Molecules, polarity, and hydrogen bonds. Examples: Water and carboxylic acid.

Hydrophobicity (dislike of water) of non-polar long carbon chains and hydrophilicity (like of water) of polar molecules. Behavior of amphipathic molecules such as phospholipid bilayer, micelle, and vesicles.

Hydrogen bond and electrostatic interactions between carboxylic (COO-) and amine (NH₂) groups. Van der Waals interaction between uncharged, non-polar molecules.

Synthesis and properties of lipid. Permeability of phospholipid bilayer membranes to ions, water, gases, and amino acids. Membrane as a barrier to create concentration gradients on the outside and inside of the cell.

Name, composition, synthesis, and hydrolysis. Alternate structures and linkages of cyclic carbohydrates. Examples: Glucose, fructose, galactose, and lactose.

Synthesis of glycogen, cellulose, and polysaccharides from monomers.

Transmembrane portions of proteins consist of hydrophobic amino acids so they can interact with the hydrophobic tails of phospholipids in the membrane. All charged side chains must be neutralized by opposite charges.

Chemical alterations are made to the protein after translation.

Atomic and molecular composition of cells. Four classes of macromolecules-proteins, DNA/RNA, carbohydrates, and lipids.

Description, length, strength, and examples. Forming and breaking of bonds; ability to rotate, stretch, and bend without breaking; single, double, and triple bonds and saturation.

Carbon as a chiral center with four attached groups. Mirror images.

General formula, 3D structure (linear and cyclic), linkage, and examples. Synthesis/polymerization and hydrolysis of disaccharides and polysaccharides.

Nucleotide structure and components-sugar, phosphate group, and bases. Formation of DNA/RNA from monomeric nucleotides through phosphodiester bonds. Hydrogen bonds and base pairing results in the double helical structure of DNA.

Formation and properties of the peptide bond. Side chains of amino acid with unique properties-positive and negative charges, polar and non-polar, hydrophobic and hydrophilic. Special cases-glycine, cysteine, and proline.

Primary (amino acid sequence) and secondary (alpha helix and beta sheets) structures. Hydrogen bonds are important in secondary structures.

Transfer of electrons result in ionic bonds between positively and negatively charged atoms. Transient polarity in non polar bonds result in VDW interactions. VDW interactions are weak with short ranges. Example: geckos.

Hydrophobic amino acids tend to congregate and stay away from water.

Primary (amino acid sequence) and secondary (alpha helix and beta sheets) structures. Hydrogen bonds are important in secondary structures.

Ionic, van der Waals, and hydrophobic interactions are responsible for the tertiary structure, the association between various parts of the protein.

Interactions between polypeptide subunits form the quaternary structure. Movie of a protein dimer.

Proteins as enzymes/catalysts, structures, antibodies/immune responses, motors and machines. Movie on protein motors.

Definition, structure and synthesis. Saturated versus unsaturated fat. Structure, formation, amphipathic properties, and permeability of phospholipid bilayers as the cell membrane and barrier. Movie of transmembrane protein.

Synthesis of glycogen, cellulose, and polysaccharides as polymers from monomers. Storage of glucose and energy in long chains of glycogen.

Charges and structure of amino acids with carboxyl, amino groups, and side chains. Formation of peptide bonds during protein synthesis.

Side chains of each of the 20 amino acids unique biochemical properties-- polar versus non-polar, hydrophilic versus hydrophobic, and positive and negative charges. A brief list of individual amino acid and behavior

Primary, secondary, tertiary and quaternary structures of proteins. Hydrogen bonds as the main force in the secondary structure (alpha-helices and beta-sheets).

Primary, secondary, tertiary and quaternary structures of proteins. Hydrogen bonds as the main force in the secondary structure (alpha-helices and beta-sheets).

Overview of catalytic functions of proteins that speed up biochemical reactions and structural functions of proteins in the cell.

A brief exploration of the temperature-sensitive nature of biological processes.

Definition and description of macromolecules, polymers, bonds and bond types, condensation and hydrolysis reactions, and the four major types of macromolecules/polymers.

Description of lipids and their chemistry.

Description of carbohydrates and their chemistry.

Introduction to nucleic acids, the four bases, and a brief look at their chemistry and importance.

Biochemical forces that drive all molecular interaction in biology.

Structures, linkages, and names of mono-, di-, and polysaccharides.

Structures and names of the components of nucleotides-deoxyribose and ribose, and pyridimine and purine nitrogenous bases.

Structures of amino acids grouped based on side chain properties. Polymerization of amino acids to form peptide bonds and proteins.

Structures and names of various lipids and phospholipids.

Chemical interactions between an enzyme and a substrate in its binding pocket.

Solution (PDF)^#

Using hemoglobin as an example to illustrate different levels of protein structure and how mutations can affect each level.

Solution (PDF)

Strength of molecular interactions and boiling points.

Solution (PDF)

Various types of chemical interactions and their relevance in enzyme-substrate interactions. Uses substrate analogs to demonstrate the importance of chemical interactions.

Solution (PDF)

Structure and functions of proteins and other macromolecules.

Solution (PDF)

Chemical bonds and interactions in biological molecules.

Solution (PDF)

Chemical interactions between amino acids on a proteins and its substrate, GDP.

Properties of the phospholipid bilayer and transmembrane proteins. Tertiary and quaternary structures of proteins involving multiple subunits.

Solution (PDF)

Small molecule-protein interaction based on amino acid residues in the protein binding pocket.

Solution (PDF)

Properties of the phospholipid bilayer and transmembrane proteins. Secondary, tertiary and quaternary structures of proteins involving multiple subunits.