Proteins are sequences of amino acids joined by peptidelinks.
When 2 amino acids join together, it is a dipeptide.
When 3 amino acids join together, it is a tripeptide.
When many amino acids join together, it is a protein or polypeptide.
Formation of a protein= Condensation reaction= Two amino acids are joined together, linked through a peptide link, one molecule of water is released.
Destruction of a protein= Hydrolysis reaction= Peptide link is broken between two amino acids, requires one molecule of water.
A) Amino acid
B) Amino acid
C) Condensation
D) Hydrolysis
E) Dipeptide
F) Peptide link
2 different amino acids can join to form 2different dipeptides:
Proteins, polypeptides, dipeptides and tripeptides can all be hydrolysed back into their constituent amino acids. This can be done using an acid or alkaline catalyst.
Acidic hydrolysis:
Conditions - 6 mol dm-3 HCl, reflux 24 hours:
Produces an alkyl ammonium salt.
Alkali hydrolysis:
Conditions - Solution of aqueous NaOH, heated above 100 degrees.
Produces an carboxylate salt.
Structure of proteins:
Primary structure - Sequence of aminoacids joined by peptide links.
Secondary structure - Hydrogen bonds form between peptide links. This causes the amino acid sequence of coil, into an alphahelix, or fold, into a beta-pleated sheet.
Tertiary structure- The secondary structure folds and coils on itself to give a 3-dimensional structure. Additional bonds and intermolecular forces hold the polypeptide or protein in this shape.
Additional bonds and intermolecular forces:
VanderWaals’forces of attraction, these form between the alkyl R side groups
Hydrogenbonds, these form between OH / NH / C=O in the R side groups and the main chain. They stabilise and provide support for the secondary structure.
Ionicbonds, form between COO- and NH3+ in the R side group.
Disulphidebonds (sulphur – sulphur bonds), formed between cysteine residues. They stabilise the protein.