Protein Bonds In Protein Structure Flashcards
Which bonds maintain protein primary structure?
Covalent peptide bonds
Which bonds maintain protein secondary structure?
Hydrogen bonds
Which bonds maintain protein tertiary and quaternary structure?
- Covalent disulphide
- Ionic
- H bonds
- Van der Walls
- Hydrophobic
What are disulphide bonds and in which proteins are they commonly found?
- Strongest (214 kJ/mol)
- Formed between Cys residues: lose 2H+ and 2e- (from -SH -SH to -S -S).
- Limits protein folding but helps maintain structure.
- Present mainly in proteins that are secreted or in hostile environment (e.g. Ribonuclease in the gut)
What can disulphide bonds be broken by?
Reducing agents, e.g. Beta-mercaptoethanol.
What are electrostatic interactions?
- Relatively weak, 10-30 kJ/mol
- Formed between charged groups (salt bridges), e.g. Glu-, Asp- and Arg+, Lys+
What are hydrogen bonds?
- Polarised, 10-30 kJ/mol
- Formed between an electronegative atom and a hydrogen bound to another electronegative atom.
What is the hydrophobic effect?
- ~10kJ/mol
- Interaction between hydrophobic side chains due to displacement of water.
What are van dear Wales forces?
- 4 kJ/mol
- dipole-dipole interactions
- Important when surfaces of 2 large molecules come together.
What is protein denaturation?
- Disruption of protein structure due to breaking of forces holding proteins.
- E.g. Heat increases vibrational energy
pH alters ionisation state of aa and changes ionic/H bonds
Organic solvents disrupt hydrophobic interactions
Describe the process of protein folding.
- Ordered process (or would take too long)
- Each step involves localised folding with stable conformations maintained
- Driven by need to find most stable conformation.
Name diseases caused by protein misfolding.
- AMYLOIDOSES involve amyloid fibres
- misfolded, insoluble form of normally soluble protein
- highly ordered with a high degree of beta-sheet
E.g. Alzheimer’s, T2 diabetes, Parkinson’s, Spongiform encephalopathies