Biological Macromolecules

Biological Macromolecules

Introduction

  • Biological macromolecules are large molecules essential for life, constructed from smaller organic molecules.

  • There are four major classes of biological macromolecules:

    • Carbohydrates

    • Lipids

    • Proteins

    • Nucleic Acids

  • These molecules are organic, meaning they contain carbon and may include hydrogen, oxygen, nitrogen, and other minor elements.

Dehydration Synthesis

  • Macromolecules (polymers) are formed from monomers through a covalent bond.

  • Monomers (from Greek 'mono' meaning one) are subunits or building blocks of larger molecules.

  • Polymers (from Greek 'poly' meaning many) consist of multiple monomers covalently bonded.

  • Dehydration Synthesis: This is the process of bonding two or more monomers together, releasing water as a byproduct.

Hydrolysis

  • Hydrolysis: The process by which polymers break down into monomers.

  • The terms are derived from:

    • Hydro: meaning water

    • Lysis: meaning to break apart.

  • Both dehydration synthesis and hydrolysis reactions are catalyzed by specific enzymes.

  • Dehydration synthesis requires energy to bond monomers, while hydrolysis releases energy when breaking down polymers.

Carbohydrates

Defining Carbohydrates

  • Carbohydrates are organic molecules that can be represented by the formula C<em>nH</em>2nOnC<em>nH</em>{2n}O_n (1:2:1 ratio of carbon to hydrogen to oxygen).

Monosaccharides
  • Monosaccharides are simple sugars, with glucose being the most common example.

  • The term monosaccharide (from Greek 'mono' meaning one and 'sacchar' meaning sugar) refers to the simplest form of carbohydrates.

  • Common characteristics:

    • Carbons range from 3 to 7.

    • They can exist in linear forms or ring-shaped molecules.

    • Important examples include Glucose, Galactose, and Fructose, which are isomeric monosaccharides with the formula C<em>6H</em>12O6C<em>6H</em>{12}O_6.

  • Example of a function: Glucose is used to produce ATP, the energy currency of cells.

Disaccharides
  • Disaccharides are formed when two monosaccharides undergo a dehydration reaction to form a covalent bond.

  • The term 'disaccharide' derives from 'di' meaning two and 'sacchar' meaning sugar.

  • Glycosidic Bond: This is the covalent bond that forms between a carbohydrate molecule and another molecule.

  • Common disaccharides include:

    • Lactose (milk sugar)

    • Maltose (grain sugar)

    • Sucrose (table sugar).

Polysaccharides
  • Polysaccharides: Long chains of monosaccharides linked by glycosidic bonds.

  • The term 'polysaccharide' comes from 'poly' meaning many and 'sacchar' meaning sweet.

  • They can be branched or unbranched and composed of different types of monosaccharides.

  • Common polysaccharides include:

    • Starch: Storage form of sugar in plants.

    • Glycogen: The storage form of glucose in humans and other vertebrates, primarily composed of glucose monomers.

    • Cellulose: A structural component of the plant cell wall.

    • Chitin: A nitrogen-containing polysaccharide.

Benefits of Carbohydrates

  • Essential for a balanced diet.

  • Energy content: 1 gram of carbohydrates provides approximately 4.3 kilocalories.

  • Fiber: Promotes regular bowel movements and regulates blood glucose levels. It removes excess cholesterol, preventing its entry into the bloodstream and may reduce the occurrence of colon cancer.

  • Glucose serves as an immediate energy source, particularly for cellular processes such as ATP production.

Lipids

Defining Lipids

  • Lipids are a diverse group of compounds characterized primarily by their hydrophobic nature; they are mostly nonpolar in composition.

  • They include hydrocarbons predominantly consisting of carbon-carbon or carbon-hydrogen bonds.

  • Key characteristics:

    • Nonpolar Molecules: Hydrophobic, unable to mix with water.

    • Functions include storing long-term energy, providing insulation, serving as building blocks for hormones, and forming cellular membranes.

  • Main categories of lipids:

    • Fats

    • Oils

    • Waxes

    • Phospholipids

    • Steroids.

Fats and Oils
  • A fat molecule consists of:

    • Glycerol: An organic compound with three carbons, five hydrogens, and three hydroxyl (OH) groups.

    • Fatty Acids: Long chains of hydrocarbons with a carboxyl group attached; lengths ranging from 4 to 36 carbons.

Saturated and Unsaturated Fatty Acids
  • Saturated Fatty Acids: Characterized by single bonds between neighboring carbons in the fatty acid chains, resulting in a solid state at room temperature.

    • Examples: Stearic acid, palmitic acid, butyric acid, and animal fats.

  • Unsaturated Fatty Acids: Contain at least one double bond within the hydrocarbon chains and typically remain liquid at room temperature (oils).

    • Plant-derived, they assist in lowering blood cholesterol levels.

    • Identified as either cis (hydrogens on the same side) or trans (hydrogens on opposite sides).

    • Examples: Oleic acid, olive oil, corn oil, and cod liver oil.

Trans Fats
  • Trans Fats: Created by artificially hydrogenating oils to transform them into a semi-solid state.

  • High trans fat intake can elevate low-density lipoproteins (LDL - bad cholesterol), posing cardiovascular risks.

  • Food labeling is required when trans fats are present. Common examples include margarine and certain peanut butter types.

Omega Fatty Acids
  • Omega Fatty Acids: Essential fatty acids that must be obtained through the diet since the body cannot synthesize them.

    • Health benefits include reducing heart attack risks, lowering triglyceride levels, and decreasing blood pressure.

    • Examples: Omega-3 fatty acids include alpha-linoleic acid (ALA), eicosatetraenoic acid (EPA), and docosahexaenoic acid (DHA) found in fatty fish like salmon, trout, and tuna.

Waxes and Phospholipids
  • Waxes: Lipids comprising long-chain fatty acids esterified to long-chain alcohols, serving protective functions on surfaces like leaves and animal fur.

  • Phospholipids: Major components of plasma membranes, comprised of fatty acid chains linked to a glycerol backbone, characterized as amphipathic (having both hydrophobic and hydrophilic parts).

Steroids
  • Steroids: Comprise fused ring structures, are hydrophobic and insoluble in water. Many, such as cholesterol, possess –OH functional groups, classifying them as sterols.

Proteins

Defining Proteins

  • Proteins are among the most abundant organic molecules in living systems and showcase the widest variety of functions of any macromolecule.

  • Functions may include:

    • Structural roles

    • Regulatory roles

    • Protective functions

    • Involvement in transport, storage, toxin creation, or enzymatic activity.

  • Each cell may contain thousands of types of proteins, which are polymers of amino acids arranged in specific linear sequences.

Types and Functions of Proteins
  • Enzymes: Catalysts for biochemical reactions, often complex or conjugated proteins, specialized for substrates.

    • Example: Digestive enzymes like amylase, lipase, pepsin, and trypsin facilitate nutrient breakdown into monomeric units.

  • Hormones: Chemical-signaling molecules, often small proteins or steroids, secreted by endocrine cells to regulate physiological processes, including growth and metabolism.

  • Additional protein types include:

    • Transport: Hemoglobin and albumin carrying substances in blood or lymph.

    • Structural: Includes actin, tubulin, keratin for constructing structural components like the cytoskeleton.

    • Defense: Immunoglobulins for protecting against pathogens.

    • Contractile: Actin and myosin for muscle contraction.

    • Storage: Legume storage proteins and egg white (albumin) providing nourishment during early development stages.

Amino Acids
  • Proteins are formed from monomers called amino acids, with 20 common amino acids.

  • Among these, 9 are essential amino acids that humans must obtain from dietary sources.

  • Amino acids are linked by peptide bonds, which form through dehydration reactions and create polypeptides (polymers of amino acids with free amino groups).

Protein Structure

  • Primary Structure: Linear sequence of amino acids constituting a protein.

  • Secondary Structure: Regular structures formed through hydrogen bonds between amino acids, including:

    • α-Helix: A helical structure stabilized by hydrogen bonds.

    • β-Pleated Leaflet: A structure with hydrogen bonding creating 'pleats'.

  • Tertiary Structure: The overall three-dimensional conformation resulting from interactions between secondary structural elements and amino acid side chains.

  • Quaternary Structure: The assembly of discrete polypeptide subunits within a protein.

Denaturation and Protein Folding
  • Denaturation: The loss of structural integrity in a protein due to environmental factors (e.g., temperature, pH, chemicals), which can be reversible or irreversible.

  • Protein Folding: Critical for protein function, often assisted by chaperones that help the protein achieve its proper configuration before dissociating after folding completion.

Nucleic Acids

Defining Nucleic Acids

  • Nucleic Acids are biological macromolecules that carry the genetic blueprint for cells and instruct cell functioning.

  • Two primary types exist:

    • DNA (Deoxyribonucleic Acid)

    • RNA (Ribonucleic Acid).

  • Both nucleic acids are made of monomers called nucleotides, which consist of:

    • A nitrogenous base

    • A pentose (five-carbon) sugar

    • A phosphate group.

DNA Structure
  • Double Helix Structure: Formed by two strands of nucleotides coiling around each other.

    • The sugar and phosphate groups form the backbone of the helices, while nitrogenous bases (A, T, G, C) stack in the center like steps on a staircase.

    • Hydrogen bonds connect the base pairs.

    • Strands exhibit antiparallel orientation (running in opposite directions).

Base Pairing in DNA and RNA
  • In base pairing, the following relationships hold:

    • Cytosine pairs with Guanine

    • Adenine pairs with Thymine in DNA and Uracil in RNA.

  • Purines include Adenine and Guanine; Pyrimidines include Cytosine, Thymine, and Uracil.

RNA Structure and Types
  • RNA is involved in protein synthesis, typically single-stranded, comprising ribonucleotides linked by phosphodiester bonds.

    • Contains ribose as the sugar and has bases A, U, G, and C.

  • Four types of RNA:

    • Messenger RNA (mRNA): Carries genetic information from DNA to ribosomes during protein synthesis.

    • Ribosomal RNA (rRNA): Helps align mRNA and tRNA during translation and catalyzes peptide bond formation.

    • Transfer RNA (tRNA): Transports activated amino acids to the ribosome during protein synthesis.

    • MicroRNA (miRNA): Involved in regulating gene expression and suppressing mRNA messages.

Central Dogma of Molecular Biology
  • The Central Dogma of Life describes the flow of genetic information in organisms as:

    • From DNA to RNA to Protein.

    • The processes:

    • Transcription: The synthesis of mRNA from DNA.

    • Translation: The synthesis of proteins based on mRNA structure.

    • Exceptions occur in specific viral processes that do not conform to this flow.