Hypothesis for denaturation of egg albumen

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#1
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#1
After reading through most of the biology threads ive begun my write up.

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.
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how about
'....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
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snake_n_shades
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don't hypothesise until after you've done some preliminary work and then you'll have some data to use
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At4798
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i'm prolly not right...but i wrote the copper sulphate is alkaline and the albumen needs to be neutral as it contains the nutrients for the embryo in the egg....proteins are denatured when it is the wrong pH
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Hayley
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CuSO4 does not alter the pH it acts with the positively charged ionic bonds
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At4798
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i dont understand all that....o well...i'll hafta resign myself to a retake in jan...thanks anyway
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Hayley
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The reason why albumin denatures has nothing to do with pH, temperature or anything like that...
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.
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At4798
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thanks Hayley...i think i get it now. im just not into all the chemistry bit of biology, but thanks, it made sense
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Originally posted by Hayley
These ions neutralize the charge on the R groups so that the R groups no longer bind to each other.
do u not reckon that the Copper sulphate forms complexes with protein molecules instead, seeing as its 2+ charge allowsit to bind to protein n all, that means that more than 1 protein can bind to the copper - so u get a complex and an opaque solution
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snake_n_shades
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#10
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i _think_ that its the case that the copper ions bond to the R groups instead of the R groups binding to themselves, so the protein denatures and becomes a fibrous protein instead of a globular one
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There is no need for a hypothesis for this biology planning so dont worry about it, all you need to say really is that copper(ll)sulphate denatures egg albumen. Or you could make a null hypothesis where you say something like "copper (ll) sulphate does not denature egg albumen" and you can prove that your wrong.
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