Currently unavailable: for new students
Degree: Biosciences (Masters) - Durham University
I am studying biological sciences at Durham University. I have always really loved science, and I hope to enthuse others with this and help them to be willing to learn. There were some topics I found challenging but eventually understood, so this will mean I am able to explain them clearly and patiently to others. I am very thorough, careful and patient, and will aim for any student to get the top marks and give them the confidence to know they can achieve. Related reading and knowledge from my degree means I can explain the subjects clearly and in a way that will be interesting and enjoyable.
My tutorial sessions
These will be guided by what you want to learn. I will start by getting to know how you like to learn, so we can have helpful and enjoyable discussions. I will use different ways of explaining topics, including use of diagrams, to help inspire you and ensure you fully understand the topic. Then I will ask challenging questions to make you think, and eventually get you to explain it to me, as the best way to understand something is to teach it! Then you should be fully confident to ace your exams!
I have been through UCAS applications for university so will be able to answer any questions about this. I took a gap year before starting at Durham, in which I had a job, did some work experience and travelled and volunteered in Australia and Moldova.
I am very organised and can manage my time well, particularly through doing my DofE Gold Award. I have worked with young people by volunteering at girl guides and a church kids’ camp. I also am a wildlife photographer and have a wildlife blog, something which has complimented my study of biology.
Contact me with a message or book a ‘Meet the Tutor Session’, both via this website. Don’t forget to tell me your subject(s), exam board and any particular topics/questions you’d like to go over.
I look forward to meeting you and having some interesting science discussions!
|Biology||A Level||£20 /hr|
|Maths||13 Plus||£18 /hr|
|Maths||11 Plus||£18 /hr|
|Before 12pm||12pm - 5pm||After 5pm|
Please get in touch for more detailed availability
Grace (Student) October 18 2016
Lisa (Parent) August 22 2016
This is quite a complicated sounding question but it is actually quite simple if you break it down! Start by writing a balanced equation for the reaction:
3H2 (g) + N2 (g) => 2NH3 (g)
Now you can see there is four molecules on the left and two on the right, which will help with the answer. It is a good habit to always write your state symbols, especially when this question mentions pressures.
Remember causing a change in the conditions of an equilibrium results in changes to get the equilibrium back to normal.
a) An increase in pressure will cause the amount of product to increase. The equilibrium will shift to the right where there are fewer molecules in order to counteract the change, and decrease the pressure.
b) The reaction is exothermic, which means it has a negative enthalpy change, ie it gives out heat. The amount of product will decrease. The equilibrium will move to the left in the endothermic direction in order to cool the reaction, so less ammonia is produced.
c) This is a bit of a trick question! Think about it: a catalyst basically speeds up a reaction. If the reaction is at equilibrium, the catalyst will simply speed up the reaction in both directions, and not have an affect on the amount of product formed, but just cause the product to be formed more quickly.see more
Break this question down into the four stages: primary, secondary, tertiary and quarternary and for each one describe the structure and what the non-covelant interactions are that hold the protein together. Make sure your sentences are clear and concise, not waffley!
There are four stages of protein folding, primary, secondary, tertiary and quarternary.
The primary structure is the sequence of amino acids held together by peptide bonds
The secondary structure is the protein beginning to fold up. It can have two types of structure: the alpha helix, a coil shape held by hydrogen bonds in the same direction as the coil. The beta pleated sheet is an S shape pattern, also with hydrogen bonds holding the structure together. The hydrogen bonds are between NH and CO groups on the peptides.
The tertiary structure is the protein folded into its precise 3D structure, relating to the functon. This is held together by a range of non-covelant interactions between side groups, including ionic interations, disuplhide bridges, hydrophobic interactions, Van der Waals forces and hydrogen bonds.
The quarternary structure is when single peptides bond to other peptides, for example in haemoglobin.see more
This might be hard at first, but if you work through step by step you'll get there!
Start by getting rid of the fraction, multiply both sides by (3x-1) to get y(3x-1) = 2(1+x)
Multiply out the brackets: 3yx-y = 2+2x. The 3yx might seem hard to sort out but leave it for the moment and it can be factorised and sorted at the end!
Put the x terms on one side (including 3yx) and the non x terms on the other: 3yx-2x = 2+y
Factorise the left side to get a single x term multiplied by everything else: x(3y-2) = 2+y
Then you simply divide both sides by (3y-2) to get
x = (2+y)/(3y-2) and thats your final answer.see more