Chapter 3: The Organic Molecules of Life

3.1 Organic Molecules

  • Organic molecules contain carbon and hydrogen; inorganic molecules do not contain a combination of carbon and hydrogen (e.g., ext{H}_2 ext{O} and ext{NaCl}).

  • Carbon atom basics:

    • Total of six electrons; four in the outer shell.

    • Almost always shares electrons with elements such as hydrogen, nitrogen, and oxygen.

    • Can bond with as many as four other elements.

    • Most often shares electrons with other carbon atoms.

  • Hydrocarbons: chains of carbon atoms bonded only to hydrogen atoms.

  • Isomers: same number and kinds of atoms (same molecular formula) but different arrangements; may have different properties.

  • When discussing isomers, several types are introduced:

    • Constitutional (structural) isomers: different connectivity.

    • Stereoisomers (spatial isomers): same connectivity, different spatial arrangement.

    • Diastereomers: stereoisomers that are not mirror images.

    • Enantiomers: non-superimposable mirror images.

    • Conformers (rotamers): different shapes due to rotation around single bonds; cis-trans isomerism is a type of stereoisomerism for double bonds.

  • Figure 3.2 highlights that carbon chains can vary in:

    • Length, presence of double bonds, and branching.

    • Carbon rings can form in different sizes and have double bonds.

  • The carbon skeleton size/shape and attached functional groups determine molecule behavior; functional groups are a key determinant of reactivity.

    • Functional group defined: a specific bonded set of atoms that imparts characteristic properties and reactions to the molecule.

    • Often use R to represent the remainder of the molecule attached to the functional group.

  • Figure 3.3: Common Functional Groups (structure and examples at a glance)

    • Hydroxyl group: structure R–OH; Found in alcohols and sugars.

    • Carboxyl group: structure R–C(=O)–OH; Found in fatty acids and amino acids.

    • Amino group: structure R–NH_2; Found in amino acids and proteins.

    • Sulfhydryl group: structure R–S–H; Found in cysteine and proteins.

    • Phosphate group: structure O ext{–}P(=O)(OH)_2 (often bound via an ester linkage); Found in ATP and nucleic acids.

    • Other notes: functional groups determine the chemical properties and reactivity of organic molecules; their presence and combination explain diversity of biomolecules.

  • 3.2 Carbohydrates and Lipids overview:

    • There are four categories of biological molecules: Carbohydrates, Lipids, Proteins, Nucleic Acids.

    • Digestion breaks these molecules into subunits to build macromolecules.

  • Building complex molecules:

    • Monomers: subunits.

    • Polymers: monomers joined together.

    • Dehydration synthesis (condensation): joins monomers to form polymers with removal of a water molecule;
      ext{Monomer} + ext{Monomer}
      ightarrow ext{Polymer} + ext{H}_2 ext{O}

    • Hydrolysis: adding water to break polymer bonds; OH from water attaches to one monomer, H attaches to the other.
      ext{Polymer} + ext{H}2 ext{O} ightarrow ext{Monomer}1 + ext{Monomer}_2

  • Monosaccharides and disaccharides and polysaccharides are the carbohydrates.

  • 3.3 Proteins and Nucleic Acids are addressed later in this unit with details on structure and function.

3.2 Carbohydrates and Lipids (in detail)

  • Carbohydrates are mainly used for immediate energy; they are enzymatically broken down to release energy used to make ATP. They can also serve structural roles (e.g., cellulose in plant cell walls).

  • Carbohydrate classification:

    • Monosaccharides: a single sugar molecule; simple sugars.

    • Disaccharides: two monosaccharides linked together.

    • Polysaccharides: long chains of monosaccharides; can be energy storage or structural.

  • Monosaccharides specifics:

    • Carbon backbone ranges from 3 to 7 carbons; general formulas vary by size.

    • Glucose: ext{C}6 ext{H}{12} ext{O}_6; two isomers—fructose and galactose.

    • Ribose: ext{C}5 ext{H}{10} ext{O}_5; found in RNA.

    • Deoxyribose: ext{C}5 ext{H}{10} ext{O}_4; found in DNA (lacks one O).

    • Glycose variants include triose (e.g., glyceraldehyde, dihydroxyacetone), pentose (e.g., ribose), and hexose (e.g., glucose).

  • Simple carbohydrate definitions:

    • Simple carbohydrates (sugars) are readily digested and provide rapid energy.

  • Monosaccharide examples and structures (brief):

    • Glyceraldehyde, dihydroxyacetone (trioses).

    • Ribose (pentose), glucose (hexose).

    • Structural diagrams depict linear and ring forms; note that sugars can cyclize to rings in solution.

  • Disaccharides:

    • Maltose: glucose–glucose; yeast fermentation for energy in beer; hydrolysis of maltose yields two glucose molecules.

    • Sucrose: glucose + fructose (table sugar).

    • Lactose: galactose + glucose.

    • General hydrolysis: disaccharide + water → two monosaccharides (e.g., maltose + water → 2 glucose).

    • Maltose fermentation: maltose + H₂O → 2 glucose; yeast fermentation converts glucose to ethanol and CO₂ (beer production).

  • Polysaccharides: many are used as energy storage molecules or structural components.

    • Plant storage: starch (amylose, amylopectin) made of α-glucose; storage in plants.

    • Animal storage: glycogen; highly branched polymer of glucose.

    • Structural roles: cellulose (plant cell walls) and chitin (exoskeletons of crustaceans and insects).

    • Most abundant organic molecule overall is cellulose; digested mainly by specific microbes.

  • Figure references summarize structure and function of starch, glycogen, and cellulose.

  • Carbohydrate structures (summary):

    • Amylose vs amylopectin in starch; branching patterns differ (1→4 vs 1→6 glycosidic bonds).

    • Glycogen is highly branched; cellulose is unbranched with parallel chains; hydrogen bonding holds cellulose chains together.

  • Lipids overview:

    • All lipids are insoluble in water; composed of long nonpolar hydrocarbon chains; low hydroxy group content; highly diverse in structure and function.

    • Primary roles: long-term energy storage; waterproofing effects on skin, hair, and feathers; membrane components (phospholipids).

  • Fats and oils are triglycerides: three fatty acids attached to glycerol.

    • Glycerol: ext{C}3 ext{H}8 ext{O}_3 with three —OH groups.

    • Fatty acid: long carbon chain with a carboxyl group at one end; general formula for saturated or unsaturated hydrocarbon chains; energy-dense molecules.

    • A triglyceride forms when the carboxyl portions of three fatty acids react with the three –OH groups of glycerol, releasing 3 H₂O in the process (dehydration synthesis).

  • Fatty acids details:

    • Unsaturated fats have double bonds in the carbon chain; fewer hydrogens than two per carbon atom.

    • Trans fats are unsaturated fats with trans orientation around the double bond.

    • Saturated fatty acids have no double bonds (fully saturated with hydrogens).

    • Examples with typical formulas (illustrative):

    • Arachidic: ext{C}{20} ext{H}{40} ext{O}_2

    • Stearic: ext{C}{18} ext{H}{36} ext{O}_2

    • Palmitic: ext{C}{16} ext{H}{32} ext{O}_2

    • Oleic: ext{C}{18} ext{H}{34} ext{O}_2

    • Linoleic: ext{C}{18} ext{H}{32} ext{O}_2

    • Common fat sources and terms shown: canola oil (unsaturated), butter (saturated).

  • Phospholipids: membrane components

    • Form the bulk of the plasma membrane.

    • One end is water-soluble (polar head); the other end is nonpolar (nonpolar tails).

    • Polar head typically includes a phosphate group; nonpolar tails are fatty acid chains connected via glycerol.

    • They form a bilayer that lines the inside and outside of the cell membrane; the inside is hydrophobic while the outside interacts with water.

    • Example components: phosphatidylcholine (PC), phosphatidylserine (PS), phosphatidylethanolamine (PE), phosphatidylinositol (PI), phosphatidylglycerol (PG), sphingomyelin, cholesterol as membrane components.

  • Steroids: four fused rings

    • Lipids made of four fused rings; no fatty acids; insoluble in water; derived from cholesterol.

    • Differ by functional groups; examples include cholesterol, testosterone, estrogen.

    • Example overview of steroid synthesis: cholesterol is converted through a series of enzyme-catalyzed steps (e.g., pregnenolone, progesterone, 17α-hydroxylase, 17,20-lyase, 3β-HSD) leading to various steroids including glucocorticoids, mineralocorticoids, and sex steroids (androgens, estrogens).

    • Cellular locations of enzymes may include mitochondria and smooth endoplasmic reticulum.

3.3 Proteins and Nucleic Acids

  • Proteins: many roles including support, metabolism, transport, defense, regulation, and motion.

  • Proteins are polymers of amino acid monomers.

    • Each amino acid has a central (α) carbon bonded to a hydrogen atom, an amino group, a carboxyl group, and a side chain (R group).

    • There are 20 standard amino acids; the R group defines the identity and properties (polar vs nonpolar, acidic/basic).

  • Amino acids and peptides:

    • Peptide: two or more amino acids covalently linked.

    • Peptide bond: formed by a dehydration reaction between amino acids.

    • Polypeptide: a chain of many amino acids joined by peptide bonds.

    • The sequence of amino acids (primary structure) determines the final three-dimensional shape and function of the protein.

  • Examples of amino acids (selected from diagrams):

    • Valine (Val): nonpolar.

    • Glutamate (Glu): ionized (negative charge at physiological pH).

    • Cysteine (Cys): nonpolar; contains a thiol group (—SH).

    • Tryptophan (Trp): nonpolar; complex ring structure.

  • Figure 3.18 Synthesis and Degradation of Peptide

    • Dehydration synthesis builds a dipeptide from two amino acids, releasing a water molecule.

    • Hydrolysis breaks a dipeptide into two amino acids by adding water.

  • Protein structure organization (levels):

    • Primary structure: amino acid sequence (polymeric chain);

    • Example sequence includes various amino acids (e.g., Val, Asn, Ala, Lys, Ser, Val, Leu, Cys, His, etc.).

    • Secondary structure: alpha helix and beta-pleated sheet; hydrogen bonds stabilize the structure.

    • Tertiary structure: overall three-dimensional globular or fibrous shape resulting from interactions among R groups (hydrophobic interactions, hydrogen bonds, ionic/salt bridges, disulfide bonds, etc.).

    • Quaternary structure: more than one polypeptide chain interact to form a functional protein.

  • Protein denaturation:

    • Denaturation is the loss of structure and function, often due to changes in pH or temperature.

    • Example: native albumin can denature under heat or chemical exposure; crosslinking (disulfide bonds) can also alter structure.

  • Nucleic Acids: DNA and RNA

    • DNA: deoxyribonucleic acid; stores genetic information.

    • RNA: ribonucleic acid; helps to make proteins.

    • Nucleotides: the monomer units of nucleic acids; composed of a phosphate group, a five-carbon sugar, and a nitrogenous base.

    • Nitrogenous bases: Adenine (A), Guanine (G), Cytosine (C), Thymine (T) in DNA; Uracil (U) replaces thymine in RNA.

    • Structure of DNA: deoxyribose sugar, nitrogenous bases, and a phosphate backbone forming a double helix; base pairing rules: A pairs with T (two hydrogen bonds), C pairs with G (three hydrogen bonds).

    • DNA structural variants: A-DNA, B-DNA, Z-DNA; distinct forms with different sugar-phosphate geometries.

    • RNA structure: single-stranded; ribose sugar; uses uracil instead of thymine; bases include A, G, C, U; backbone consists of sugar-phosphate linkages.

  • Comparing proteins and nucleic acids:

    • The sequence of bases in DNA determines the sequence of amino acids in a protein.

    • The sequence of amino acids determines a protein’s three-dimensional structure and function.

    • Small changes in the DNA can cause large changes in a protein, illustrating the tight coupling between genotype and phenotype.

    • Sickle-cell disease example: a single amino acid substitution—valine replaces glutamate at position 6 in the β-globin chain—leading to sickle-shaped red blood cells and disease phenotype.

  • Practical and real-world implications:

    • Understanding the link between DNA sequence and protein structure helps explain genetic diseases and informs approaches in medicine and biotechnology.

    • The study of nucleic acids underpins modern genetics, sequencing, and gene editing debates and ethics.

  • Ethical and philosophical notes (implicit in content):

    • Knowledge of DNA structure and sequence has profound implications for privacy, genetic testing, and potential gene therapies.

    • The ability to alter proteins and genes raises questions about safety, equity, and responsible use of biotechnology.

Summary of key formulas and notations

  • General polymerization (dehydration synthesis):

    • ext{Monomer} + ext{Monomer}
      ightarrow ext{Polymer} + ext{H}_2 ext{O}

  • Hydrolysis (bond cleavage):

    • ext{Polymer} + ext{H}2 ext{O} ightarrow ext{Monomer}1 + ext{Monomer}_2

  • Carbohydrate formulas (examples):

    • Glucose: ext{C}6 ext{H}{12} ext{O}_6

    • Ribose: ext{C}5 ext{H}{10} ext{O}_5

    • Deoxyribose: ext{C}5 ext{H}{10} ext{O}_4

    • Sucrose (disaccharide): ext{C}{12} ext{H}{22} ext{O}_{11}

  • Fatty acids and lipids (examples):

    • Saturated fatty acid: ext{C}{18} ext{H}{36} ext{O}_2

    • Unsaturated fatty acid: ext{C}{18} ext{H}{34} ext{O}_2

    • Trans fat note: trans configuration around a double bond; still unsaturated overall.

  • Lipid components (triglyceride): glycerol + three fatty acids; general glycerol formula: ext{C}3 ext{H}8 ext{O}_3

  • DNA structure and base pairing (high level):

    • Base pairs: ext{A} ext{ pairs with } ext{T}, ext{ two hydrogen bonds}

    • ext{C} ext{ pairs with } ext{G}, ext{ three hydrogen bonds}

  • Nucleotide composition (DNA vs RNA):

    • DNA sugar: deoxyribose (no 2' OH); bases A, G, C, T.

    • RNA sugar: ribose (with 2' OH); bases A, G, C, U.


Note: The above notes summarize the content from the provided transcript, including major and minor points, definitions, structures, examples, and the numerical/formula references given (formatted in LaTeX). The organization follows the lecture's order: organic molecules and isomers, carbohydrates and lipids, proteins and nucleic acids, with emphasis on structure–function relationships, biochemical processes (synthesis and hydrolysis), and real-world relevance such as energy storage and genetic information.