Covers the organization of the course, protein structure, molecular interactions, and the significance of pH and functional groups.
Explores hydropathicity, amino acids, and their interaction with water, including measuring hydrophobicity and properties of common amino acids.
Explains chromatography principles for protein purification, covering peak broadening causes, band broadening components, and common stationary phases.
Explores the primary, secondary, tertiary, and quaternary structures of proteins and the interactions between amino acid side chains.
