Chapter 2: The Chemical Level of Organization (Principles of Anatomy and Physiology)

Basic Principles of Chemistry

  • Chemistry is the science of the structure and interactions of matter.

  • Matter is anything that has mass and takes up space.

  • Mass is the amount of matter contained in a substance; weight is the force of gravity acting on that mass.

Matter and Forms of Matter

  • Matter exists in three fundamental forms:

    • Solid: definite shape and volume

    • Liquid: definite volume, takes the shape of its container

    • Gas: no definite shape or volume

  • All forms of matter are composed of chemical elements.

Chemical Elements

  • Elements are given chemical symbols (examples):

    • O = oxygen, C = carbon, H = hydrogen, N = nitrogen

  • These four elements make up the majority of the human body.

Atoms

  • Atoms are the smallest units of matter that retain the properties of an element.

  • Subatomic particles:

    • Protons (p+), located in the nucleus

    • Neutrons (n0), located in the nucleus

    • Electrons (e−), negatively charged, orbit the nucleus in the electron cloud

  • Atoms are composed of a nucleus (protons and neutrons) and surrounding electron cloud.

Atomic Structures (key isotopes and values)

  • Hydrogen (H):

    • Atomic number Z = 1; Mass number A = 1 or 2; Atomic mass ≈ 1.01

  • Carbon (C):

    • Z = 6; A = 12 or 13; Atomic mass ≈ 12.01

  • Nitrogen (N):

    • Z = 7; A = 14 or 15; Atomic mass ≈ 14.01

  • Oxygen (O):

    • Z = 8; A = 16, 17, or 18; Atomic mass ≈ 16.00

  • Sodium (Na):

    • Z = 11; A = 23; Atomic mass ≈ 22.99

  • Chlorine (Cl):

    • Z = 17; A = 35 or 37; Atomic mass ≈ 35.45

  • Potassium (K):

    • Z = 19; A = 39, 40, or 41; Atomic mass ≈ 39.10

  • Iodine (I):

    • Z = 53; A = 127; Atomic mass ≈ 126.90

  • Isotope note: Mass number A = number of protons + neutrons; boldface in slides indicates the most common isotope.

Ions, Molecules, and Compounds

  • Ions: atoms that have lost or gained electrons, resulting in a positive (cation) or negative (anion) charge.

  • Ion formation depends on valence electrons to achieve stability.

  • Molecule: two or more atoms sharing electrons.

  • Compound: a substance composed of two or more different elements.

Free Radicals

  • Free radicals have an unpaired electron in the outer shell, making them unstable, highly reactive, and potentially destructive to nearby molecules.

  • Sources include UV light, ozone, x-rays, pollution, cigarette smoke.

  • Antioxidants help neutralize reactive oxygen species.

Chemical Bonds

  • A chemical bond occurs when atoms are held together by forces of attraction.

  • The likelihood of bond formation is largely determined by the number of electrons in an atom’s valence (outer) shell.

  • The octet rule (rule of eight): a stable valence shell has 8 electrons.

  • Bonding outcomes: gain, loss, or sharing of electrons depending on valence electron count and energetics.

  • The periodic table helps predict valence electron counts and bonding behavior.

Ionic Bonds

  • Ionic bonds form when a positively charged ion (cation) is attracted to a negatively charged ion (anion).

  • No electrons are shared; instead, electrons are transferred to achieve stable electron configurations.

  • Example: sodium chloride, NaCl.

    • Na tends to lose one electron to form Na+ with a complete valence shell.

    • Cl tends to gain an electron to form Cl− with a complete valence shell.

  • Cations vs. Anions: note that the electron transferred during bond formation may come from a different atom than the one that accepts it.

  • Ionic bonds create compounds with overall neutral charge but composed of oppositely charged ions.

Covalent Bonds

  • Covalent bonds form when two or more atoms share electrons.

  • Can share one (single), two (double), or three (triple) pairs of electrons.

  • Strength generally increases with the number of shared electron pairs.

  • Covalent bonds can occur between atoms of the same element or different elements.

  • Polar vs. Nonpolar Covalent Bonds:

    • Nonpolar covalent: electrons shared equally; no partial charges.

    • Polar covalent: electrons pulled more toward one nucleus, creating partial charges (dipole).

Hydrogen Bonds

  • Hydrogen bonds arise from the attraction between oppositely charged parts of polar molecules.

  • They are much weaker than ionic or covalent bonds but are crucial for the properties of water and biomolecules.

Structural Organization in Water and Hydrogen Bonding

  • Water’s polarity makes it an excellent solvent for ionic and polar substances (hydrophilic) and poor solvent for nonpolar substances (hydrophobic).

  • Hydrogen bonding between water molecules provides cohesion and surface tension.

  • Water plays a key role in biochemical reactions as a solvent and participant (hydrolysis and dehydration synthesis).

Chemical Reactions

  • Reactions occur when bonds are formed or broken; reactants become products.

  • Metabolism refers to all chemical processes in organisms, including energy transformations.

Forms of Energy & Chemical Reactions

  • Energy types:

    • Potential energy: stored energy

    • Kinetic energy: energy of motion

    • Chemical energy: energy stored in chemical bonds

  • Law of conservation of energy: energy cannot be created or destroyed, only converted.

  • Reactions may release energy (exergonic) or require energy input (endergonic).

  • Cellular coupling: exergonic reactions power endergonic ones (e.g., glucose catabolism releases energy; ATP bonds store energy released by breakdown).

Activation Energy and Catalysts

  • Activation energy (E_a): energy required to start a reaction; reactants must collide with sufficient energy/orientation to react.

  • Catalysts speed up reactions; most are enzymes; catalysts are not consumed in the reaction and can catalyze many cycles.

  • Body conditions (temperature, concentration) influence reaction rates; enzymes help overcome these limitations.

Types of Chemical Reactions

  • Synthesis (anabolism): two or more substances combine to form a larger, more complex product.

  • Decomposition (catabolism): larger molecules split into smaller components.

  • Exchange (displacement): parts of molecules exchange places.

  • Reversible: reactions can proceed in both directions; products can revert to reactants.

  • Oxidation-reduction (redox): electron transfer between reactants; oxidation involves loss of electrons and energy release; reduction involves gain of electrons and energy gain.

Inorganic vs Organic Compounds and Solutions

  • Inorganic compounds: typically lack carbon and are simpler (water is the most important inorganic compound in living things).

  • Organic compounds: contain carbon, usually with hydrogen, and form covalent bonds; typically large molecules with carbon chains.

  • Water properties and role in solutions are central to many biological processes.

Properties of Water and Solvent Capabilities

  • Water is a versatile solvent for ionic and polar substances (hydrophilic) due to its polarity.

  • Nonpolar substances (lipids) are hydrophobic.

  • Water participates in reactions as a reactant or product (hydrolysis and dehydration synthesis).

  • Water exhibits high heat capacity and high heat of vaporization, enabling thermal regulation in organisms.

  • Water acts as a lubricant in body cavities and joints.

Percentages and Molarity in Solutions

  • Percentage (mass per volume): grams of solute per 100 milliliters of solution.

    • Example: to make a 10% NaCl solution, dissolve 10 g NaCl in enough water to make 100 mL solution.

  • Molarity (M, moles per liter): 1 M = 1 mole of solute per liter of solution.

    • Example: to make 1 M NaCl, dissolve 1 mole of NaCl (58.44 g) in water to make 1 L of solution.

  • Note: A mole is defined as the amount of substance containing as many elementary entities as there are atoms in 12 g of carbon-12; the slide humorously adds, “A mole is the amount of any substance that has a mass in grams equal to the sum of the atomic masses of all its atoms,” and includes a joking aside about the mole’s origin.

  • A key aside from the slides: the exact numerical value 58.44 g/mol is the molar mass of NaCl.

Acids, Bases, & Salts

  • Dissociation in water:

    • Acids dissociate to yield H+ and anions (proton donors).

    • Bases dissociate to yield OH− (and cations) (proton acceptors).

    • Salts dissociate into cations and anions, neither being H+ or OH−.

  • Examples (illustrated in slides): HCl (acid), KOH (base), KCl (salt).

pH and Buffers

  • pH measures the hydrogen ion concentration in solution.

  • pH scale ranges from 0 to 14; lower values mean more acidic; 7 is neutral; higher values are basic.

  • The scale is logarithmic: a change of one pH unit represents a tenfold change in hydrogen ion concentration.

  • Expressions:

    • ext{pH} = -
      \log_{10} [H^+]

    • [H^+] = 10^{- ext{pH}}

  • A neutral pH at 25°C corresponds to [H^+] = [OH^-] = 1.0 imes 10^{-7} ext{ M}.

  • Buffers maintain blood and body fluid pH within a narrow range by converting strong acids or bases into weak acids or bases, often involving H+ donation or removal. Example: bicarbonate ion (
    ext{HCO}3^-) neutralizes an acid by forming ext{H}2 ext{CO}3: ext{HCO}3^- + ext{H}^+
    ightarrow ext{H}2 ext{CO}3.

Overview of Organic Compounds

  • Carbon is the backbone of organic chemistry; carbon forms four bonds (valence = 4).

  • Carbon can form chains, rings, and various shapes; carbon compounds are often hydrophobic in water.

  • Carbon compounds are key energy sources; hydrocarbon skeletons may be bonded to functional groups that determine reactivity.

Major Functional Groups of Organic Molecules (selected)

  • Hydroxyl group: –OH (polar, hydrophilic; many –OH groups increase water solubility)

  • Sulfhydryl group: –SH (polar, can stabilize protein structure via disulfide bonds; e.g., cysteine)

  • Carbonyl group: C=O (polar; present in ketones and aldehydes)

  • Aldehydes: carbonyl at the end of the carbon skeleton

  • Ketones: carbonyl within the carbon skeleton

  • Carboxyl group: –COOH (acidic; amino acids have –COOH; deprotonates at body pH to become –COO−)

  • Ester: –COO– (common in fats/oils; triglycerides)

  • Phosphate: –PO4^{2−} (very hydrophilic; energy carrier in ATP)

  • Amines: –NH2 (acts as a base in physiology; amino acids contain –NH2)

Carbohydrates

  • Composed of C, H, O; H:O ratio ≈ 2:1 (author calls it “watered carbon”).

  • Main energy source for cells; include sugars, glycogen, starch, cellulose.

  • Classes based on size: monosaccharides, disaccharides, polysaccharides.

  • Monosaccharides examples: Glucose, Fructose, Galactose; also ribose and deoxyribose (pentoses).

  • Disaccharides: Sucrose (glucose + fructose), Lactose (glucose + galactose), Maltose (glucose + glucose).

  • Polysaccharides: Glycogen, Starch, Cellulose.

Lipids

  • Lipids are hydrophobic and insoluble in water.

  • Classes include fatty acids, triglycerides, phospholipids, steroids, and more.

  • Fatty acids can be saturated or unsaturated.

  • Triglycerides: energy storage, insulation, protection; made from glycerol plus three fatty acids via ester linkages.

  • Phospholipids: major components of cell membranes; amphipathic with polar heads and nonpolar tails.

  • Steroids: cholesterol (membrane component; precursor to bile salts, vitamin D, steroid hormones); other steroids include bile salts, cortisol, and sex hormones.

  • Eicosanoids: prostaglandins and leukotrienes; regulate inflammation, immunity, etc.

  • Other lipids: carotene (vitamin A precursor/antioxidant), vitamin E (antioxidant and wound healing), vitamin K (blood clotting), lipoproteins (lipid transport in blood).

Fatty Acids and Triglycerides (structural notes)

  • Palmitic acid (saturated, C16:0) vs. oleic acid (unsaturated, C18:1).

  • Dehydration synthesis links fatty acids to glycerol to form triglycerides; hydrolysis can release fatty acids.

Phospholipids and Membranes

  • Phospholipids have polar heads (hydrophilic) and nonpolar tails (hydrophobic).

  • Arranged in a bilayer to form cell membranes; polar heads face aqueous environments, nonpolar tails face inward.

Steroids

  • Four-ring hydrocarbon skeleton.

  • Examples: Cholesterol; Estradiol; Testosterone; Cortisol.

Proteins

  • Proteins are large nitrogen-containing molecules with many functions:

    • Structural: collagen, keratin

    • Regulatory: hormones (e.g., insulin), signaling molecules

    • Contractile: actin, myosin

    • Immunological: antibodies

    • Transport: hemoglobin

    • Catalytic: enzymes (e.g., amylase, sucrase, ATPase)

  • Amino Acids: building blocks of proteins; each amino acid has:

    • Central carbon (C)

    • Hydrogen atom (H)

    • Amino group (–NH2)

    • Carboxyl group (–COOH)

    • Side chain (R group) that defines identity

  • Peptide bonds: link amino acids; a protein is a chain of amino acids connected by peptide bonds.

Protein Structure (four levels)

  • Primary structure: unique amino acid sequence (linear chain).

  • Secondary structure: local folding/alignment (alpha helices and beta pleated sheets) stabilized by hydrogen bonds.

  • Tertiary structure: three-dimensional folding of a single polypeptide chain.

  • Quaternary structure: assembly of two or more polypeptide chains (many proteins stop at tertiary structure).

Enzymes

  • Enzymes are biological catalysts that speed up reactions.

  • Names typically end in -ase.

  • Properties:

    • Highly specific: each enzyme fits one substrate.

    • Extremely efficient: can increase reaction rates dramatically (up to billions of times).

    • Regulated by cellular controls: enzymes can be activated or inhibited.

  • Active site: region where substrate binds; formation of the enzyme–substrate complex enables the chemical reaction.

Nucleic Acids

  • Nucleic acids are chains of nucleotides.

  • Each nucleotide consists of:

    • Nitrogenous base (adenine A, thymine T, cytosine C, guanine G, or uracil U in RNA)

    • Pentose sugar (deoxyribose in DNA, ribose in RNA)

    • Phosphate group

  • DNA forms the genetic code in cell nuclei; RNA relays instructions from genes to guide protein synthesis.

Components of a Nucleotide (illustrative)

  • Nitrogenous bases: purines (A, G) and pyrimidines (C, T, U).

  • Sugar: deoxyribose (DNA) or ribose (RNA).

  • Phosphate group connects sugars to form the backbone.

DNA and RNA Structures and Pairs

  • DNA is a double helix with two strands of nucleotides.

  • Bases pair via hydrogen bonds: A pairs with T (2 hydrogen bonds), G pairs with C (3 hydrogen bonds).

  • RNA is typically single-stranded; in DNA vs RNA distinctions:

    • DNA: deoxyribose sugar; bases A, T, C, G; two strands; A–T and G–C pairings.

    • RNA: ribose sugar; bases A, U, C, G; usually single strand; A–U and G–C pairings.

Adenosine Triphosphate (ATP)

  • ATP is the principal energy-storing molecule in the body.

  • Structure: adenosine attached to three phosphate groups (adenosine triphosphate).

  • High-energy phosphate bonds: cleavage releases usable energy for cellular processes.

  • General note: ATP hydrolysis provides energy for muscle contraction, active transport, and many biosynthetic reactions.

Cellular ATP Production (overview)

  • Cellular respiration catabolizes glucose to release energy that is stored in ATP bonds.

  • Two main phases:

    • Anaerobic respiration: without oxygen; glucose partially broken down to pyruvic acid; yields 2 ATP per glucose.

    • Aerobic respiration: with oxygen; glucose is broken down to CO2 and H2O; yields approximately 30–32 ATP per glucose.

  • Detailed chapters on respiration are covered later in the course.

Connections to Foundational Principles

  • Matter and energy transformation: chemical reactions involve conversion between potential, kinetic, and chemical energy.

  • The covalent/ionic/hydrogen bonding framework explains molecular stability, structure, and function in biomolecules.

  • The property of water as a solvent underpins hydration, ionic interactions, and biochemical reaction environments.

  • Organic chemistry underpins biomolecular structure and function (carbohydrates, lipids, proteins, nucleic acids).

  • Buffers and pH homeostasis are essential for maintaining protein structure and enzyme activity.

Practical and Ethical/Contextual Notes

  • The study of chemical principles is essential for understanding physiology, medicine, and biochemistry.

  • Some slides include lighthearted asides (e.g., about molarity humor) — educational context should prioritize scientific accuracy in exams.

  • Real-world relevance: acid-base balance, energy metabolism, and macromolecule function underpin health, disease, and pharmacology.

[H^+] = 10^{- ext{pH}}
[OH^-] = 10^{- ext{pOH}}
ext{pH} = -
\log_{10}[H^+]
1 ext{ M} = rac{1 ext{ mole}}{1 ext{ liter}}
58.44 ext{ g/mol} for NaCl

  • Example buffer reaction: ext{HCO}3^- + ext{H}^+ ightarrow ext{H}2 ext{CO}_3

  • For a typical neutral body pH: [H^+] \approx 1.0 \times 10^{-7} \text{ M} and [OH^-] \approx 1.0 \times 10^{-7} \text{ M} at 25°C.

  • Key practical values from the slides:

    • Gastric juice pH: 1.2 - 3.0

    • Lemon juice: pH \approx 2.3

    • Vinegar: pH \approx 3.0

    • Orange juice: pH \approx 3.5

    • Blood: pH \approx 7.35 - 7.45

    • Cerebrospinal fluid: pH \approx 7.4

    • Urine: pH \approx 4.6 - 8.0

    • Saliva: pH \approx 6.35 - 6.85

    • Milk: pH \approx 6.8

    • Distilled water: pH = 7.0

    • Lye (strong base): pH = 14.0

  • Major groups and example molecules provide a framework to analyze biomolecules in exams (e.g., identify functional groups in a given molecule, predict solubility, or predict bonding patterns).

Summary of Key Formulas and Concepts

  • Atomic structure and isotopes: Z = number of protons; A = Z + number of neutrons; common isotopes are noted by mass number.

  • Ionic vs covalent bonding; polarity and partial charges in covalent bonds influence solubility and biological interactions.

  • Hydrogen bonding, cohesion, and surface tension are essential for water properties and biomolecule interactions.

  • Energy changes in reactions: exergonic vs endergonic; activation energy; catalysis by enzymes.

  • Carbohydrates, lipids, proteins, and nucleic acids form the core of biological macromolecules; their monomers, polymers, and functional roles define cellular structure and function.

  • ATP and cellular respiration as central energy pathways; understanding glucose catabolism and ATP synthesis is foundational for physiology and bioenergetics.