Proteins

What you will learn

• Relate the four levels of protein structure to the bonds that stabilize them.
• Distinguish the main protein classes and their physicochemical properties.
• Describe a strategy for purifying, analysing, and sequencing a protein.

Course outline

1. Entering the world of proteins

   Connecting sequence, folding, function, and study methods.

   10 min

2. Functions and synthesis: from information to activity

   Studying the major protein roles and the steps that produce an active protein separately.

   16 min

3. Primary structure: reading and writing a protein

   Defining sequence, direction, codes, and biological significance.

   14 min

4. Secondary structure: building local motifs

   Studying the α-helix, β-sheets, and β-turn separately.

   20 min

5. From tertiary folding to quaternary assembly

   Studying each stabilising force, domains, dynamics, and subunits.

   26 min

6. Classifying proteins and understanding fibrous architectures

   Separating composition, shape, collagen, and keratin to understand each criterion.

   24 min

7. Physicochemical properties and denaturation

   Separately connecting mass, light, viscosity, charge, solubility, and loss of conformation.

   28 min

8. Detecting, separating, and purifying proteins

   Choosing a method according to colour, recognition, density, size, charge, or affinity.

   34 min

9. Preparing a protein and identifying its termini

   Isolate the chains, determine their composition, then identify the N- and C-terminal residues.

   32 min

10. Fragmenting, reading and reconstructing a sequence

    Produce complementary fragments, sequence them, then recover chain order and disulfide bridges.

    38 min