← Biology β€” Std 11
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Biomolecules

Ch. 6Std 11

Easy Overview

When you eat a meal, what happens to that food inside your body? It gets broken down into molecules β€” tiny particles that your cells can actually use. And your body itself is made of these same kinds of molecules. This chapter is about the chemical building blocks of life: the biomolecules. Carbohydrates, proteins, lipids, and nucleic acids β€” plus the enzymes that make everything work and the vitamins that keep everything running smoothly. Let us start with carbohydrates. The name comes from 'hydrate of carbon' because these molecules have a ratio of roughly one carbon to one water molecule (CHβ‚‚O)β‚™. Carbs are the most abundant biomolecules on Earth. Their primary function is to provide energy, but they also serve structural roles. Simple carbohydrates are monosaccharides β€” single sugar units like glucose, fructose, and galactose. Glucose is the most important monosaccharide because it is the primary fuel for cellular respiration. Two monosaccharides joined together make a disaccharide β€” sucrose (table sugar), lactose (milk sugar), and maltose. Complex carbohydrates (polysaccharides) are long chains of monosaccharides: starch (energy storage in plants), glycogen (energy storage in animals), and cellulose (structural component of plant cell walls). Cellulose is the most abundant organic molecule on Earth β€” and humans cannot digest it because we lack the enzyme cellulase. Proteins are the workhorses of the cell. They do almost everything: catalyze reactions (enzymes), provide structure (collagen in skin and bones), transport molecules (hemoglobin carries oxygen), defend the body (antibodies are proteins), regulate processes (insulin regulates blood sugar), and enable movement (actin and myosin in muscles). Proteins are made of amino acids linked together by peptide bonds. There are 20 standard amino acids, of which 9 are essential β€” they must come from your diet because your body cannot make them. Each amino acid has a central carbon bonded to an amino group (-NHβ‚‚), a carboxyl group (-COOH), a hydrogen atom, and a variable R group that gives each amino acid its unique properties. A protein's function depends entirely on its structure β€” from the sequence of amino acids (primary structure), how the chain folds locally (secondary structure β€” alpha helices and beta sheets), the overall three-dimensional shape (tertiary structure), and how multiple chains assemble (quaternary structure). If the shape changes, the protein stops working β€” this is what happens when you cook an egg; the proteins denature and the egg white turns solid. Lipids are a diverse group of hydrophobic molecules. Fats and oils store energy β€” fat contains about twice the calories per gram as carbohydrates. Phospholipids make up cell membranes. Steroids like cholesterol and hormones regulate body processes. Nucleic acids carry genetic information. DNA holds the genetic blueprint; RNA helps execute it. Both are made of nucleotides. And then there are enzymes β€” biological catalysts that speed up reactions without being consumed. Almost all enzymes are proteins. They work by lowering the activation energy of reactions. Their activity is affected by temperature, pH, and inhibitors. Vitamins and minerals are essential micronutrients that often act as helpers for enzymes. Understanding biomolecules is understanding the chemistry of life itself.

What are Biomolecules?

Biomolecules are organic molecules produced by living organisms. The four major classes are carbohydrates, proteins, lipids, and nucleic acids. In addition, there are vitamins, minerals, and water. Biomolecules can be classified as micromolecules (small molecules like monosaccharides, amino acids, nucleotides, fatty acids) and macromolecules (large polymers like polysaccharides, proteins, and nucleic acids built from micromolecule subunits). Primary metabolites are directly involved in normal growth, development, and reproduction β€” these include sugars, amino acids, nucleotides, and vitamins. Secondary metabolites have ecological functions β€” they are not essential for growth but help the organism survive: alkaloids (nicotine, morphine, quinine β€” often toxic to herbivores), terpenoids (menthol, camphor, rubber), phenolics (tannins, flavonoids β€” antioxidants and defense), and antibiotics (penicillin). Living organisms are essentially complex chemical systems, and biomolecules are the components that make these systems work. Every life process β€” from muscle contraction to thought to digestion β€” is ultimately a series of chemical reactions involving biomolecules.

Carbohydrates β€” Classification and Structure

Carbohydrates are compounds with the general formula Cβ‚™(Hβ‚‚O)β‚˜ β€” hydrates of carbon. They are classified based on the number of sugar units. Monosaccharides (1 unit) are simple sugars that cannot be hydrolyzed further. They have 3-7 carbon atoms: trioses (glyceraldehyde β€” 3C, important in glycolysis), pentoses (ribose Cβ‚…H₁₀Oβ‚… β€” in RNA; deoxyribose Cβ‚…H₁₀Oβ‚„ β€” in DNA), and hexoses (glucose C₆H₁₂O₆ β€” the primary fuel; fructose β€” in fruits; galactose β€” in milk). Glucose exists in two ring forms: Ξ±-glucose and Ξ²-glucose, which differ in the orientation of the -OH group on carbon 1. This small difference is crucial β€” starch is made of Ξ±-glucose, while cellulose is made of Ξ²-glucose. Disaccharides (2 units) are formed by a glycosidic bond between two monosaccharides with the removal of a water molecule (condensation reaction). Sucrose = glucose + fructose (table sugar from sugarcane/beet). Lactose = glucose + galactose (milk sugar). Maltose = glucose + glucose (malt sugar, from starch digestion). Polysaccharides (many units) are long chains: starch (amylose β€” unbranched, amylopectin β€” branched; energy storage in plants), glycogen (highly branched energy storage in animals, stored in liver and muscles), cellulose (Ξ²-1,4 linked glucose, structural in plant cell walls β€” the most abundant organic molecule on Earth), and chitin (modified glucose units, structural in arthropod exoskeletons and fungal cell walls).

Proteins β€” Structure and Functions

Proteins are polymers of amino acids linked by peptide bonds (a covalent bond between the carboxyl group of one amino acid and the amino group of another, with the release of water). The 20 standard amino acids have a common structure: a central Ξ±-carbon bonded to an amino group (-NHβ‚‚), a carboxyl group (-COOH), a hydrogen atom, and a variable R group (side chain) that determines the amino acid's properties. Nine amino acids are essential and must come from diet: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine. Proteins have four levels of structure. Primary structure is the linear sequence of amino acids β€” determined by the gene. Secondary structure is local folding into Ξ±-helices (right-handed spiral stabilized by hydrogen bonds between every 4th amino acid) and Ξ²-pleated sheets (zigzag chains held together by hydrogen bonds between adjacent segments). Tertiary structure is the overall 3D shape of a single polypeptide chain, stabilized by disulfide bridges (covalent bonds between cysteine residues), hydrophobic interactions, ionic bonds, and hydrogen bonds. Quaternary structure is the assembly of multiple polypeptide chains into a functional protein β€” hemoglobin has four subunits (two Ξ± and two Ξ² chains), collagen has three chains wound together. If a protein loses its structure (denatures), it stops functioning β€” this happens when you cook an egg, when you have a fever, or when pH changes drastically.

Lipids β€” Fats, Oils, and Membrane Components

Lipids are a heterogeneous group of hydrophobic (water-fearing) molecules β€” they do not dissolve in water but dissolve in organic solvents like chloroform, ether, and benzene. Simple lipids are esters of fatty acids with glycerol. Fats (triglycerides) consist of one glycerol molecule bonded to three fatty acid chains. Saturated fatty acids (palmitic acid C₁₆, stearic acid Cβ‚β‚ˆ) have no double bonds between carbons β€” the carbon chain is fully 'saturated' with hydrogen. They are solid at room temperature (butter, ghee, animal fat). Unsaturated fatty acids (oleic acid Cβ‚β‚ˆ:₁, linoleic acid Cβ‚β‚ˆ:β‚‚) have one or more double bonds, which create kinks in the chain preventing tight packing. They are liquid at room temperature (oils from plants β€” olive, sunflower, mustard). Compound lipids include phospholipids β€” similar to triglycerides but with one fatty acid replaced by a phosphate group bonded to a nitrogen-containing molecule. The phosphate head is hydrophilic (water-loving) and the fatty acid tails are hydrophobic β€” this amphipathic nature makes phospholipids perfect for forming cell membranes. Lipoproteins (lipid + protein) transport lipids in the blood. Derived lipids include steroids (four fused carbon rings β€” cholesterol, testosterone, estrogen, cortisol β€” all derived from cholesterol), terpenes (carotenoids, vitamin A, rubber), and waxes (long-chain fatty acids + long-chain alcohols β€” waterproof coatings on leaves, feathers, and insect exoskeletons). Cholesterol is a component of animal cell membranes and a precursor for steroid hormones, vitamin D, and bile salts.

Nucleic Acids β€” DNA and RNA

Nucleic acids are polymers of nucleotides that store and transmit genetic information. Each nucleotide has three components: a nitrogenous base, a pentose sugar (ribose in RNA, deoxyribose in DNA), and a phosphate group. Nitrogenous bases are of two types: purines (double-ring structures β€” adenine A and guanine G) and pyrimidines (single-ring structures β€” cytosine C, thymine T in DNA only, uracil U in RNA only). DNA (deoxyribonucleic acid) is double-stranded β€” two antiparallel strands (one runs 5'β†’3', the other 3'β†’5') wound into a right-handed double helix, discovered by Watson and Crick in 1953. Base pairing is specific: A pairs with T (two hydrogen bonds), G pairs with C (three hydrogen bonds β€” stronger). This complementary base pairing is the basis for DNA replication and transcription. RNA (ribonucleic acid) is usually single-stranded, has ribose sugar instead of deoxyribose, and uses uracil instead of thymine. Types of RNA: messenger RNA (mRNA β€” carries the genetic code from DNA to ribosomes), transfer RNA (tRNA β€” brings specific amino acids to the ribosome during protein synthesis, has an anticodon and an amino acid attachment site), and ribosomal RNA (rRNA β€” a major structural and functional component of ribosomes). ATP (adenosine triphosphate) is a special nucleotide that stores and transfers energy in cells β€” it has three phosphate groups; the bond between the second and third phosphate is a high-energy bond that releases energy when broken.

Enzymes β€” Biological Catalysts

Enzymes are protein catalysts (though some RNA molecules called ribozymes also have catalytic activity) that speed up chemical reactions by lowering the activation energy β€” the minimum energy required to start a reaction. They are not consumed in the reaction β€” one enzyme molecule can catalyze thousands of reactions per second. Each enzyme is highly specific for its substrate (the molecule it acts on) β€” this specificity is due to the shape of the active site, the region where the substrate binds. The lock and key model (Fischer, 1894) suggests the active site is exactly complementary in shape to the substrate β€” like a key fitting a lock. The induced fit model (Koshland, 1958) suggests the active site is flexible and changes shape slightly when the substrate binds, like a hand fitting into a glove. Factors affecting enzyme activity: temperature (activity increases with temperature up to an optimum around 37Β°C for human enzymes, then declines as the enzyme denatures), pH (each enzyme has an optimum pH β€” pepsin works best at pH 2 in the stomach, trypsin at pH 8 in the small intestine), substrate concentration (rate increases until the enzyme is saturated β€” all active sites occupied), and enzyme concentration (rate increases proportionally if substrate is not limiting). Inhibitors decrease enzyme activity. Competitive inhibitors resemble the substrate and compete for the active site (statins inhibit cholesterol synthesis by competing with the substrate). Noncompetitive inhibitors bind elsewhere on the enzyme and change the active site shape (cyanide binds to cytochrome oxidase in the ETC, blocking respiration).

Mechanism of Enzyme Action

Enzymes lower the activation energy by providing an alternative reaction pathway. They achieve this through several mechanisms. (1) Proximity and orientation β€” enzymes bring substrates close together in the correct orientation for the reaction to occur. Instead of substrates randomly colliding in solution, the enzyme holds them in the right position. (2) Acid-base catalysis β€” amino acid side chains in the active site donate or accept protons, facilitating bond breaking and formation. For example, histidine can act as either an acid or a base depending on pH. (3) Covalent catalysis β€” the enzyme forms a temporary covalent bond with the substrate, creating an intermediate that is more reactive. (4) Metal ion catalysis β€” metal ions (Zn²⁺, Mg²⁺, Fe²⁺) help stabilize charges on intermediate molecules. The rate of an enzyme-catalyzed reaction follows Michaelis-Menten kinetics. Vmax is the maximum reaction rate when all active sites are occupied. Km (Michaelis constant) is the substrate concentration at half Vmax β€” it reflects the enzyme's affinity for the substrate. A low Km means high affinity (the enzyme reaches half-maximal rate at a low substrate concentration). The catalytic efficiency of an enzyme is measured as kcat/Km, where kcat is the turnover number (the number of substrate molecules converted per second per enzyme molecule). Some enzymes have turnover numbers of millions per second (catalase breaks down 40 million hydrogen peroxide molecules per second).

Classification of Enzymes

Enzymes are classified into six major classes by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme has a four-digit EC (Enzyme Commission) number. Oxidoreductases catalyze oxidation-reduction reactions (transfer of electrons or hydrogen atoms). Examples: dehydrogenases (lactate dehydrogenase), oxidases (cytochrome c oxidase), catalase. Transferases transfer functional groups (methyl, acyl, amino, phosphate) from one molecule to another. Examples: hexokinase (transfers phosphate to glucose), transaminases. Hydrolases catalyze hydrolysis β€” breaking bonds by adding water. Examples: lipases (break fats), proteases (break proteins), amylases (break starch), nucleases (break nucleic acids). Lyases catalyze the addition or removal of groups to form double bonds without hydrolysis or oxidation. Examples: pyruvate decarboxylase (removes COβ‚‚), aldolase (splits fructose-1,6-bisphosphate in glycolysis). Isomerases catalyze isomerization β€” rearranging atoms within a molecule. Examples: phosphoglucose isomerase (converts glucose-6-phosphate to fructose-6-phosphate in glycolysis), triose phosphate isomerase. Ligases (synthetases) catalyze the joining of two molecules using ATP energy. Examples: DNA ligase (joins DNA fragments), aminoacyl-tRNA synthetase (attaches amino acids to tRNA).

Vitamins β€” Essential Micronutrients

Vitamins are organic compounds required in small amounts for normal metabolism. They cannot be synthesized by the body in sufficient quantities and must be obtained from food. They are classified into two groups based on solubility. Fat-soluble vitamins (A, D, E, K) are absorbed with dietary fats and can be stored in the liver and adipose tissue β€” you do not need to consume them every day. Vitamin A (retinol): needed for vision (retinal is part of rhodopsin in rod cells), immune function, and epithelial cell maintenance. Deficiency causes night blindness and xerophthalmia. Sources: carrots, spinach, liver, eggs. Vitamin D (calciferol): synthesized in skin exposed to sunlight, needed for calcium absorption and bone health. Deficiency causes rickets in children (soft, bent bones) and osteomalacia in adults. Sources: sunlight, fatty fish, fortified milk. Vitamin E (tocopherol): antioxidant that protects cell membranes from free radical damage. Deficiency is rare but causes nerve damage. Sources: vegetable oils, nuts, seeds. Vitamin K (phylloquinone): needed for blood clotting (synthesis of clotting factors). Deficiency causes bleeding problems. Sources: green leafy vegetables, produced by gut bacteria. Water-soluble vitamins (B-complex and C) are not stored in significant amounts and need regular intake β€” excess is excreted in urine. B-complex includes B1 (thiamine β€” beriberi, nerve damage), B2 (riboflavin β€” skin lesions), B3 (niacin β€” pellagra with dermatitis, diarrhea, dementia), B5 (pantothenic acid β€” part of Coenzyme A), B6 (pyridoxine β€” amino acid metabolism), B7 (biotin β€” cofactor for carboxylation reactions), B9 (folic acid β€” DNA synthesis, prevents neural tube defects in newborns), B12 (cobalamin β€” red blood cell formation, nerve function β€” only from animal sources, deficiency causes pernicious anemia). Vitamin C (ascorbic acid): collagen synthesis, antioxidant, enhances iron absorption. Deficiency causes scurvy (bleeding gums, slow wound healing). Sources: citrus fruits, berries, tomatoes.

Minerals in the Body

Minerals are inorganic elements essential for body function. They are classified as macrominerals (required in amounts >100 mg/day) and trace minerals (required in smaller amounts). Macrominerals: Calcium (Ca) β€” bones and teeth, muscle contraction, nerve transmission, blood clotting. Deficiency causes osteoporosis. Sources: milk, cheese, leafy greens. Phosphorus (P) β€” bones, ATP, nucleic acids, cell membranes. Potassium (K) β€” nerve impulses, muscle contraction, fluid balance. Sodium (Na) β€” nerve impulses, fluid balance, nutrient absorption. Chlorine (Cl) β€” fluid balance, stomach acid (HCl). Magnesium (Mg) β€” enzyme cofactor (involved in over 300 reactions), muscle function, DNA synthesis. Sulfur (S) β€” component of methionine and cysteine (amino acids), in biotin and thiamine. Trace minerals: Iron (Fe) β€” hemoglobin (carries oxygen), myoglobin, cytochromes. Deficiency causes iron-deficiency anemia (fatigue, pale skin). Sources: red meat, spinach, legumes. Zinc (Zn) β€” enzyme cofactor, immune function, wound healing. Copper (Cu) β€” enzyme cofactor, iron metabolism. Iodine (I) β€” component of thyroid hormones (T3 and T4), regulates metabolism. Deficiency causes goiter (enlarged thyroid gland). Sources: iodized salt, seafood. Selenium (Se) β€” antioxidant enzyme (glutathione peroxidase). Fluorine (F) β€” strengthens tooth enamel, prevents cavities. Cobalt (Co) β€” component of vitamin B12. Minerals work as cofactors for enzymes, maintain osmotic balance, transmit nerve impulses, and provide structural components.

Water β€” The Solvent of Life

Water is the most abundant molecule in living organisms β€” about 70% of human body weight, up to 95% in jellyfish. Its unique properties make it essential for life. Water is a polar molecule β€” the oxygen atom is slightly negative and the hydrogen atoms are slightly positive. This polarity allows water to form hydrogen bonds with other water molecules and with other polar molecules. Key properties: (1) Universal solvent β€” water dissolves more substances than any other liquid because its polarity interacts with charged and polar molecules. This makes it the medium for all biochemical reactions. Nutrients, gases, and waste products are transported dissolved in water. (2) High specific heat capacity β€” water resists temperature changes because breaking hydrogen bonds requires energy. This helps organisms maintain stable internal temperatures and makes water a good thermal buffer. (3) High heat of vaporization β€” evaporating water requires a lot of energy (the hydrogen bonds must be broken). This makes sweating an effective cooling mechanism β€” as sweat evaporates, it takes heat from the body. (4) Cohesion and adhesion β€” water molecules stick to each other (cohesion) and to other surfaces (adhesion). This enables capillary action, which pulls water up narrow tubes β€” essential for water transport in plants from roots to leaves. (5) Ice is less dense than water β€” water expands when it freezes because hydrogen bonds form a crystalline structure with more space between molecules. This means ice floats, insulating the water below and allowing aquatic life to survive under ice.

Primary vs. Secondary Metabolites

Primary metabolites are directly involved in normal growth, development, and reproduction of an organism. They are produced in large quantities and are generally consistent across species. Examples include carbohydrates (glucose, starch), amino acids and proteins, nucleotides and nucleic acids, lipids (membrane phospholipids), and vitamins. Many primary metabolites are used in biotechnology and industry: ethanol from yeast fermentation (alcoholic beverages, biofuel), citric acid from Aspergillus niger (food preservative), lactic acid from Lactobacillus (yogurt, cheese), and amino acids (glutamic acid as flavor enhancer MSG). Secondary metabolites are not directly involved in growth but have ecological functions such as defense against herbivores and pathogens, attraction of pollinators, and competition with other organisms. They are typically produced in specific developmental stages or in response to stress. They are often unique to particular species or groups. Examples: alkaloids (morphine from poppy β€” painkiller, quinine from cinchona β€” antimalarial, nicotine from tobacco β€” insecticide, caffeine from coffee/tea β€” stimulant), terpenoids (menthol from mint β€” flavor, camphor β€” medicinal, rubber from Hevea trees β€” industrial), phenolics (flavonoids β€” plant pigments and antioxidants, tannins β€” anti-herbivore, lignin β€” structural), antibiotics (penicillin from Penicillium β€” antibacterial, tetracycline from Streptomyces), and pigments (anthocyanins β€” red/blue/purple in flowers and fruits, carotenoids β€” yellow/orange). Many secondary metabolites are used as medicines, flavors, fragrances, dyes, and pesticides. The study of these compounds has led to many life-saving drugs.

Key Points

  • β€’Four major biomolecules: carbohydrates, proteins, lipids, nucleic acids.
  • β€’Carbohydrates: Cβ‚™(Hβ‚‚O)β‚˜. Monosaccharides (glucose), disaccharides (sucrose), polysaccharides (starch, glycogen, cellulose).
  • β€’Glucose (C₆H₁₂O₆) is the primary fuel molecule. Starch and glycogen store energy. Cellulose is structural.
  • β€’Proteins: polymers of amino acids linked by peptide bonds. 20 standard amino acids, 9 essential.
  • β€’Four levels of protein structure: primary (sequence), secondary (Ξ±-helices, Ξ²-sheets), tertiary (3D shape), quaternary (multiple subunits).
  • β€’Lipids: hydrophobic. Fats (triglycerides), phospholipids (membranes), steroids (hormones, cholesterol).
  • β€’Saturated fats: solid at room temp, no double bonds. Unsaturated fats: liquid, have double bonds.
  • β€’Nucleic acids: DNA (double helix, A-T, G-C) and RNA (single strand, A-U, G-C). Polymers of nucleotides.
  • β€’ATP is the energy currency β€” a special nucleotide with high-energy phosphate bonds.
  • β€’Enzymes are protein catalysts that lower activation energy. Specific, reusable, regulated.
  • β€’Lock and key model and induced fit model describe enzyme-substrate binding.
  • β€’Enzyme activity affected by temperature, pH, substrate concentration, and inhibitors.
  • β€’Competitive inhibitors bind active site; noncompetitive inhibitors bind elsewhere.
  • β€’Vitamins: organic, essential in small amounts. Fat-soluble (A, D, E, K) and water-soluble (B-complex, C).
  • β€’Minerals: inorganic elements β€” Ca, P, K, Na, Fe, Zn, I, Mg, etc.
  • β€’Water: universal solvent, high specific heat, high heat of vaporization, cohesion/adhesion β€” essential for life.

Practice Questions

  • Classify carbohydrates with suitable examples for each class.
  • Describe the four levels of protein structure. Why does structure determine function?
  • Differentiate between saturated and unsaturated fatty acids. How are phospholipids different from triglycerides?
  • Explain the structure of DNA. What is complementary base pairing? Why is it important?
  • What are enzymes? Explain lock and key and induced fit models of enzyme action.
  • List the factors affecting enzyme activity and explain how each affects the reaction rate.
  • What are vitamins? Differentiate between fat-soluble and water-soluble vitamins with deficiency diseases.
  • Explain the role of water as a solvent. What unique properties make water essential for life?