LW

Unit 1 Lec 3

Organic vs. Inorganic and essential context

  • Organic chemistry in biology focuses on molecules that contain carbon-hydrogen (C–H) bonds.
  • Living things predominantly use elements such as hydrogen (H), carbon (C), oxygen (O), and nitrogen (N). Other smaller elements exist but the key feature is carbon_backbone with hydrogen attached.
  • Definition distinction:
    • Organic molecules: contain carbon and hydrogen (C–H bonds) and typically form a carbon backbone with various atoms bonded to it.
    • Inorganic molecules: lack the carbon–hydrogen framework or are carbon-containing but without C–H bonds; for example, water is H₂O (inorganic).
  • Water (H₂O) is essential for all metabolic processes; life depends on water as a solvent and medium for reactions.
  • In living systems, molecules bond via covalent bonds to form larger macromolecules; common elements in biological macromolecules include O, H, N, C.
  • When biological molecules bond to proteins, you can get glycoproteins: glyco- means carbohydrate; a carbohydrate is attached to a protein to form a single molecule with both protein and carbohydrate components.
  • Four major biomolecule categories (structure and function are tied to monomer length/arrangement):
    • Carbohydrates
    • Nucleic acids
    • Lipids
    • Proteins

The four major biomolecule groups and their overarching principle

  • For each category, the length and arrangement of monomers determine the type of polymer produced and, consequently, function.
  • Shape determines function: monomers link to form polymers; the resulting three-dimensional structure dictates activity.
  • Monomer/polymer concepts recur across categories; breaking and forming bonds involves water in hydrolysis and dehydration synthesis, respectively.

Carbohydrates

  • Monomer units: monosaccharides (the smallest carbohydrate unit).
    • Examples include:
    • Glucose, fructose, galactose (common monosaccharides in biology). ext{C}6 ext{H}{12} ext{O}_6 (general formula for a simple monosaccharide is illustrative; specific monosaccharide formulas vary).
    • Ribose (in RNA) and deoxyribose (in DNA) as sugar components of nucleic acids.
  • Linkage of monosaccharides forms disaccharides via covalent bonds; breaking these bonds with water is hydrolysis. The reverse process (joining monomers) is dehydration synthesis.
    • Disaccharides example: sucrose (table sugar), lactose (milk sugar).
    • Hydrolysis reaction:
      ext{Disaccharide} + ext{H}2 ext{O} ightarrow ext{Monosaccharide}1 + ext{Monosaccharide}_2
  • Polysaccharides: long chains of monosaccharides; multiple units linked by glycosidic bonds.
    • Examples: starch, glycogen, cellulose.
    • Functions:
    • Energy storage (glycogen in animals; starch in plants).
    • Structural support (cellulose in plant cell walls).
    • Quick energy sources when polysaccharides are broken down into monosaccharides.
  • Metabolic role and energy flow:
    • In digestion, polysaccharides are hydrolyzed into monosaccharides, providing quick energy after meals.
    • The liver and muscles store excess glucose as glycogen; in the absence of immediate energy demand, glycogen is mobilized for later use.
  • Physical chemistry note:
    • Carbohydrates are polar and tend to dissolve well in polar solvents like water; water is the universal solvent for polar substances. This supports transport of sugars in bodily fluids.
  • Context on diet and energy:
    • For athletic performance, high-carbohydrate meals before activity supply glycogen stores for sustained energy.
    • Quick energy snacks (e.g., candy or soda) supply monosaccharides that rapidly raise blood glucose.
  • Structural note:
    • In plant cells, cellulose provides structural integrity (cell wall) and is not digestible by humans.
  • Quick mnemonic:
    • Monosaccharides → Disaccharides → Polysaccharides; energy storage vs. structure.

Lipids

  • General properties:
    • Lipids include fats and oils (triglycerides), phospholipids, cholesterol, and more.
    • They are nonpolar (hydrophobic) and do not dissolve well in water; they are not soluble in polar solvents.
  • Triglycerides (fats/oils): main energy storage lipids.
    • Structure: glycerol backbone with three fatty acids attached (via ester bonds). They are a major energy source and insulator.
    • Saturated vs. unsaturated fatty acids:
    • Saturated fats: no double bonds between carbon atoms; straight chains; tend to be solid at room temperature (e.g., animal fats, butter).
    • Unsaturated fats: contain one or more double bonds; kinked chains due to double bonds; typically liquid at room temperature (oils).
    • Shape and function example: a double bond creates a kink, which prevents tight packing; “shape determines function.”
  • Phospholipids: key structural components of cell membranes.
    • Structure: glycerol backbone with two fatty acid tails (nonpolar, hydrophobic) and a phosphate-containing head (polar, hydrophilic).
    • Amphipathic nature: two lives—polar head interacts with water, nonpolar tails avoid water.
    • Membrane formation: spontaneously form a phospholipid bilayer in aqueous environments, with hydrophilic heads facing outward and hydrophobic tails packed inside.
    • Cell membrane relevance: this bilayer forms the boundary of cells; contains various proteins and other molecules that regulate transport and signaling.
  • Cholesterol:
    • Essential component of membranes; stabilizes and modulates fluidity.
    • Synthesized in the liver and obtained from diet; excessive cholesterol in blood is a risk factor for cardiovascular disease.
    • Cholesterol also serves as a precursor for steroid hormones.
  • Lipids in signaling:
    • Some hormones are lipid-derived and can diffuse through lipid membranes to act quickly on target cells.
  • Absorption and digestion note:
    • Not all dietary fats are absorbed; some pass through the digestive tract; efficiency of absorption depends on digestion and transport mechanisms.
  • Real-world context:
    • The balance of saturated and unsaturated fats influences health outcomes; dietary patterns can affect membrane properties and signaling processes.

Nucleotides and Nucleic Acids

  • Monomer: nucleotide (the building block for nucleic acids).
    • Required components of a nucleotide:
    • A sugar (ribose in RNA or deoxyribose in DNA),
    • A nitrogenous base, and
    • A phosphate group.
    • At least one sugar, one nitrogen base, and one phosphate must be present in each nucleotide.
    • Example: ATP (adenosine triphosphate) contains adenosine (adenine + ribose) and three phosphate groups; it functions as an energy carrier.
    • ATP hydrolysis provides energy for biological processes: ext{ATP}
      ightarrow ext{ADP} + ext{P}_i + ext{energy}
  • Nucleic acids:
    • DNA (deoxyribonucleic acid) and RNA (ribonucleic acid) store and transmit genetic information.
    • ATP and other nucleotides also play roles as energy carriers and cofactors in metabolism.
  • Sugar components:
    • DNA uses deoxyribose; RNA uses ribose; these sugars are part of the nucleotide backbone.
  • Functional implication:
    • The sequence of nucleotides encodes information that directs protein synthesis and cellular function.

Proteins

  • Major roles:
    • Growth, repair, and maintenance of body tissues; enzymes as catalysts; antibodies as part of the immune system; structural and transport roles, etc.
  • Monomers: amino acids (20 standard amino acids).
    • General structure of an amino acid:
    • A central carbon (alpha carbon) attached to a hydrogen atom, an amino group (–NH₂), a carboxyl group (–COOH), and a side chain (R group).
    • The R group (side chain) differentiates amino acids and determines chemical properties and function.
    • The 20 amino acids differ only in their R groups, which include hydrophobic, hydrophilic, acidic, and basic residues.
  • Protein synthesis and variety:
    • The sequence of amino acids (primary structure) determines the protein’s final shape and function.
    • A protein can be thousands of amino acids long; even a single amino acid change can produce a different protein.
    • The arrangement of amino acids is like letters that form a vast set of words (proteins) with diverse functions.
  • Protein structure levels:
    • Primary structure: linear sequence of amino acids.
    • Secondary structure: local folding patterns, mainly alpha helices and beta pleated sheets, stabilized by hydrogen bonds.
    • Tertiary structure: overall three-dimensional shape formed by further folding, culled by interactions among R groups (hydrophobic interactions, disulfide bonds, ionic bonds, hydrogen bonds).
    • Quaternary structure: assembly of multiple polypeptide subunits into a functional protein (e.g., hemoglobin).
  • Factors and helpers:
    • Chaperone proteins assist in proper folding of polypeptides.
    • The correct folding is essential for function; misfolding can lead to loss of function or diseases.
  • Enzymes and specificity:
    • Enzymes are proteins that act as catalysts, speeding up reactions by lowering activation energy without being consumed.
    • Activation energy is the energy required to start a reaction; enzymes reduce this barrier to initiate reactions efficiently.
  • Protein diversity and function:
    • The shape and charge distribution of a protein determine its function (e.g., enzymes, antibodies, structural proteins).
  • Glycoproteins:
    • Some proteins are glycosylated; they have carbohydrate (glycan) moieties attached, affecting stability, localization, and function.

Connections to metabolism, health, and real-world relevance

  • The four biomolecule classes work together to sustain life: energy production (carbohydrates, lipids), information storage and transfer (nucleic acids), structure and function of cells (proteins, lipids), and signaling (hormones, enzymes).
  • Diet and energy balance illustrate practical outcomes of these biomolecules: carbohydrates provide quick energy; lipids provide long-term energy and membrane structure; proteins supply amino acids for repair and enzymes; nucleotides underpin genetic information and energy transactions (ATP).
  • Health implications:
    • Membrane composition (phospholipids, cholesterol) affects fluidity, signaling, and transport.
    • Excess saturated fats can impact membranes and cardiovascular health; unsaturated fats tend to be healthier for many diets.
    • Cholesterol is essential but needs to be regulated; statins and dietary choices influence blood cholesterol levels and overall health risk.
  • Ethical/practical considerations:
    • Dietary guidelines and lifestyle choices can influence membrane function, enzyme activity, and disease risk; understanding these biomolecules informs healthcare choices.