Disaccharides: two monosaccharides linked together (e.g., sucrose, lactose, maltose).
Polysaccharides: long chains of monosaccharides (e.g., glycogen).
Basic monosaccharides (from Page 3):
Glucose, Fructose, Galactose are isomers with the same molecular formula: C<em>6H</em>12O6.
Structural note: Monosaccharides display different arrangements but share the same formula; depicted with CH2OH groups in various orientations (illustrated on the slides).
Monosaccharides details:
They can be isomers of each other, all with formula C<em>6H</em>12O6.
Glucose, Fructose, Galactose are common examples.
Basic disaccharides (Page 4):
Sucrose = Glucose + Fructose.
Lactose = Galactose + Glucose.
Maltose = Glucose + Glucose.
Note: Each disaccharide is formed by a dehydration synthesis joining two monosaccharides.
The polysaccharide glycogen (Page 5):
Structure: polymer of glucose units.
Glycogen is highly branched, enabling rapid release of glucose when needed.
Where are the carbohydrates stored and found (Page 6):
Muscle glycogen: ~2000 kcal.
Muscle triglyceride (fat): ~4000 kcal. (Note: fats are a separate lipid store but listed here as a reference for energy storage comparison.)
Blood glucose: ~40 kcal.
Liver glycogen: ~300 kcal.
Key concepts:
Carbohydrates serve as immediate energy sources (blood glucose), quick-access energy reserves (glycogen in liver and muscle), and stored energy in fats (triglycerides) elsewhere.
Quick recap: Carbohydrates include monosaccharides, disaccharides, and polysaccharides such as glycogen; they differ in size and linkages but share common chemical fundamentals.
Lipids
Overview: A diverse group including fatty acids, triglycerides, phospholipids, glycolipids, and steroids. Hydrophobic or amphipathic properties drive their functions.
Fatty acids: saturated vs. unsaturated (Page 8).
Saturated fatty acids: no double bonds between carbon atoms (no kinks).
Unsaturated fatty acids: contain one or more double bonds; typically have cis configuration creating kinks that affect packing.
Diagrammatic note: double bonds introduce bends; saturated chains tend to be solid at room temperature, unsaturated often liquid.
Triglycerides (Page 9):
Structure: glycerol backbone + three fatty acid chains.
Formation: Dehydration synthesis links three fatty acids to glycerol; yields triglyceride and 3 H2O.
Variations in ring substituents produce diverse biological roles (membrane fluidity, hormone signaling, etc.).
Summary note: Lipids provide energy storage (triglycerides), form essential barriers and signaling molecules (phospholipids, glycolipids, steroids), and influence membrane structure and function.
Proteins
Overview: Proteins are built from amino acids linked by peptide bonds; they perform virtually all cellular functions.
Basic structure of an amino acid (Page 17):
Components: amino group (NH2), central carbon (Cα), carboxyl group (COOH), and an R group (side chain) that defines identity.
General formula: NH2−CH(R)−COOH
Peptide bond formation (Page 18):
Condensation (dehydration synthesis) reaction linking the carboxyl group of one amino acid to the amino group of the next, releasing H2O.
Example shown: Glycine (Gly) to Alanine (Ala) illustrating peptide-bond formation.
Amino acids and properties (Page 19):
Amino acids categorized by side-chain properties:
Nonpolar (hydrophobic): Gly (Gly, G); Ala (Ala, A); Val (Val, V); Leu (Leu, L); Ile (Ile, I); Pro (Pro, P); Met (Met, M); Trp (Trp, W); Phe (Phe, F); Cys (Cys, C) [note: Cys is often considered polarizable; included here as nonpolar in the slide].
Definition: The overall 3D folding of a single polypeptide chain.
Arises from interactions among R groups (side chains):
Hydrophobic interactions
Hydrogen bonds
Ionic bonds
Disulfide bridges (covalent S–S bonds between cysteine residues)
Mention of internal features such as heme units within some proteins (functional groups within tertiary structure).
Quaternary structure (Page 23):
Definition: A protein composed of more than one polypeptide chain (subunits).
Levels of protein organization (Page 23):
Primary: sequence of amino acids.
Secondary: local folding due to hydrogen bonds (alpha helix, beta-pleated sheet).
Tertiary: 3D folding due to interactions among R groups.
Quaternary: assembly of multiple polypeptide chains.
Protein chemistry and biology (Page 24):
Ligand binding can change protein shape (conformational change).
Binding can alter affinity for other ligands.
Mechanistic basis for many physiological processes and functions:
Enzyme function
Muscle contraction
Action potentials
Hormone actions
Blood clotting
Immunity
Notes on structure-function relationships:
The sequence (primary structure) directs higher-order structure and ultimately function.
Proper folding is essential for activity; misfolding can lead to dysfunction.
Nucleic Acids
Overview: The genetic material of cells; include DNA and RNA.
Subunits: Nucleotides.
Components of a nucleotide (general knowledge):
Sugar (deoxyribose in DNA; ribose in RNA)
Phosphate group
Nitrogenous base (adenine, thymine or uracil, cytosine, guanine)
Key note from transcript: Nucleic acids are composed of nucleotides, the basic building blocks for genetic information storage and transmission.
Connections, implications, and real-world relevance
Energy and metabolism:
Carbohydrates provide immediate and stored energy; glycogen provides rapid glucose release; fats store large amounts of energy in triglycerides.
Membrane biology and signaling:
Phospholipids form cell membranes (bilayers) and micelles; membrane composition influences permeability and signaling.
Steroids (cholesterol and steroid hormones) modulate membrane fluidity and regulate gene expression with hormones like estrogen and testosterone.
Protein structure-function relationships:
Sequence dictates structure; structure determines function; ligand binding can regulate activity and signaling pathways.
Protein folding underpins enzyme catalysis, transport, immune defense, and many cellular processes.
Genetic information:
Nucleic acids store and transmit genetic information through nucleotide sequences; DNA serves as the blueprint; RNA participates in decoding and expression.
Practical implications:
Understanding biomolecule structure helps in drug design, nutrition, disease mechanisms, and biotechnology applications.