Hypothesis for denaturation of egg albumenWatch
I have made a hypothesis that states that the albumen is denatured at 0.03 dm mols. However I need a because and havent a clue what to put. How do i justify this? does anyone know. Why would it be denatured at this point or why wouldn't it?
I do need a hypothesis, im on AQA and my teacher says i need it.
im glad this site is here, its really helpful. Thanx to everyone who has posted especially the uni students.
'....because after this point the solution is too weak to fully denature the egg albumen.....'
just a suggestion, I haven't even started writting it up yet!
Any help always welcome!
Good Luck everyone, EJ
Egg Albumen is a globular protein held together by interaction between R groups.
Some of the bonds between R groups are Ionic, i.e. a positively charged R group is attracted to a negatively charged R group and the force of attraction holds the shape of the protein.
Copper sulphate dissociates into Ions in solution. These Ions are also attracted to the charged R groups. The positive Copper ions are attracted to negative R groups, the Sulphate ions to the positive R groups.
These ions neutralize the charge on the R groups so that the R groups no longer bind to each other. This makes the protein uncoil into long strands. Some of the bonds in the protein strand are polar, slightly charged at one end.
H groups are slightly positive, and become attracted to the slightly negative O end of OH groups. As the protein has uncoiled the H and OH groups are free to line up.
The resulting hydrogen bonds cause the molecules to stick together. It is this more compact, regular arrangement of molecules that makes the albumen white.
Instead of using a colorimeter you can compare the amount of albumin that has been denatured with a solution that is obviously denatured for example 0.1 concentration of copper sulphate should be enough.
These ions neutralize the charge on the R groups so that the R groups no longer bind to each other.