APR ASSIGNMENT. Comprehensive Notes on Atomic Structure, Bonding, Organic Molecules, Electrolytes, and Enzymes

Atoms and Atomic Structure

  • An atom is the smallest particle of an element that retains the properties of that element.

  • Subatomic particles:

    • Protons: positively charged, +1.

    • Neutrons: neutral, no charge.

    • Electrons: negatively charged, −1; move around the nucleus in concentric regions called electron shells or energy levels.

  • The central nucleus contains protons and neutrons; electrons occupy regions around the nucleus.

  • An element is uniquely defined by the number of protons in its atoms.

    • Example: only carbon atoms have 6 protons; only potassium atoms have 19 protons.

  • The atomic number Z is the number of protons in an atom of a particular element.

  • In a neutral atom, the number of protons equals the number of electrons, so the overall charge is zero.

  • Atomic mass is the sum of an atom’s protons and neutrons:

    • A = Z + N

    • The number of neutrons (N) can vary for a given element, giving different atomic masses (isotopes).

  • Isotopes: atoms with the same atomic number Z but different atomic weights (A) due to differing numbers of neutrons.

  • Electron shells are filled in fixed numbers:

    • 1st shell (closest to the nucleus) holds a maximum of 2 electrons: 2

    • 2nd shell holds up to 8 electrons: 8

    • 3rd shell can hold up to 18 electrons: 18

    • Subsequent shells can hold higher numbers.

    • The outermost shell is the valence shell and holds a maximum of 8 electrons (octet rule).

  • The electrons in the valence shell determine an atom’s chemical bonding properties.

  • Stable structures: atoms with filled valence shells (e.g., helium) are chemically inactive.

  • Atoms with partially filled valence shells tend to lose, gain, or share electrons to achieve a stable valence electron count.

  • Bond formation basics:

    • Ionic bonding: octet is formed by transferring valence electrons from one atom to another, creating ions that are held together by electrostatic attraction.

    • Covalent bonding: octet is formed by sharing valence electrons between atoms.

  • Key example: ionic bonding (Na and Cl)

    • Sodium (Na) has one valence electron, chlorine (Cl) has seven valence electrons.

    • If Na transfers one electron to Cl, both achieve an octet and form ions: ext{Na}
      ightarrow ext{Na}^+ + e^- \ ext{Cl} + e^-
      ightarrow ext{Cl}^-

    • The resulting ionic bond is the electrostatic attraction between ext{Na}^+ and ext{Cl}^- in the compound NaCl.

  • Covalent bonding examples:

    • Nonpolar covalent bond: sharing of electrons equally; electron density is symmetrical. Example: ext{Cl}_2 (two chlorine atoms share electrons equally).

    • Polar covalent bond: one atom attracts the bonding electrons more strongly (higher electronegativity), leading to an unequal sharing and partial charges. Example: hydrogen chloride (HCl): chlorine is more electronegative, so the electrons spend more time near Cl, giving:

    • partial negative charge on Cl (δ⁻)

    • partial positive charge on H (δ⁺)

  • Hydrogen and electronegativity concept:

    • Hydrogen has only one valence electron (and seeks a second to complete its valence shell, like helium).

    • In H–Cl, chlorine’s greater attraction for electrons creates a polar covalent bond with unequal electron sharing.

  • Bonding summary:

    • Ionic bonds form when electrons are transferred to achieve octets, with electrostatic attraction between ions.

    • Covalent bonds form when electrons are shared to achieve octets; can be nonpolar (equal sharing) or polar (unequal sharing).

    • The number and type of bonds an atom forms depend on the valence electrons needed to fill the valence (outer) shell.

Electrons, Bonding, and Electronegativity in Water and Ions

  • The distribution of electrons around atoms in a bond influences polarity and reactivity.

  • The most electron-rich region is often represented as red, while electron-poor regions may appear blue in visualizations (conceptual).

  • Hydrogen–chlorine examples illustrate two extremes:

    • Nonpolar covalent bond (e.g., Cl–Cl): electrons shared equally; no permanent dipole.

    • Polar covalent bond (e.g., H–Cl): electrons drawn toward the more electronegative atom (Cl), creating partial charges and a dipole.

  • In any given bond, electronegativity differences drive bond type and polarity, affecting molecular interactions and properties in solution.

Organic Molecules and Biological Macromolecules

  • Organic molecules are compounds found in or produced by living things and typically contain carbon.

  • Carbon’s tetravalence allows it to form long chains or backbones by bonding with itself and other elements, enabling the vast diversity of biomolecules.

  • Carbohydrates

    • General formula: empirical ratio H: C: O ≈ 2:1:1; for example, glucose: ext{C}6 ext{H}{12} ext{O}_6

    • Carbohydrates have a two-to-one ratio of hydrogen to carbon and oxygen when expressed as H:C:O ≈ 2:1:1.

    • Functions: important energy sources for cells.

  • Proteins

    • Built from amino acids; each amino acid has:

    • A central carbon atom (the α-carbon)

    • A hydrogen atom

    • An amino group (–NH₂)

    • A carboxyl group (–COOH)

    • A radical (side) group (R) that differentiates each amino acid

    • Amino acids join to form peptides; longer chains form polypeptides; groups of polypeptides form proteins.

    • Proteins have complex folded structures that determine their function.

    • Functions include:

    • Structural support

    • Regulation of body processes

    • Transport of molecules

    • Catalysis of chemical reactions

    • Defense against invaders

    • Muscle contraction

    • Cell-to-cell binding

  • Lipids

    • Organic molecules composed mainly of carbon, hydrogen, and oxygen.

    • Fatty acids: carboxyl group, hydrocarbon chain, and a methyl group.

    • Triglycerides: three fatty acids bonded to a glycerol molecule.

    • Roles: energy storage and thermal insulation in body fat.

    • Lipids are generally hydrophobic due to long hydrocarbon chains.

  • Nucleic acids

    • Comprised of repeating units called nucleotides.

    • Each nucleotide has three components:

    • A monosaccharide (sugar)

    • A nitrogen-containing ring (nitrogenous base)

    • One or more phosphate groups

    • Nucleic acids (e.g., DNA) are important for the storage and transmission of genetic information.

  • Simple biochemical interactions in solution

    • An electrolyte is a substance that, when dissolved in water, yields a solution capable of conducting electricity.

    • The light bulb example illustrates that a solution containing many ions conducts electricity well (strong electrolyte).

    • In solvation, polar water molecules orient around ions:

    • Positive ends of water (hydrogen sides) attract negative ions (e.g., Cl⁻).

    • Negative ends of water (oxygen side) attract positive ions (e.g., Na⁺).

    • Dissociation of salts:

    • For sodium chloride in water:

      • ext{NaCl}{(s)} ightarrow ext{Na}^+{(aq)} + ext{Cl}^-_{(aq)}

    • This ionization leads to a large number of free ions and strong electrical conduction.

  • Carbon dioxide in water and carbonic acid

    • Carbon dioxide dissolves in water to form carbonic acid:

    • ext{CO}2 + ext{H}2 ext{O}
      ightleftharpoons ext{H}2 ext{CO}3

    • Carbonic acid (H₂CO₃) is a weak acid that only partially ionizes in water, making it a weak electrolyte.

    • At equilibrium, the solution contains mostly nonionized H₂CO₃ and small amounts of ions:

    • ext{H}2 ext{CO}3
      ightleftharpoons ext{H}^+ + ext{HCO}_3^-

  • Glucose in water

    • Glucose does not dissociate into ions in water; it is a nonelectrolyte.

    • Glucose contains many polar –OH groups; the oxygen bears partial negative charges and hydrogens bear partial positive charges, forming a molecular dipole.

    • Water (also polar) interacts with glucose via dipole–dipole attractions and hydrogen bonding:

    • These interactions help break glucose–glucose attractions and allow glucose to dissolve, while covalent glucose molecules remain intact.

    • By comparison, ionic compounds like NaCl dissociate into ions in solution.

  • Hydrogen bonding and dipole interactions

    • Dipole-dipole attractions occur between polar molecules (e.g., water–glucose).

    • Hydrogen bonds are a specific, strong type of dipole–dipole interaction between a hydrogen atom bonded to a highly electronegative atom (e.g., O, N) and a lone pair on another electronegative atom (often O in water or glucose).

    • These interactions contribute to solubility and the physical properties of water, glucose, and other polar molecules.

  • Enzymes: biological catalysts

    • Enzymes are proteins that speed up chemical reactions in the cell.

    • The active site is a special region whose shape fits specific substrate molecules.

    • Mechanism:

    • Substrates bind at the active site to form an enzyme–substrate (ES) complex:

      • E + S
        ightleftharpoons ES

    • The enzyme stabilizes the transition state, stresses or weakens certain chemical bonds, and promotes a chemical transformation to form a product:

      • ES
        ightarrow E + P

    • The enzyme returns to its original shape after the reaction and can catalyze additional reactions.

    • Some enzymes can catalyze two products from a single substrate, illustrating versatility in catalytic outcomes.

  • Connections to broader concepts

    • Atomic structure underpins chemical bonding, reactivity, and the formation of molecules essential for life.

    • The octet rule (valence electrons) governs the stability of atoms and the types of bonds formed.

    • Water’s polarity and hydrogen-bonding capability are central to solubility, acid-base behavior (e.g., carbonic acid), and biochemical interactions.

    • The four major biomolecule classes (carbohydrates, proteins, lipids, nucleic acids) form the basis of cellular structure and function.

    • Enzymes exemplify how protein structure determines function and how biochemical reactions are regulated in living systems.