School of Peptide Chemistry
Peptide Chemistry Foundations
Peptide fundamentals through mass, charge, hydrophobicity, solubility, and amphipathic behavior.
10 lessons
Learning Objectives
- Define peptides and amino-acid building blocks
- Explain peptide-bond formation and primary structure
- Describe higher-order structure concepts
- Calculate and interpret peptide molecular weight
- Relate charge, hydrophobicity, solubility, and amphipathic behavior
Lesson order
1 of 15 · 22–28 min · Beginner
What Is a Peptide?An evidence-based introduction to peptides, amino acids, peptide bonds, sequence, structure, and the differences among peptides, polypeptides, and proteins.
2 of 15 · 30–38 min · Beginner–Intermediate
Amino Acids: Structure, Classification, and Chemical BehaviorA detailed guide to amino-acid structure, side-chain classes, stereochemistry, ionization, and the chemical features that shape peptide behavior.
3 of 15 · 28–34 min · Intermediate
Peptide Bonds: Formation, Geometry, and Chemical StabilityAn in-depth explanation of peptide-bond formation, resonance, planarity, cis-trans behavior, hydrolysis, and analytical implications.
4 of 15 · 26–32 min · Intermediate
Primary Structure: How Sequence Defines Peptide IdentityA technical guide to peptide sequence, residue numbering, terminal modifications, sequence variants, molecular mass, and identity confirmation.
5 of 15 · 30–38 min · Intermediate–Advanced
Higher-Order Peptide StructureAn accessible technical guide to peptide conformation, alpha helices, beta structures, turns, disorder, cyclization, aggregation, and structural analysis.
6 of 15 · 26–32 min · Intermediate
Peptide Molecular Weight and Mass CalculationLearn how peptide molecular weight is calculated, why monoisotopic and average mass differ, and how termini, disulfides, salts, and modifications affect expected mass.
7 of 15 · 28–34 min · Intermediate
Peptide Charge, pKa, and Isoelectric PointUnderstand how ionizable groups, pH, pKa, and isoelectric point determine peptide charge, solubility, electrophoretic behavior, and analytical performance.
8 of 15 · 26–32 min · Intermediate
Peptide Hydrophobicity and Molecular InteractionsExplore how residue composition, sequence, solvent exposure, and conformation control peptide hydrophobicity, reversed-phase retention, aggregation, and surface adsorption.
9 of 15 · 32–40 min · Intermediate–Advanced
Peptide Solubility: Chemical Drivers and Analytical ConsiderationsLearn how pH, charge, hydrophobicity, concentration, ionic strength, temperature, and physical state determine peptide solubility and analytical recovery.
10 of 15 · 28–36 min · Intermediate–Advanced
Amphipathic Peptides and Interfacial BehaviorUnderstand how peptides containing distinct hydrophobic and hydrophilic regions interact with water, membranes, interfaces, chromatographic systems, and one another.