Proteins and Water
Amino acids (H₂N–CHR–COOH) join by condensation into peptide bonds. Primary structure: amino acid sequence. Secondary: α-helix or β-pleated sheet held by hydrogen bonds between C=O and N–H. Tertiary: further folding held by hydrogen, ionic and disulfide bonds and hydrophobic interactions between R groups. Quaternary: more than one polypeptide (and maybe a prosthetic group). Globular proteins (e.g. haemoglobin: 4 chains, haem with Fe²⁺, hydrophilic outside) are soluble and metabolic; fibrous proteins (e.g. collagen: three chains in a triple helix, glycine every third residue, cross-links) are insoluble and structural. Biuret test: purple. Water is polar; hydrogen bonding gives it high specific heat capacity, high latent heat of vaporisation, cohesion and solvent properties.
Learning objectives
- Describe the four levels of protein structure and their bonds.
- Compare haemoglobin and collagen.
- Carry out the biuret test.
- Explain the properties of water.
Sickle cell anaemia is caused by one amino acid change in haemoglobin. How can one change matter so much?
Core idea
A protein is just a chain until it folds. Get the fold wrong and it can't do its job.
The amino acid sequence decides how a protein folds; bonds between R groups hold the 3D shape. Water's hydrogen bonds give it the properties life needs.
Each level depends on the one before.
How many different tripeptides are possible from 20 amino acids?
- Goal
- Number.
- Strategy
- 20 choices at each position.
- Three positions.
- Multiply.
Summary
- Primary → quaternary.
- Haemoglobin globular; collagen fibrous.
- Biuret purple.
- Peptide bond
- Bond between amino acids formed by condensation.
- Prosthetic group
- Non-protein part attached to a protein, e.g. haem.
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