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Denaturation of Egg Albumen.

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Alex Payne Biology Planning Exercise Denaturation of Egg Albumen Aim: The aim of this experiment is to determine the lowest concentration of copper (II) sulphate solution that brings about full denaturation of egg albumen at room temperature. Biological Knowledge: Egg albumen is a protein that is the make up of egg whites. Proteins are made up of many amino acids in chains. The chains are in very complex arrangements and this determines the function of the protein. The arrangement of the proteins can be separated into four levels: StructurePropertiesPrimaryThis is the chain of amino acids held together by peptide bonds.SecondaryThis is the regularly occurring patterns such as alpha - helixes, held together by hydrogen bonds.TertiaryHow the secondary structure affects the overall shape of the protein.QuaternaryThis is determined by the protein chains. The proteins function is determined by these four structures. When the structure is altered it can either change it's function or it can make the protein ineffective. When a protein is made ineffective it is denatured. Changing the structure of any of the four levels can denature a protein, this is when the protein is unfolded or folded incorrectly. Some times they can be renatured by reversing the effects but not very often. ...read more.


I did a simple colorimeter experiment on the effect of the copper (II) sulphate on the light transmission through the albumen. I measured the light transmission after using the copper (II) sulphate as a standard. Here are the results: All to 5ml of albumen and 10ml of copper sulphate solution: Concentration of copper (II) sulphate (mol dm-3)Light Transmission (%)0.110.07510.0520.02520.01380.005560.0025640.0100 From this I can see that from 0.025 mol dm-3 to 0.0 mol dm-3 would be a good range, with 0.0025 mol dm-3 intervals, as this will include the lowest concentration of copper (II) sulphate at which full denaturation occurs. Hypothesis: From my background knowledge I predict that these will be a concentration of copper (II) sulphate that will be the minimum to bring about full denaturation. This is because it will have the corresponding amount of copper ions to the amount of peptide bonds that need to be altered for all the albumen to be denatured. From my preliminary results I can see that this point will around 0.0175mol dm-3. I predict that as the concentration of copper (II) solution increases the speed and the extent of concentration will rise. Thus the amount of light transmitted through the albumen will decrease with the concentration. ...read more.


The more opaque it is the less light transmitted. * Put 0.025 mol dm-3 concentration copper sulphate into the first test tube. Lightly shake it until there is no more activity. Pour carefully into cuvettes holding cuvettes on dull side as not to affect light transmission. * Put into colorimeter and get a reading of the light transmission. Note this in table. * Repeat process for each concentration three times. * The control is the distilled water on its own as it shows that the copper sulphate is responsible. * From the graph find the lowest concentration needed to complete denaturation. Risk Assessment: Go by all of the usual biological lab rules i.e. wear goggles and wear protective clothing. The only dangerous substance we are using is carbon (II) sulphate, it is very dangerous to swallow. Results: The table will be as so: Concentration of copper (II) sulphate (mol dm-3) LightTransmission(%) 0.0 0.0025 1.0 0.005 2.0 0.0075 3.0 0.01 4.0 0.0125 5.0 0.015 6.0 0.0175 7.0 0.02 8.0 0.0225 9.0 0.025 The graphs axis will be as so: I will use the graph to find the minimum concentration needed. This will be done my drawing a best-fit line then reading off at a point where there is very little transmission. ...read more.

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