4Biomolecules

📚
INTRODUCTION
Biomolecules: Molecules \(organic/inorganic\) present in living organisms
Cellular Pool:
Definition: Collection of biomolecules in cells
Nature: Crystallocolloid
Contents:

Table 1: Cellular pool components

Type
Examples
Organic
Carbohydrate, lipid, protein
Inorganic
Water, minerals, salts
📚
ORGANIC COMPOUNDS
📖
Carbohydrate
Introduction:
  • \(C,H,O\) compound → \(C_n(H_2O)_n\) → hydrate of carbon
  • Ratio often → \(C:H:O = 1:2:1\)
  • Nature’s most abundant organic substance
  • Modern definition → optically active polyhydroxy aldehyde/ketone → monosaccharides on hydrolysis
  • Major energy source → glucose, fructose
Key Terms:
table:
    Classification:
    Taste + Structure + Solubility:
    table:
      Reducing Nature:
      table:
        Hydrolysis:
        Monosaccharides / Simple Sugar:
        Carbonyl Group:
        table:
          Carbon Number:
          table:
            Oligosaccharides:
            Disaccharides:
            1. Maltose
            2. Sucrose
            3. Lactose
            Other:
            1. Trisaccharides
            2. Tetrasaccharides
            Polysaccharides:
            1. Starch
            2. Glycogen
            3. Cellulose
            Important Carbohydrates:
            table:
              Honey: Mainly fructose \(\approx 38\%\) + glucose \(\approx 32\%\)
              Functions:
              • Energy source
              • Storage form → glycogen/starch
              • Structural form → cellulose
              📖
              Lipid
              Introduction:
              • Biological molecules → water insoluble
              • Soluble in non-polar organic solvents → chloroform, benzene
              • Not polymers
              • Heterogeneous group → \(C,H,O\)
              • Oxygen atoms << carbon atoms
              • True lipids = esters of fatty acids + alcohol
              Ester Formation: \(RCOOH + R'OH \rightarrow RCOOR' + H_2O\)
              Fatty Acids:
              Definition: Large molecules with acidic group → \(R-COOH\)
              Saturation:

              Table 1: Saturated vs Unsaturated fatty acids

              Feature
              Saturated fatty acids
              Unsaturated fatty acids
              Double bond
              Absent
              One/more present
              Melting point
              Higher
              Lower
              Health note
              Healthy fats
              Examples
              Palmitic acid \(16C\), stearic acid \(18C\)
              Oleic acid → 1 double bond; linoleic acid → 2 double bonds; linolenic acid → 3 double bonds
              Iodine value = degree of unsaturation of oils/fats
              Essentiality:

              Table 1: Essential fatty acids

              Type
              Examples / Note
              Essential fatty acids
              Linoleic acid, linolenic acid, arachidonic acid
              Deficiency
              Toad skin / phrynoderma
              Non-essential fatty acids
              Synthesized in body
              Major Categories:
              Simple Lipids:
              Definition: Esters of fatty acids + alcohol
              Types:
              Fats:
              Definition: Fatty acids + glycerol; triglycerides
              Glycerides:

              Table 1: Glycerides

              Type
              Composition
              Water released
              Monoglyceride
              1 glycerol + 1 fatty acid
              \(H_2O\)
              Diglyceride
              1 glycerol + 2 fatty acids
              \(2H_2O\)
              Triglyceride
              1 glycerol + 3 fatty acids
              \(3H_2O\)
              General Reaction: \(Glycerol + 3RCOOH \rightarrow Triglyceride + 3H_2O\)
              Oils: Fats rich in unsaturated fatty acids
              Waxes:
              • Long-chain fatty acids + long-chain alcohols other than glycerol
              • Water insoluble; soluble in benzene/light petroleum
              • Protective agent → moisture penetration ↓
              • Candles → paraffin wax + higher fatty acids
              • Moisture barrier + heat insulator
              Fats vs Oils:

              Table 1: Fats vs Oils

              Feature
              Fats
              Oils
              Fatty acid
              Rich in saturated FA
              Rich in unsaturated FA
              Room temperature
              Solid/semi-solid
              Liquid
              Source
              Animals only
              All plants + some animals
              Examples
              Vanaspati ghee, margarine
              Sunflower oil, mustard oil
              Compound / Complex Lipids:
              Definition: Simple lipid + other compound

              Table 1: Compound lipids

              Type
              Composition
              Special point
              Glycolipid
              Carbohydrate + lipid
              Phospholipid
              Phosphoric acid + lipid
              Cell membrane + intracellular membrane; lung surfactant prevents collapse
              Lipoprotein
              Protein + lipid
              Derived Lipids:
              Definition: Lipid derivatives
              Important Example:
              Steroids:
              • Fused hydrocarbon rings + long hydrocarbon chain
              • Cholesterol → animal fat
              • Phytosterol → plant fat
              • Diosgenin → antifertility pills
              • Steroid hormones → corticoids, testosterone, oestrogen, progesterone
              Special Points:
              • Lipids ≠ polymers
              • All lipids ≠ fats; e.g., steroids = lipid but not fat
              • Superheated steam hydrolysis → glycerol + fatty acid
              • Saponification = alkaline hydrolysis of fat
              • \(Fat + NaOH \rightarrow Soap + Glycerol\)
              • Soap = sodium/potassium salt of higher fatty acid
              • Sodium soap → hard soap → washing/cleaning
              • Potassium soap → bathing
              • Chylomicrons = lipids
              • Rancidification = spoilage of fats/oils on long storage
              📖
              Protein
              Introduction:
              • Complex natural compounds
              • Many \(\alpha\)-amino acids + peptide linkages
              • Basis of structure + function of life
              • Nitrogenous organic compounds of protoplasm
              • Animals > plants in protein content
              • Hydrophilic high-polymer colloids
              • Optically active → chiral centers at \(\alpha\)-position
              Amino Acids:
              Definition: Amino-substituted acids → amino \((-NH_2)\) + carboxyl \((-COOH)\) groups
              Nature:
              • Amphoteric
              • Slightly acidic pH
              • Building blocks of proteins
              General Structure:

              Table 1: \(\alpha\)-amino acid components

              Central atom
              Attached groups
              \(\alpha\)-carbon
              \(-NH_3^+\), \(-COO^-\), \(H\), variable side chain \((-R)\)
              Zwitter Ion:
              Definition: Proton shift: carboxyl group → amino group → dipolar ion
              Charge: + and - charge together
              Isoelectric Point:
              • pH where amino acid does not migrate in electric field
              • Net charge = 0
              • Constant for each amino acid
              • Minimum solubility
              • Dipolar ion concentration maximum
              20 Amino Acids:

              Table 1: Amino acids + one-letter symbols

              Amino acid
              Symbol
              Special point
              Alanine
              A
              Arginine
              R
              Semi-indispensable
              Asparagine
              N
              Aspartic acid
              D
              Cysteine
              C
              Sulphur-containing; deficient in pulses
              Glutamine
              Q
              Glutamic acid
              E
              Glycine
              G
              Simplest; lowest molecular weight; no asymmetric carbon; no optical isomerism
              Histidine
              H
              Blood buffer in haemoglobin; semi-indispensable
              Isoleucine
              I
              Essential
              Leucine
              L
              Essential
              Lysine
              K
              Essential; deficient in cereals
              Methionine
              M
              Sulphur-containing; deficient in pulses
              Phenylalanine
              F
              Essential
              Proline
              P
              Cyclic; imino acid; no free amino + carboxyl group
              Serine
              S
              Threonine
              T
              Essential; deficient in cereals
              Tryptophan
              W
              Most complex; indole ring; deficient in maize
              Tyrosine
              Y
              Precursor: dopamine, melanin, thyroxine, adrenaline, noradrenaline
              Valine
              V
              Essential
              Essentiality:

              Table 1: Essential vs Non-essential amino acids

              Non-essential
              Essential
              Alanine
              Arginine
              Asparagine
              Histidine
              Aspartic acid
              Isoleucine
              Cysteine
              Leucine
              Glutamine
              Lysine
              Glutamic acid
              Methionine
              Glycine
              Phenylalanine
              Proline
              Threonine
              Serine
              Tryptophan
              Tyrosine
              Valine
              Arginine + histidine = semi-indispensable; not essential in adult organisms
              Colour Reactions:

              Table 1: Protein colour tests

              Test
              Reaction
              Indicates / Note
              Biuret test
              Protein + 10% NaOH + few drops \(CuSO_4\) → reddish violet
              Peptide linkage; colour ∝ peptide bonds
              Millon’s reaction
              Protein + Millon’s reagent → white ppt; heat → brick red
              Phenol group; tyrosine-containing proteins
              Ninhydrin reaction
              Protein + pyridine solution of ninhydrin → deep blue to violet pink
              Amino acids/proteins
              Xanthoproteic test
              Protein + \(HNO_3\) + heat → yellow
              Aromatic amino acids
              Denaturation:
              • Agents → heat, UV radiation, solvents, reagents
              • Change may be reversible/irreversible
              • Most readily near isoelectric point
              • Primary structure intact; 3D structure destroyed
              • Reversal → renaturation / refolding
              • Example → boiled egg = irreversible denaturation
              • Globular protein → fibrous protein
              Classification:
              By Hydrolysis Product:

              Table 1: Simple, conjugated and derived proteins

              Type
              Hydrolysis product
              Examples
              Simple proteins
              Only \(\alpha\)-amino acids
              Albumins, albuminoids, globulins, glutelins
              Conjugated proteins
              \(\alpha\)-amino acids + non-protein substance
              Nucleoproteins, glycoproteins, phosphoproteins, haemoglobins
              Derived proteins
              Intermediate hydrolysis products of proteins
              Peptides, proteoses, peptones
              By Function:

              Table 1: Functional classification of proteins

              Class
              Examples
              Enzymes
              Ribonuclease, amylase, trypsin, catalase
              Regulatory proteins
              Insulin, growth hormone, parathormone
              Storage proteins
              Ovalbumin, casein, ferritin, glutelins, globulins
              Contractile + motile
              Actin, myosin, tubulin, kinesin
              Structural proteins
              Collagen, \(\alpha\)-keratin, elastin, chondrin, ossein, fibroin
              Protective proteins
              Immunoglobulin, thrombin, fibrinogen
              Transport proteins
              Haemoglobin, myoglobin, albumin
              Albumins bind ligands and transport them
              By Shape:

              Table 1: Fibrous vs Globular proteins

              Feature
              Fibrous proteins
              Globular proteins
              Shape
              Thread-like; side-by-side fibres
              Folded compact units; often spheroidal
              Stabilizing force
              Hydrogen bonds
              Various intramolecular interactions
              Solubility
              Insoluble in water; soluble in concentrated acids/alkalies
              Soluble in water, dilute acids/alkalies
              Examples
              Collagen, keratin of hair/nails, myosin of muscles
              Insulin, haemoglobin, myoglobin, albumin, actin, troponin
              Structure:

              Table 1: Levels of protein structure

              Level
              Meaning
              Bonds / Key points
              Primary
              Linear amino acid sequence
              Determines protein function
              Secondary
              Shape of individual polypeptide chain
              Hydrogen bonds between \(-C=O\) and \(-NH\); \(\alpha\)-helix + \(\beta\)-sheet
              Tertiary
              3D compact folding of polypeptide chain
              H-bonds, Van der Waals interactions, disulphide bonds, electrostatic bonds, hydrophobic effect
              Quaternary
              Inter-relation between >2 polypeptide chains
              Subunit arrangement
              Secondary Details:
              • \(\alpha\)-helix → single amino acid chain coiled spirally; H-bond between 1st and 4th amino acids
              • \(\beta\)-pleated sheet → two/more polypeptide chains; parallel or antiparallel
              MCQ Point: Primary bonds for secondary + tertiary structure → H-bond
              Functions:
              • Energy source
              • Body defense → immunoglobulins
              • Muscle contraction → actin + myosin
              • Structural component → collagen, keratin; hair, nail, bone
              • Catalysis → enzymes
              • Chemical messengers → insulin, GH, oxytocin
              • Transport → haemoglobin, myoglobin, albumin
              📖
              Vitamins
              Listed only
              📚
              INORGANIC COMPOUNDS
              📖
              Water
              Listed only
              📖
              Mineral
              Listed only
              📖
              Salts
              Listed only
              Q1.
              The disaccharide present in milk is  [IOM 2008]
              📅IOM 2008
              Q2.
              The enzyme used during fermentation carbohydrate to CO2, and alcohol is [IOM 2003, MOE 2064]
              📅IOM 2003, MOE 2064
              Q3.
              Which is not a carbohydrate? [BPKIHS ]
              📅BPKIHS
              Q4.
              Which of the following is not a polysaccharide [BPKIHS]
              📅BPKIHS
              Q5.
              Which of the following is a polysaccharide [I.E.]
              📅I.E.
              Q6.
              Hydrolysis of table sugar produces [MOE - Curriculum]
              📅MOE - Curriculum
              Q7.
              Which of the following base is purine [MOE 2065]
              📅MOE 2065
              Q8.
              Which of the following is an aldohexose? [I.E.]
              📅I.E.
              Q9.
              Molisch test is given by  [I.E.]
              📅I.E.
              Q10.
              Maltose on hydrolysis produces [BPKIHS]
              📅BPKIHS
              Q11.
              Which of the following cannot form peptide bond on polypeptide chain? [IOM]
              📅IOM
              Q12.
              Amino acids usually exist in the form of zwitter ions. This means that they consist of [IOM 1999]
              📅IOM 1999
              Q13.
              Isoelectric point is the pH at which [BPKIHS 2000]
              📅BPKIHS 2000
              Q14.
              The enzyme pepsin hydrolyses [BPKIΗΑ]
              📅BPKIΗΑ
              Q15.
              Presence of peptide bond is the characteristic features of [MOE 2065)
              📅MOE 2065)
              Q16.
              Lipids consist up of  [KU 2008]
              📅KU 2008
              Q17.
              Enzyme is a [I.E. 2003]
              📅I.E. 2003
              Q18.
              DNA multiplication is called [MOE]
              📅MOE
              Q19.
              The purine base present in RNA is
              Q20.
              Glycolipids and Phospholipids are  [BPKIHS/ KU/ MOE]
              📅BPKIHS/ KU/ MOE
              Q21.
              Milk sugar is [MOE/IOM/KU]
              📅MOE/IOM/KU
              Q22.
              Starch is hydrolyzed to maltose by an enzyme [MOE)
              📅MOE)
              Q23.
              Which of the following is the sweetest sugar?[BPKIHS
              📅BPKIHS
              Q24.
              Hydrolysis of sucrose is called  [MOE]
              📅MOE
              Q25.
              Alkaline hydrolysis of esters is known as [MOE, IOM, BPKIHS 2005]
              📅MOE, IOM, BPKIHS 2005
              Q26.
              Which of the following enzymes hydrolyses triglycerides to fatty acid and glycerol? [KU]
              📅KU
              Q27.
              Fat is a [K.0.]
              📅K.0.
              Q28.
              Two complementary strands of DNA in a double helix are joined to each other by [IOM]
              📅IOM
              Q29.
              The main function of RNA in the body is [IOM]
              📅IOM
              Q30.
              Upon hydrolysis protein give [BPKIHS]
              📅BPKIHS
              Q31.
              Liquid fats are converted into solid fats by [BPKIHS]
              📅BPKIHS
              Q32.
              Synthetic detergents can be represented by the general formula [BPKIHS/IE]
              📅BPKIHS/IE
              Q33.
              The degree of unsaturation of fat can be determined by means of [BPKIHS]
              📅BPKIHS
              Q34.
              Fats and oil are [BPKIHS]
              📅BPKIHS
              Q35.
              Magnesium is present in  [BPKIHS]
              📅BPKIHS
              Q36.
              Which of the following metal ion play an important role in muscle contraction? [IOM]
              📅IOM
              Q37.
              Antimony compounds are used in the treatment of [IOM]
              📅IOM
              Q38.
              The cation necessary for coagulation of blood is [I.E. 2003]
              📅I.E. 2003
              Q39.
              Yeast is an important source of [BPKIHS]
              📅BPKIHS
              Q40.
              Fatty acids which must be obtained from diet are [BPKIHS 2005]
              📅BPKIHS 2005
              Q41.
              The component of blood which maintain osmotic pressure is [BPKIHS 2005]
              📅BPKIHS 2005
              Q42.
              The enzyme pepsin hydrolyses [BPKIHS 2005]
              📅BPKIHS 2005
              Q43.
              DNA has which sugar in it [BPKIHS 2004]
              📅BPKIHS 2004
              Q44.
              Maximum energy is produced by the oxidation of [BPKIHS 2005
              📅BPKIHS 2005
              Q45.
              Nucleic acids are polymers of  [IOM 2011]
              📅IOM 2011
              Q46.
              Every carbohydrate is  [IOM 2010]
              📅IOM 2010
              Q47.
              Almost all pharmaceutical products produced by DNA technology [MOE 2013 Magh - 6]
              📅MOE 2013 Magh - 6
              Q48.
              Simplest amino acid  [BPKIHS - 2016]
              📅BPKIHS - 2016
              Q49.
              The common point among enzymes, hormone and vitamin in our body is [BPKIHS - 2016]
              📅BPKIHS - 2016
              Q50.
              The building block of protein is  [BPKIHS - 2016)
              📅BPKIHS - 2016)
              Q51.
              α-helical structure of protein is stabilized by  [BPKIHS - 2014]
              📅BPKIHS - 2014
              Q52.
              Which of the following is present in least proportion in cell membrane? [BPKIHS - 2011]
              📅BPKIHS - 2011
              Q53.
              Corn is immersed in boiling water. It is then cooled and solution becomes sweet. It is due to [BPKIHS - 2011]
              📅BPKIHS - 2011
              Q54.
              Which of the following is a co enzymes? [BPKIHS - 2010]
              📅BPKIHS - 2010
              Q55.
              Starch is polymer of  BPKIHS - 2010
              📅BPKIHS - 2010
              Q56.
              All are essential amino acids except [BPKIHS - 2010]
              📅BPKIHS - 2010
              Q57.
              Cane sugar on hydrolysis gives  [IOM-2014]
              📅IOM-2014
              Q58.
              Which component is most dispersed in a cell? [IOM-2012)
              📅IOM-2012)