L11 Protein Structure Flashcards
What are proteins made of?
Proteins are polymers of amino acids linked by peptide bonds.
What is a peptide bond?
A bond formed by condensation between the α-amino group and carboxyl group of two amino acids.
Name the four levels of protein structure.
Primary (sequence), Secondary (α-helix/β-sheet), Tertiary (3D shape), Quaternary (multi-chain arrangement).
What interactions stabilise protein folding?
H bonds, ionic bonds, hydrophobic interactions, Van der Waals forces, disulfide bonds.
What is the difference between α-helix and β-sheet?
α-helix: Coiled, H bonds between n & n+4.
β-sheet: Flat/twisted, strands are parallel or anti-parallel.
What is protein denaturation?
Loss of 3D structure and function due to heat, pH, detergents.
What is a protein domain?
An independently folding unit often linked to specific functions.
How do proteins recognise other molecules?
Via multiple weak interactions: H bonds, ionic bonds, hydrophobic interactions.
Give an example of a structural protein.
Collagen (connective tissue) or Keratin (hair, skin).
Give an example of a transport protein.
Haemoglobin (O₂ transport) or Porin (membrane channel).
What is de novo protein design used for?
Vaccines, enzyme therapies, drug development, sustainability.