate + Protein)
•   Carbohydrates combine covalently with proteins to form glycoprotein.
•   Most of the cellullar secretions are glycoprotein in nature.
       (mnemonic: SP = Secretion Proteins (glyco), not glycolipids)
•   They function as hormones, transport proteins, structured proteins and receptors.
•   The blood group antigens contain glycoproteins, which also play an important role in blood grouping.
•   They are also present in egg albumin.
•   Glycoproteins are integral components of plasma membrane.
•   Glycoprotein and glycolipids have a structural role in the extracellular matrix of animals and bacterial cell wall.
✓ Glycolipids (Carbohydrate + Lipid)
•   These are lipids attached with a carbohydrate through glycosidic bond.
•   Glycolipids are complex lipids containing one or more simple sugars in connection with long fatty acids or
    alcohol.
•   Glycolipids are present in white matter of brain and myelin sheath of nerve fibres and chloroplast membrane.
•   They are also integral structural components of plasma membrane.
✓ Lipoproteins (Lipid+ Protein)
•   Lipoprotein formed by combination of lipids and proteins.
•   It is basic structural framework of all types of membranes in the cells.
•   They occur in milk, blood, cell nucleus, egg yolk membrane and chloroplasts of plants.
✓ Nucleoproteins (Nucleic acid + Protein)
• Nucleic acids have special affinity for basic proteins. They are combined together to form nucleoproteins.
• They are present in ribosomes.
• The nucleohistones (histone protein+nucleic acid) are present in chromosomes.
• They play an important role in regulation of gene expression.
• These are slightly acidic and soluble in water.
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➢ Shortlisting
•  Approximately 25 elements bio elements. Humans have 16 of them. Out of which 6 are major.
•  These may be organic or inorganic.
•  Proteins are the most abundant organic compounds while nucleic acids are the most essential
•  about 20 percent water in bone cells and 85 percent (FTB = 85 to 90%) in brain cells.
•  Hydrogen bonding is responsible for exceptional thermodynamic properties of water.
•  The specific heat of vaporization of water is 574 kcal/kg..
•  The specific heat capacity of water is 4.184 J/g°C or 1 cal/g°C.
•  carbohydrates are defined as “polyhydroxy aldehydes or ketones, or complex substances which on
   hydrolysis yield polyhydroxy aldehyde or ketone subunits.”
• They are classified into monosaccharides (having one monomer), oligosaccharides (having 3 to 7 monomers),
   polysaccharides (having 1000s of units).
• Enantiomers: These are mirror images of each other, differing in configuration at every chiral center (e.g., D-
   glucose and L-glucose).
• Diastereoisomers: Non-mirror image isomers differing in configuration at one or more (but not all) chiral
   centers (e.g., D-glucose and D-mannose).
• Epimers: A subtype of diastereoisomers differing in configuration at only one specific chiral center (e.g., D-
   glucose and D-galactose).
• Anomers: Isomers that differ at the newly formed chiral center after ring closure, typically at the C-1 carbon
   (e.g., α-D-glucose and β-D-glucose).
• Our blood normally contains 0.08% glucose.
• For the synthesis of 10g of glucose 717.6 kcal of solar energy is used.
• Sucrose: Glucose + Fructose, α-1,2 glyosidic linkage
• Lactose: Galactose + Glucose, β-1,4 glyosidic linkage
• Maltose: Glucose + Glucose, α-1,4 glyosidic linkage
Polysaccharides
• Starch: Glucose, α-1,4 and α-1,6 glyosidic linkages
• Cellulose: Glucose, β-1,4 glyosidic linkage
• Glycogen: Glucose, α-1,4 and α-1,6 glyosidic linkages
• Chitin: N-acetylglucosamine, β-1,4 glyosidic linkage
• About 170 types of amino acids have been found to occur in cells and tissues.
• Most of the proteins are however, made of 20 types of amino acids.
• Insulin is composed of 51 amino acids(49 peptide linkages) in two chains. One of the chains had 21 amino
   acids and the other had 30 amino acids
• Similarly, Haemoglobin is composed of 574 amino acids (570 peptide linkages) in four chains, two alpha and
   two beta chains. Each alpha chain contains 141 amino acids, while each beta chain contains 146 amino acids
• α-helix 3.6 amino acids in each turn.
• Primary structure: Comprises the sequence of amino acids linked by peptide bonds.
• Secondary structure: Includes α-helices and β-sheets formed through hydrogen bonds.
• Tertiary structure: Refers to three-dimensional folding driven by side chain interactions, involving disulfide
   bonds, ionic bonds, hydrogen bonds, and hydrophobic interactions.
• Quaternary structure: Represents the assembly of multiple polypeptide chains, connected by the same types
   of bonds as found in the tertiary structure — disulfide, ionic, hydrogen, and hydrophobic interactions.
• Sickle cell Hb shows only one difference from normal Hb i.e., glutamic acid is replaced by valine at position
   number six in both β-chains.
• The most abundant protein:
    1. Earth = rubisco
    2. Human body = collagen type (I)
    3. Blood = albumin
• Lipids classes:
• Acylglycerols: Glycerol + fatty acids; triacylglycerols are most abundant.
• Waxes: Long-chain esters; melting point is high, e.g., beeswax.
• Phospholipids: Amphiphilic lipids; form cell membranes.
• Glycolipids: Lipid + carbohydrate; present in membranes.
• Terpenoids: Isoprene polymers; C5H8 units, e.g., vitamin A.
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•   Steroids: Four-ring structure; includes cholesterol, hormones. 17 C
•   Prostaglandins: Arachidonic acid derivatives; 20-carbon structure.
•   Nucleic acids were first isolated (in 1869) by a Swiss physician, Fredrick miescher from the nuclei of pus cells
    (white blood cells) and sperm of salmon fish.
•   Nucleotide: Consists of a phosphate group, a sugar, and a nitrogenous base.
•   Nucleoside: Contains only a sugar and a nitrogenous base, without the phosphate group.
•   In polynucleotides there is phosphodiester linkage(C-O-P-O-C) between consecutive nucleotides.
•   Glycolipids: Lipid + carbohydrate; function in cell recognition and signaling.
•   Lipoproteins: Lipid + protein; transport lipids like cholesterol and triglycerides in blood.
•   Glycoproteins: Protein + carbohydrate; involved in immune response and intercellular communication.
•   Nucleoproteins: Protein + nucleic acid; key roles in genetic material organization (e.g., chromatin) and protein
    synthesis (e.g., ribosomes).
                                             Carbohydrates
11. A biochemical test used for detection of reducing sugars is:
A. Biuret test                 B. Benedict test             C. Spot test                     D. Iodine test
12. All of the following elements are found in all carbohydrates except:
A. Carbon                      B. Hydrogen                  C. Nitrogen                      D. Oxygen
13. Ratio of hydrogen and oxygen in carbohydrates is:
A. 1:1                         B. 2:2                       C. 1:2                           D. 2:1
14. General formula of carbohydrates is:
A. Cn(H2O)n                    B. (CH2O)n                   C. Cx(H2O)y                      D. Cn(H2O)n-1
15. These are primary products of photosynthesis:
A. Carbohydrates               B. Proteins                  C. Lipids                        D. Nucleic acids
16. It is not true for carbohydrates:
A. Carbohydrates are used in synthesis of lipids
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B. Carbohydrates are less soluble than fats in water
C. Carbohydrates form a component of nucleic acids
D. Carbohydrates are utilized in the synthesis of amino acids
17. It is not a carbohydrate:
A. Starch                      B. Glycogen                     C. Chitin                      D. Cutin
18. Most of the energy from glucose is released by breakdown of:
A. C—C                         B. C—N                          C. C—H                         D. C—OH
19. Cn(H2O)n is not applicable on:
A. Glucose                     B. Fructose                     C. Deoxyribose                 D. Ribose
20. The reducing sugars are so called because they can ____ electron/s:
A. Donate                      B. Gain                         C. Share                       D. Excite
21. All of the following are polymers of glucose except:
A. Glycogen                    B. Cellulose                    C. Amylase                     D. Amylopectin
22. Glycosidic bond cannot be found in:
A. Glucose                     B. Cellulose                    C. Glycogen                    D. Lactose
23. The covalent bond between two monosaccharides is called:
A. Peptide Linkage            B. Glucosidic linkage           C. Glycosidic linkage D. Ester linkage
24. Most familiar disaccharide is:
A. Maltose                     B. Lactose                      C. Sucrose                     D. Cellobiose
25. An important sugar occurring only in animals is:
A. Glucose                     B. Lactose                      C. Sucrose                     D. Fructose
26. Hydrolysis of which of the following would yield only glucose?
A. Lactose                     B. Maltose                      C. Cellulose                   D. Cellulase
27. Structural polysaccharides include:
A. Cellulose, Hemicellulose, Chitin                            C. Cellulose, Starch, Glycogen
B. Cellulose, Starch, Chitin                                   D. Cellulose, Glycogen, Chitin
28. It is an example of polysaccharide that is soluble in hot water:
A. Amylose                     B. Glycogen                     C. Cellulose                   D. Amylopectin
29. Most abundant carbohydrate in nature is:
A. Starch                      B. Glycogen                     C. Hemicellulose               D. Cellulose
30. Type of glycosidic linkage present in cellulose is:
A. α-1, 4                      B. β-1, 4                       C. α-1, 4 and α-1, 6           D. β-1, 4 and β-1, 6
                                                   Proteins
31. Primary structure of a protein molecule does not comprise:
A. Number of amino acids                                     C. Size of protein molecule
B. Sequence of amino acids                                   D. Shape of protein molecule
32. All proteins in living organism always show following structural levels:
A. Primary & secondary structure                             C. Tertiary & quaternary structure
B. Secondary & tertiary structure                            D. Secondary & quaternary structure
33. In quaternary structure, polypeptide chains are aggregated and held together by all of the following except:
A. Hydrophobic interactions B. Glycosidic linkages          C. Hydrogen bond        D. Ionic bond
34. It is an example of globular protein:
A. Myosin                       B. Fibrin                    C. Fibrinogen                   D. Keratin
35. An amino acid molecule has the following structure... Which two of the groups combine to form a peptide
    link?
                                                   Lipids
41. Chemical compounds that are defined on base of physical properties are:
A. Carbohydrates               B. Proteins                     C. Lipids                D. Nucleic acids
42. Lipids store energy due to higher proportion of:
A. C—C bonds                   B. C—O bonds                    C. C—H bonds             D. C—N bonds
43. This is an example of conjugated molecule of lipid:
A. Acylglycerol                B. Phospholipid                 C. Glycoprotein          D. Glycolipid
44. Most important components of triglycerides are:
A. Glycerols                   B. Fatty acids                  C. Ketones               D. Isoprenoid
45. Functional group of fatty acid is:
A. –CH₃                        B. –OH                          C. –CHO                  D. –COOH
46. Which characteristics are applicable to all fats and oils?
  FATS                                                      OILS
  I) Saturated fat acids                                    Unsaturated fat acids
  II) Solid at room temperature                             Liquid at room temperature
  III) Can be crystalized                                   Cannot be crystallized
  IV) Obtained from animals                                 Obtained from plants
A. I & II                      B. I & III                      C. I, II & III           D. I, II, III & IV
47. Saturated fatty acids have C-C double bonds:
A. 0                           B. 2                            C. 1                     D. 3
48. All of the following nitrogenous bases are found in phospholipids except:
A. Choline                     B. Cytosine                     C. Ethanolamine          D. Serine
49. Fatty acids are found in all of the following except:
A. Acylglycerols               B. Phospholipids                C. Terpenoids            D. Waxes
50. Formation through condensation of which of the following is not associated with release of water:
A. Amylose                     B. mRNA                         C. Fibrin                D. Carotenoid
53. In a typical nucleotide the nitrogenous base is attached to ______ carbon of pentose sugar:
A. C-1                          B. C-5                       C. C-3                          D. C-6
54. Phosphodiester bond is formed between:
A. Two phosphate groups                                      C. One phosphate & two hydroxyl groups
B. Two phosphates & one hydroxyl group                       D. Two phosphate & two hydroxyl groups
55. All of the following are examples of dinucleotides except:
A. ADP                          B. NAD                       C. NADP                         D. FAD
56. It is the major proportion of RNA in the cell:
A. mRNA                         B. tRNA                      C. rRNA                         D. rDNA
57. Messenger RNA carries the genetic information from:
A. Nucleus to nucleolus B. Nucleolus to ribosome C. DNA to tRNA D. DNA to ribosome
58. Which one is correct about the following diagram?
A. It is a nucleotide                                        C. It is used to form DNA
B. It contains pyrimidine nitrogen                           D. It is used to form RNA
59. Conjugated molecules are of ______ significance:
A. Structural significance only                              C. Structural and functional significance
B. Functional significance only                              D. Has no structural and functional role
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60. Which of the following conjugated molecule is incorrectly matched?
A. Lipo-proteins ------- cell membrane B. Glyco-proteins ------- cell surface antigens/ receptors
C. Glyco-lipids ------- cell wall              D. Nucleic acids ------- chromosomes
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Q.33           B   Glycosidic linkages are for carbohydrates, not proteins.
Q.34           C   Fibroin is silk protein.
                   Fibrinogen is globular while fibrin is fibrous.
Q.35           B
Q.52 D
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Q.53           A
Q.54 C
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