all this bout ions denaturing the protein......am i right in thinking that they break down the H-bonds that keep the protein in shape?
They interfere with the Ionic attraction between some R groups, by neutralising the charge.
And to get around the distribution for th colorimeter, blend it first. simple.
All of this has been a lot of help, thanks to everyone who has posted on here.
I think that I know what I am doing but I'm not entirely sure what I should write for my hypothesis; I already know that the egg albumen is going to denature and so I am unsure as to what I am supposed to be mentioning. I haven't got any information which could suggest that the concentration that I am looking for is between 0.02 and 0.04.
Can someone please help, I've got to hand this in in a coupla days and I also have a german speaking test on the same day so I'm struggling to juggle revision and this.
Tbh can't you just blend it up to get an even dispersion? realistically this is the best way to do it in a school lab
That was perhaps a little harsh... 3hrs for an a-level exam, of which you had far fewer, and of course some of us do appreciate the concept of a social life, you know leaving the house... you're prolly a heineken drinker anyway.
Just put your preliminary work results in, then make a hypothesis based on those.........just say that you used your preliminary work to allow you to form a hypothesis.
And lay off her, there's still a lot of work involved in a-levels and its very easy to get overwhelmed by it all
It doesn't matter what the characteristics of the CuSO4 compound are! That's completely irrelevant! I think people are getting confused; although it is useful to have this kind of background knowledge it's stupid to spend all you time trying to understand the complex chemistry behind denaturisation. What is important is that your method is sound and that you have a way of getting good, accurate results. Keep everything the same apart from the concentration of the copper sulphate, make sure you take repeats and make sure your method works!
That's got to be simpler than trying to understand the chemistry behind it, when we only have ten days to complete it!!
This site is great. All the posts have been a great help to me. However the one criticising that girl was not necessary. Everyone copes with stress differently and I understand how she can be stressing coz i've got my history exam the day before the practical. But newayz good luck to everyone.
what could i put for my pridiction?
do a prediction based on your preliminary work if you did any, or otherwise i can't think of anythin except guessing!!
for everyone who hasn't managed to do any preliminary work for whatever reason, you can do this at home. you can buy copper suphate from chemist's shops i think, otherwise toy shops with science kits!
talk to your chemistry staff about the concentrations needed to get 0.1 mol.dm-3 CuSO4, its 294 g /litre to get 1 molar solution from the stuff we've got at school if that helps
guys if u don't want to use a calorimeter, u could always try drawing a cross on a piece of paper placing the solution in a beaker for each different conc. over the cross and time with a stopwatch how long the cross takes to completely disappear.
it works as well as the calorimeter!
i don't think timing is an issue here, its the final opacity that indicates the level of denaturation..... 0.01 mol.dm-3 will never totally denature the albumen if its in equal quantities
using a cross on a piece of paper is a good idea though, just judge whether you can see it or not
what could i put 4 independant varibles & (dependant)?
Hi does anybody know what protein structure the egg albumen is?
For example is tertiary, quaternary or globular.
And in the experiment what are the controls and variables?
Please can someone help
albumen's secondary and tertiary structure makes it globular.........the hydrophobic groups move inwards and the hydrophillic ones move outwards making it globular. when its denatured it becomes a fibrous protein
it doesnt have a quarternary structure