Unit 1 – Cell Compounds & Homeostasis Comprehensive Notes

Homeostasis and Feedback Mechanisms

  • Core idea: Living systems expend energy to keep their internal environment within narrow limits (homeostasis) despite external change.
  • Single-celled vs. Multicellular
    • Unicellular life (e.g., euglena) survives as long as the environment remains within tolerable limits and nutrients are available.
    • Humans are composed of \text{~10^{14}} cells bathed in extracellular fluid (ECF).
    • Cells co-operate to keep ECF variables (temperature, pH, osmotic pressure, nutrient & gas levels) nearly constant.
  • 4 universal components of any feedback loop
    1. Stimulus / Change – any deviation in a monitored variable (temperature, pressure, solute concentration…).
    2. Receptor / Sensor – detects the stimulus and relays input to the control centre.
    3. Control Centre (Integrator) – possesses a set point (e.g., 37C37^{\circ}C for core body temperature); compares actual value with set point; sends commands.
    4. Effector – muscle, gland or organ that carries out corrective action and restores the variable toward set point.

Negative feedback

  • Definition: Response counteracts the original change → system stability.
  • Blood-pressure example
    • Baroreceptors in carotid/aortic walls detect P.
    • Signals travel via glossopharyngeal nerve to cardiovascular centre in medulla.
    • If PP↓ → medulla ↑ heart rate & contractility ⇒ ↑ cardiac output ⇒ PP↑ toward set point; stimulus vanishes.
    • If PP↑ → opposite adjustments.
  • Other instances: thermoregulation, blood glucose control, osmoregulation, blood pO<em>2p\text{O}<em>2 / pCO</em>2p\text{CO}</em>2, calcium balance.

Positive feedback

  • Definition: Response amplifies the deviation; drives the system out of homeostatic range until an external stop signal removes stimulus.
  • Only course-required example: childbirth.
    • Fetal head stretches cervix → stretch receptors signal hypothalamus → posterior pituitary releases oxytocin → stronger uterine contractions → more stretch… loop continues until delivery, after which oxytocin falls and stability returns.

Applied activities

  • Patient-X glucose graph – data remain 70-110 mg·dL⁻¹; demonstrates intact negative feedback for glycemia.
  • Hyperthermia case (Joy & Mary)
    • Homeostasis explanation must reference: heat receptors in skin & core; hypothalamic set point; effectors (sweat glands, vasodilation).
    • Elderly w/ poor circulation have compromised vasodilation ⇒ less heat loss.
    • Evaporative cooling: water absorbs heat (endothermic) during phase change; fan ↑ convection + evaporation.
    • Avoid shivering/vasoconstriction because these raise thermogenesis and reduce peripheral heat loss.

Water: Molecular Structure and Properties

  • Bonding inside one H₂O: polar covalent bonds between O and each H (e⁻ shared unequally).
  • Intermolecular bonding: hydrogen bonds – attraction between δ\delta^{-} O of one molecule and δ+\delta^{+} H of a neighbour; each H₂O can form up to 4 H-bonds.

Emergent properties (relevant to biology)

  1. Excellent solvent
    • “Universal solvent” for ionic & polar solutes; forms hydration shells.
    • Blood plasma, cytosol ≈ 90 % water – allows transport & biochemical reactions.
    • Solution definitions: solute = lesser quantity; solvent = greater. Examples given (baking soda in water, acetone removing nail polish, antifreeze mix, metal in acid).
  2. High specific heat / heat of vaporisation
    • c_{water} = 1\;\text{cal·g}^{-1}\,^{\circ}C^{-1}; buffers body & climate.
    • Evaporative cooling: high-energy molecules leave → average kinetic energy of remaining water ↓.
  3. Density anomaly
    • Ice < liquid water density ⇒ floats, forming insulating layer; aquatic life survives winter.
  4. Transparency – lets light reach photosynthetic organisms in water.
  5. Cohesion & Adhesion
    • Cohesion ⇒ surface tension (water strider, alveolar lining).
    • Adhesion ⇒ capillary rise; alveolar surfactant reduces excessive tension.
    • Everyday examples: water beading on waxed car (cohesion); meniscus in glass cylinder (adhesion).

Functions of water in humans

  • Medium for metabolic reactions.
  • Transport & lubricant (blood, lymph, synovial fluid, mucus, CSF).
  • Temperature regulation via perspiration & blood flow.
  • Reactant/product in hydrolysis & condensation reactions.

pH, Acids, Bases, Buffers

  • pH definition: pH=log[H+]\text{pH} = -\log[H^{+}] ; scale 0-14 (logarithmic).
    • [H^{+}] > [OH^{-}] → acidic (pH < 7).
    • [H+]=[OH][H^{+}] = [OH^{-}] → neutral (pH = 7).
    • [H+]<[OH][H^{+}] < [OH^{-}] → basic (pH > 7).
  • Acid: proton donor (e.g., HClH++ClHCl \rightarrow H^{+}+Cl^{-}).
  • Base: proton acceptor / OH⁻ donor (e.g., NaOHNa++OHNaOH \rightarrow Na^{+}+OH^{-}).
  • Every pH unit = 10-fold [H⁺] change; pH 4 is 10210^{2} × more acidic than pH 6.

Buffers

  • Mixtures that minimise pH change by reversible binding of H⁺/OH⁻.
  • Composed of weak acid/conjugate base pairs (e.g., H<em>2CO</em>3/HCO3H<em>2CO</em>3/HCO_3^{-} in blood).
  • Critical because enzymes/proteins denature outside narrow pH ranges (blood ≈ 7.35–7.45).

Biological Molecules Overview

  • Carbon versatility: 4 valence electrons ⇒ can form up to 4 covalent bonds, chains & rings.
  • Terminology
    • Monomer: single subunit.
    • Polymer: large molecule of repeating monomers.
    • Dehydration synthesis (condensation): links monomers; removes H++OHH^{+}+OH^{-}H2OH_2O (energy required).
    • Hydrolysis: breaks polymers by adding water (energy released; catabolic).
  • 4 classes studied: Carbohydrates, Lipids, Proteins, Nucleic Acids.

Carbohydrates

  • Elements & general formula: C,H,OC, H, O with H:O = 2:1; empirical CH2OCH_2O.

Monosaccharides (C₅ or C₆)

  • Hexoses (C₆H₁₂O₆):
    • Glucose (blood sugar).
    • Fructose (fruit sugar; sweetest).
    • Galactose (part of lactose).
  • Pentoses: ribose (RNA) & deoxyribose (DNA; 1 O less).
  • Isomers share formula but differ in arrangement.

Disaccharides (C₁₂H₂₂O₁₁) – formed by glycosidic linkage

  1. Maltose = glucose + glucose.
  2. Sucrose = glucose + fructose.
  3. Lactose = glucose + galactose.

Polysaccharides ((C6H{10}O5)n)

  • Starch (plant glucose storage; moderately branched).
  • Glycogen (animal storage; highly branched; liver & muscle).
  • Cellulose (plant cell walls; β-1,4 linkages; indigestible fibre “roughage”).

Functions

  • Rapid energy source via respiration (C<em>6H</em>12O<em>6+6O</em>26CO<em>2+6H</em>2O+ATPC<em>6H</em>{12}O<em>6 + 6O</em>2 \rightarrow 6CO<em>2 + 6H</em>2O + ATP).
  • Structural (cell walls).
  • Energy storage (starch, glycogen).

Lipids

  • Include: neutral fats (triglycerides), phospholipids, steroids (plus oils, waxes, soaps).
  • Elements C,H,OC, H, O (H:O > 2:1) ⇒ non-polar, hydrophobic.

Fatty acids

  • Long hydrocarbon chain + terminal carboxyl (\ce{-COOH}).
  • Saturated: only C–C single bonds; straight → pack tightly (solid fat).
  • Unsaturated: ≥1 C=C double bond; kinked → liquid oils.

Neutral fats (Triglycerides)

  • 1 glycerol + 3 fatty acids (mono- & di-glycerides have 1 or 2).
  • Major energy reserve (9 kcal·g⁻¹); insulation & organ protection.

Phospholipids

  • Glycerol + 2 fatty acids + phosphate-N head.
  • Amphipathic: hydrophilic head / hydrophobic tails.
  • Form phospholipid bilayer of cell membranes; heads face ECF & cytosol, tails interior.

Steroids (sterols)

  • 4 fused carbon rings (e.g., cholesterol, testosterone, estrogen).
  • Cholesterol stabilises plasma membranes & is precursor for steroid hormones; excess → atherosclerosis ((\uparrow) BP).

Proteins

  • Elements C,H,O,NC, H, O, N (+ S, P, Fe occasionally).
  • Monomer: amino acid (central C bonded to H, amino \ce{-NH_2}, carboxyl \ce{-COOH}, variable R-group).
  • Peptide bond: \ce{-COOH + NH2 \rightarrow -CONH- + H2O} (dehydration synthesis).

Structural hierarchy

  1. Primary – linear a.a. sequence (covalent peptide bonds).
  2. Secondary – α-helix or β-sheet via H-bonds between backbone groups.
  3. Tertiary – 3-D folding; interactions among R-groups: H-bonds, ionic, hydrophobic interactions, disulfide bridges.
  4. Quaternary – assembly of >1 polypeptide (e.g., hemoglobin = 4 subunits + heme).

Denaturation

  • Loss of native shape (and active site) due to heat, pH change, heavy metals, alcohol, radiation… → loss of function; sometimes irreversible.

Functional categories

  • Enzymes (biological catalysts) – lower activation energy; e.g.,
    • Maltase: maltose → 2 glucose.
    • Carbonic anhydrase: CO<em>2+H</em>2OH<em>2CO</em>3CO<em>2 + H</em>2O \leftrightarrow H<em>2CO</em>3 (blood gas transport).
  • Transport proteins – hemoglobin, membrane channels.
  • Immune proteins – antibodies.
  • Structural proteins – keratin (hair, nails), collagen (connective tissue), actin & myosin (muscle contraction).

Nucleic Acids and ATP

  • Monomer: nucleotide = phosphate + pentose sugar + nitrogenous base.
  • Types: DNA, RNA, ATP.

DNA/RNA (genetic information)

  • DNA stores hereditary info; RNA involved in protein synthesis.

ATP – Adenosine Triphosphate

  • Adenosine (adenine + ribose) + 3 phosphates.
  • High-energy phosphoanhydride bonds ((~) symbol).
  • Energy currency:
    \text{ATP} + H2O \xrightarrow{ATPase} \text{ADP} + Pi + \text{Energy} \; (\approx 7 \text{ kcal·mol}^{-1})
  • ADP + PiP_i can be re-phosphorylated (e.g., by cellular respiration).
  • Analogy: fats = savings bonds; glycogen = bank account; glucose = piggy bank; ATP = pocket cash.