Proteins - Protein denaturation, protein stability - Agregation proteins
11 important questions on Proteins - Protein denaturation, protein stability - Agregation proteins
What determinist of a unfolded protein starts forming aggregates?
- Protein protein interaction (hydrophobic interactions)
- Protein-solvent interactions (electrostatic interactions)
Where is the natural pI of a protein?
This is because there usually are more acids than basic amino acids present.
(Glu + Asp > Lys + Arg + His)
At this point the net charge of the proteins is 0, and therefore there is no electrostatic repulsion
Where is natural the pI of a protein?
This is because there usually are more acid then basic amino acids present.
(Glu + Asp > Lys + Arg + His)
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What happens to the pI of a sample when you hydrolyse the protein?
What happens to beta-lactoglobulin when you add salt.
When salt is added the interaction with the solvent becomes more.
This is called salting in.
Why as 0.5 NaCl a completely different value for soy glycinin?
If a typical protein is hydrolyzed. What would be the explanation of the loss of solubility at pH7?
- The highe solubility of a native protein is aa result of the fact that the pH is then far away from the from the pI. If we hydrolyse, there is not 1 pI anymore. By consequence at any pH there are some peptides that are close to their pI.
- There is exposure of hydrophobic groups upon hydrolysis. This may induce aggregation between peptides, which also decrease the solubility.
What is the effect on proteins by a short and a long period of heat treatment?
Long period of (heat) treatment: irreversible
due to
* aggregation (only irreversible if you have enough of this)
* deamidation
* destruction of residues
What does protein aggregation lead to?
- High concentration: gelation (Cys)
What is the difference between a heat set and a cold set gel?
In cold set gel you change the pH to the pI of your proteins. Now you get less soluble proteins and aggregates will be formed.
To make a gel, a space-filling three-dimensional network of clustered proteins aggregates a certain minimal protein concentration is needed. This minimal concentration can very form condition to condition. Looking to the different types of aggregates would the minimal gel concentration increase or decrease with ionic strength?
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