What concentration of copper (II) sulphate brings full denaturation of egg albumen.

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Helen Spencer, candidate number: 9326, centre number: 55245

Biology Practical Examination: Planning Exercise

Introduction

This investigation is to find out what the concentration is of copper (II) sulphate that brings full denaturation of egg albumen. I can find this out by decreasing the concentration of CuSO4 using the serial dilution method to up the diluted state that no longer gets fully denatured.

Background Information

Egg albumen is a protein and can also be denatured by heat, pH and mechanical methods, so to make this experiment fair, I need to try and make sure that these factors don’t affect the experiment.

Denaturation of a protein is the breaking of bonds that hold the protein molecules together; in this case CuSO4 is being used to break the bonds. The bonds that are being broken and changed are disulphide and hydrogen bonds. The R groups on the amino acids in the proteins are responsible for the 3D shapes of the protein molecules and their functions, and they are what get changed when the protein is denatured, so when denatured, it ceases to function properly.

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CuSO4 denatures the protein, because within it, it has Cu  ions. These break the hydrogen and disulphide bonds, because they both have δ- and δ+ charges and the δ- charges are attracted to copper ions. The copper sulphate is therefore breaking the bonds, changing the structure of the protein and denaturing it.

To measure the opaqueness of the albumen in the different concentrations of copper sulphate, I could put a cross on a piece of paper and put it underneath a beaker with the egg albumen and solution in. If the albumen is completely denatured, I shouldn’t be able to ...

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