Proteins - Protein interactions
19 important questions on Proteins - Protein interactions
What are the AA contributing to the hydrophobic interactions?
- Phenylalanine (PHE)
- Tryptophan(TRP)
How can disulfide bonds be broken?
They can be broken trough:
- beta elimination: occurs during extended heating at higher temperatures at pH >8.
- Reducing agents such as DTT or beta-mercaptoethanol.
What is the clathrate structure?
This water in this low energy stat is called clathrate structure
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From what comes the hydrophobic interaction energy?
What conditions will increase or decrease the hydrophobic interaction?
So if the hydrogen bonds become less strong the hydrophobic interaction will also become less strong.
So increase temperature and organic solutions will decrease the hydrophobic interactions.
What does SDS do to the hydrophobic interactions?
What can urea do the the hydrophobic interaction?
Chinees and french people start to switch to talking english.
Will there be aggregation of you have proteins with urea?
How is the folded stat of a globular protein changed by organic solutes (urea)?
What is the molar ratio between Urea and water in a 10M urea solution?
- Water has Mw=18 g/mol.
- One liter water weights 1000g.
- So 1000/18=55.6 mol in 1 liter water
- We hav 10M urea
- So we have a ratio of 1 mol urea for 5 mols of water
What happens to the proteins if you change the pH to the IEP and then go to a high pH.
When you move away form the IEP they will start so soluble agian because the charge gets back.
What happens to the interaction potential of proteins when you change the pH?
What happens to the interaction potential of proteins when you change the salt concentration that you add?
The charge of the protein does not change. It is screened.
If you consider the effect of NaCl on the electrostatic interactons discussed in the previous parts. Why is it then plausible to assume that the ammonium sulfate precipitation (between 3-6M) is not due to electrostatic effects?
So this is more the salting out effect.
What is the salting out effect?
What is the slating in effect?
How can water bonds be broken by high temperature?
What is the main difference in graph between pH and salt effect on protein interaction potential at different distances?
With pH this is not the cause because you change the charge of the protein it self
What are the stabalizing forces for secondary, tertiary and quanternary structure?
- alfa-helix: within helix
- beta-sheet: between different strands
- beta-turn: within strand
Tertiary structure:
- Electrostatic attractions
- Hydrophobic interactions
- Disulfide bonds
- van der Waals interactions
Quaternary structure:
- Electrostatic attraction
- Hydrophobic interactions
- Disulfide bonds
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