Hello. My name is Rob Gilbert, and I'm the Biochemistry tutor here at Magdalen college. And today we're going to be showing you what it's like being interviewed for, Biochemistry in Oxford. Of course, every interview is a bit different, but, in general, interviews will follow the kind of pattern that that this one will. They will usually begin with a bit of a conversation about the interest that the candidate has in the subject and the subject of Biochemistry in this case, and then, building on that, we may discuss some of the things that are mentioned by the candidate or, or they might have been mentioned in their in the UCAS personal statement about what is drawing them to apply to Biochemistry. Then after that, that beginning of the conversation based on the information really that the candidate can provide, then we move into asking some questions. But these questions are not questions that we expect people to know all the answers to. It's really about setting up a conversation.


And in fact, the idea of an interview is, is to mimic a little bit, like the experience of having a tutorial where there's material to be discussed, there’s material to be agreed on. There are problems to be solved. And, and that process enables the candidate then to show us their interest in Biochemistry and their aptitude, for studying the course here at Oxford.

So it's very much about enabling a student to show us what they're good at, to tell us about their enthusiasm for Biochemistry. And also to, to draw out from them, the ability to solve problems or to deal with new information that we might give them.

Normally an interview, would have, at least two people in it. For the purposes of our demonstration today. It's just me going to be talking to one of our current Biochemistry undergraduates who will be taking on the role of the interviewee in this case, but normally there'll be at least two people in any interview.

And it's worth saying that, for Biochemistry, every candidate gets interviewed in two different colleges. So there's two completely different sets of people assessing candidates. And that's important to the objectivity and the collective decision making of the process

So now I'd like to introduce Kian, who has very kindly agreed to be our interview subject today.

Kian and is a current Biochemistry undergraduate. Now we're going to switch into, he and myself talking as if, as if, we were, undertaking an interview for the Biochemistry course here.

So, Kian, thank you very much for coming to see us today.

It's great to have you. And, I hope you’re okay. Are you, are you comfortable there for the interview? Is that okay? Yeah. Okay. Fine. Okay. Glass of water. Very good, very good. Okay. And can I check, have you got a piece of paper and a pen?
Pencil. Pencil or a pen.

Brilliant, brilliant. Okay, so it won't surprise you, Kian, for me to begin by just asking you to tell us a little bit about why Biochemistry is a subject that you would like to study you think at university. You could have, you know, applied for a number of different courses. You could have applied for, Medicine, Biomedical Sciences, Chemistry. So why Biochemistry?

Why, why that course? I think for me personally, I think the reason why I've chosen to study, and apply for Biochemistry is that I'm really interested in the molecular mechanisms. So I think the course like medicine was very focused on, you know, treatments and, doing like, actually treating patients. But I'm quite interested in, you know, research and trying to understand mechanisms behind, you know, a disease and cancer and understanding how our cells work.

I think Biochemistry specifically because I much prefer cell biology. So I much prefer looking at individual cells and how different things work inside of a cell, as opposed to looking at a multi cell or a whole organism scale.


Are there any particular mechanisms that you've come across that you think, you've really thought, wow, that's, you know, amazing. I never thought things could be that well controlled, or?

I think probably from what I've been looking at, I think the most interesting would be, the cell cycle, because I think it's such an intricately, finely tuned process where you've got multiple different cyclins and how they are in a process where you've got one being produced and the production leading to the destruction of another.

And it's sort of such a fine tuned process where you've got so many different kinases being activated and deactivated. And then the activation of different ubiquitin ligases to degrade other ones. I think it's, it's a really interesting process. Okay. So tell me a little bit about that. So these, these kinases so these cyclin dependent kinases, what, you know, how do they kind of regulate the process?

I mean, because you want to kind of link the cell cycle together with DNA replication as well, don't you? And make sure that kind of the cell doesn't divide until you've made a new, new copy of your DNA. So what, how, how is it all tied together, you know, how do those proteins relate? The ones you mentioned, the different, because you mentioned some different proteins.


You mentioned cyclins and kinases, you mentioned ubiquitin. Ubiquitin as well. So say a little bit for me about how that all interrelates and what's going on. Well, so during the cell cycle, at like the start of the, the process for cell division, you need to have some sort of, like growth factor to bind to your cell receptors and to trigger the pathway, which then leads to the activation of cell division.

So that's quite an important part of regulation of a process, which is that you need enough signal to activate downstream kinases to increase the transcription of the first, like cyclin, which is CDK, sorry which is cyclin D, and then once you've got that being produced, the CDK, which is activated by cyclin B, so CDK four or CDK six.


It forms a complex with the cyclins. And then this complex is then able to, phosphorylate different transcription factors. So that's I guess a key part there is that you you have to have a growth signal to produce the cyclins in the first place. But then during cell division, I think you've got, I'd say like for me, what I think the most interesting part of regulation is, is to make sure that you've got - you said about the DNA replication being finished -
and this is, I think it's quite interesting, but I'd say what's more interesting which I can remember better would be the regulation of the actual mitotic chromosomes. So like during mitosis you have to make sure they're lined up along the centre, the centre of your cell before they then start dividing, because otherwise, if they're not lined up properly you can lead to, you know, incorrect segregation and, cells with more or fewer or incorrect amount of chromosomes.

So, I think the interesting thing about how that's regulated would be that you've got this sort of this complex which is being produced by the CDK cyclin, which is active then. So the CDK cyclin B produces a sort of complex which prevents its own inhibition. So although it activates the APC, APC and C, which is a ubiquitin ligase, it also produces stuff which, helps deactivate it.

So, when the kinetochores aren't bound, this inhibitory complex binds to the APC and C and prevents it from degrading cyclin B. So you've got this really fine tuning of until this, until this, all the kinetochores are attached. You're still producing enough of this inhibitory complex to the cyclin B degradation to really time it such that you only destroy it once the cell cycle has correctly lined up the the, the chromosomes.

Okay, okay. Thank you. That's a huge amount of detail. Thank you, thank you. So, now, on your piece of paper, could you possibly draw me a molecule of benzene? I what? You mentioned receptors. I want to come back to the question of receptors in a minute, but let's talk about a little bit of basic chemistry.

You've done some chemistry. It's cool. Yeah? Yeah. Yeah. So could you, would you, would you be able to. And you’ve probably done benzene. Probably done organic molecules. Yeah. Would you be able to draw me a molecule of benzene on your piece of paper. Okay okay. No. That's okay. No, I can see it. That's fine, it's fine, it's fine.


Okay. So you've put a ring in the middle. Why have you put a ring in the middle? That's interesting. 

Well, so benzene in the benzene ring you've got these three double bonds. And yes, in the historical like the model of, like the kekule model, you've got individual double bonds followed by the single bonds. But nowadays it's understood that the double bonds form like a conjugated pi system, where the electrons are actually delocalised across the whole ring, as opposed to set into, you know, double bonds, single bond, double bonds, single bond.


So I've drawn a ring to show you that the electrons are delocalised across the whole structure. Okay. They are the electrons. You're right. Yeah. And what what orbitals are involved in that then? What's the orbital kind of, structure that's involved or you know, because, there are different orbitals aren't that are dependent on, well, that the localisation is dependent on particular orbitals.


Is that right? Yeah. The pi the pi orbitals. Right. Okay. Okay. So these are so, so this is a like a, yeah. Exactly. So this is, this is a, this is a sort of, a ring of electrons moving through, through through the p orbitals, isn't it? To create the pi bonds. Yeah. Yeah. Okay. So what does that do to the overall shape of the benzene molecule?

If you have to think about it in terms of like, describe its shape. How I mean, obviously I know it's hexagonal, but I mean it's overall kind of shape in 3D. How would you how would you describe the effect on its shape?

Well, I guess it, it makes sure it's a flat ring. Is it as opposed to being like it, I guess in a normal, like cyclohexane, you've got like a chair shape, I think. Yeah. Yeah, yeah, yeah. Because of the high, orbital interactions, it has to be flat to ensure that their all at the same level. Absolutely. Yeah. That is correct. Yeah. That's right, that's right. And so what you’re absolutely right. So it is flat. It isn't it isn't a chair shape like cyclohexane, you know. Exactly because of, of your pi bonding. And just before we, I wanted to kind of then talk little bit more about this bonding, this double bond that we're talking about. Because what we're talking about really here isn’t it, or something like double bonds, but, why is it that you can't, you know those orbitals
why is it that you can't get rotation around those orbitals that if you know, what is it about the alignment of the of the orbitals that might mean that you can't rotate around those bonds?

Well, so in - can I draw something. Is that alight? By all means draw it.

So I'm just drawing a, if you see here you've got. Oh yeah. Yeah. My diagram of the p orbitals. Yeah, yeah. And I guess what you've got is you've got - they’re above and below. So if you've got rotation of the bonds, like a noble like sigma bond, would, you just end up with your break for the interaction.


So the electrons are no longer able to bridge for two orbitals. Yeah. That's right. Yeah, yeah. So you've got your alignment of your bonding antibonding orbitals. They've got a, you know. And so because they're aligned you basically, it’s energetically very unfavourable to rotate. Yeah. Absolutely. Now I'm going to show you something actually now. Wait there. Just going to show you something on your screen.

All right. You should see a molecule of phosphatidylcholine on the screen. Is that right? Fo you see that? Okay. So out of interest, I mean, I don't know whether you come across this molecule, but have you come across phosphatidylcholine at all in what you've done at school?

I think it might have been touched on as being one of the phospholipids in the membrane. Precisely. Yeah. That's right. Absolutely. So it is, it's what is one of the principal phospholipids actually for the, for the membrane. So now this, this structure as you can say, it's that obviously, the, the kind of chains are made of, of hydrocarbon, sort of units aren't they.


And and you can see that it's saturated. Now, I just wanted to ask so, so, you know, if I was to introduce a, a double bond at some point along this, chain, I mean, let's say,let's say I introduce a double bond here. Doesn't really matter, but say I introduced a double bond here. or here.

If I was to introduce a double bond? My first question is what might that do to the shape of the chain if I introduce a double bond at that point? Oh, well, I guess linked to what we said earlier, you're not able to rotate around a double bond. Yeah. So I guess depending on how you, you put it in, you either get a trans or a cis double bond which would mean that you've got, it would introduce like a kink in the chain where either it would out or kink in but it would introduce a geometry.


Now, now of course, we, you know, when we learn about phospholipids and phospholipid membranes, we should have learned about at school kind of with, you know, the lipids and the proteins sort of sitting in the fluid mosaic. You know, we, we think of those, the change as being highly mobile.


And obviously, as you said, it's going introduce a double bond, It's going to kink it and that will produce, sort of it'll make it a bit more rigid won't it as well. Yeah. Okay. I think so. So what, what, what do you think that will do to the, to the kind of packing between the, lipid chains, what, what effect do you think it might have on the packing between the lipid chains that have a kink like, like the one that you've said, which are right. You're absolutely right. Double bond here would introduce a kink into the chain. What do you think that would do to the packing in the, in the, in the biolayer?

Well, I think if you've got a, a lipid which is more rigid and it's got this kink in it, I guess it means that you can't pack your phospholipids as closely to one another because you've got this kinked structure, which is sort of preventing it from coming as close.


Yeah, absolutely, absolutely. And final questions before we move talk a little bit about about proteins. What do you think that might do to the fluidity of the membrane? Like, you know what I mean by fluidity, sort of how well, how fluid it is. Yeah. Well, I think introducing the double bond, if you've got less tight packing, I guess it will become more fluid because. That's right.

I would assume that you'd got more like Van Der Waals interactions between the phospholipids. And so if you kink it then there's less interactions. So it's more mobile. That's great. That's great. Thank you Kian, very much. Thank you.


You mentioned when you were talking about or, you know, you had quite a lot to say about, signaling and cell cycle and so on.

And at the beginning of that, you were talking about a receptor system in the membrane. And, I just so I want to talk a little bit about proteins like that now. So like membrane embedded proteins. So membranes contain lots of different kinds of proteins. They contain, sometimes they contain receptors like, like the one that you were talking about, which kind of transmits a growth factor signal inside a cell.

But they might also contain like, channels and things. So my first question would be, you know, thinking about what you know about amino acids and how the, the different characteristics amino acids have what, what do you think might be different about the distribution of amino acids in a, in a protein, which is like the receptor you talked about, which is sitting in the membrane, which might just have like an alpha helix that it's anchored with to the, to the membrane.


And another protein, which maybe is, you know, an ion channel that signals in a neuron or in another cell. How might the amino acid patterning differ, do you think, for those two different systems? Well, I think for both the soluble protein and the membrane protein, you'd have, you'd have a, you probably have a similar amount like proportion of hydrophobic to the hydrophilic groups.


But I would assume that in the membrane protein you've got them in a row. So I don't know how wide the like, how many residues would take up a membrane. But, you'd have like a structure of hydrophobic residues to make up, like the helices which make up part of the protein. Yeah. Okay. So I was going to say that if you had a, channel, you'd have an inner lining of hydrophilic groups, probably, to interact with whatever's passing through.


So that's what I think. I thought the distribution would be similar, but you just have them packed in different areas. Okay. So. Yeah. So but yeah. So by that you mean, you mean like maybe the proportion of different kinds would be similar, but the kind of, their placing in the polypeptide would differ because it would, the kind of environment or the role and environment would you know, define a need for there to be different, well, different distributions. Different. Different arrangements of them. Yeah. Okay. But yeah. So. So that's right. That's good. So then if we think about the folding of a protein, like a folding of a protein, that sits in a membrane or a folding of a protein that's in solution then so, this is this is a difficult question. I know you were have come across this in school, so don't worry if, if you need a bit of time to think about it. But how might the different, how, you know, because proteins fold up into structures and we're gonna look at a different protein in a minute as a specific example.


But how would, how would, the folding differ, do you think, for proteins that are going to sit in the membrane and proteins that are going to sit, or are going to be in solution, carry out a role, like haemoglobin, say, in our blood. So that's the example I'm going use in a minute. But say like haemoglobin is in our blood, it carries oxygen.

It's floating around in our red blood cells. It's soluble. And then there's other proteins that are in membrane. So how might their folding differ do you think? Well so for proteins, in our A-level we study that for a soluble protein you'd have I think it's called the hydrophobic effect. To drive the folding of that protein. You would. Where you have the like hydrophobic groups within your protein would sort of pack close to one another.


And form the core of a protein. Yep. I guess if you think with a membrane protein, I guess it'd be more difficult because you'd probably, maybe need another protein to help insert it into the membrane or something , because. Oh, that's interesting. I guess it wouldn't, it wouldn't be able to just cross if you got like hydrophobic groups in the middle but then hydrophilic groups on either side, it maybe wouldn't be able to get through without having something to help it.


That's a really interesting point actually. Yeah. Yeah, that I hadn't actually thought you might say that, but you're absolutely right. That's actually a really interesting point. Yeah, indeed. You, you perhaps would need a way to insert it that kind of puts it in the right orientation. Yeah, absolutely. And that gets it as you say, because it's going to particularly it being a hydrophobic it can't just find its way there in solution. Somehow it's got to be delivered hasn't it I guess. Yeah. That's very, it's very interesting. Now, now I just want to show you one more thing. I'm just going to show you another picture.


This is haemoglobin. I just, I just, this is just a picture to sort of tell you we’re going to talk about haemoglobin briefly. And you've probably, you've probably - have you studied haemoglobin a bit at school? Yeah. Yeah. We talked about the oxygen transport in the blood with haemoglobin.

Yeah. So these are these haem groups here and the haem groups, they, they carry, as you know, they, they, they carry oxygen with, with the help of iron. Anyway, this is my next slide. So,

Now, there's one thing I want to explain about haemoglobin. Now, if we go back to this slide, you can see that it's got four subunits. Okay. And it's got you got two alpha two beta subunits. So that coloured differently here. And so you probably know that when oxygen binds there needs to be a confirmational change.

The protein needs to change shape of it in order to bind oxygen. Okay. Now it's interesting. One of the interesting things about, about this is that when oxygen binds to haemoglobin, and you follow it binding, you see the, the sort of pattern with which it binds, it's a, it's, it follows a distinctive shape. So here, here we've got the distinctive shape shown here.

So on the, on the left hand side you can see in this graph we've got the saturation of the haemoglobin in percentage. And on the, on the, on the, on the x axis at the bottom here we've got the partial pressure of the oxygen. So first question I have for you is, we’ll talk about the the distinctive pattern in the moment.

But as you can see there's two different kinds of haemoglobin on here: fetal haemoglobin and adult haemoglobin. Now, tell me, how would you say they differ? How is the adult haemoglobin different from the fetal haemoglobin? So from from the look of the graph, you've got the adult haemoglobin has been shifted to the right of the fetal haemoglobin curve.

Yeah. And from if I look at the values it looks like that it binds less tightly to oxygen. So it looks like it requires a higher partial pressure of oxygen to be, to reach the same level of saturation. Okay. Yeah. Yeah. So that's an interesting way to put it. But yes you're right. Yes. That's right. So it requires a higher partial pressure to kind of bind the oxygen, the adult haemoglobin compared to the fetal.

Yeah. Yeah. Absolutely. Just out of interest, I mean, since I know I know, you've told us that you're not really interested in organisms so much, more cells. That's fine. But just thinking about the system as a whole. Is there a reason why you might want your fetal haemoglobin to be kind of, you know, bind oxygen kind of more readily than adult haemoglobin, maybe?

 So I guess what I'm thinking is that a fetus wouldn't be able to breathe by itself. It would rely on the blood supply from its mother to provide blood. Sorry. To provide oxygen. So. Yeah. Yeah, yeah. Maybe it would need a higher. It would need to be maybe a higher affinity to oxygen so that it could take blood from, sorry to take oxygen from the mother's blood and find it with its own haemoglobin.

Yeah. That's. Yeah. Good, good. Now, let's now, I want to you one more curve. But before we get there, let's talk a little bit about the shape of the curves. Now, you've probably not done this at school, although you might have done.

I mean, if you had to describe the shape of the curve, how would you describe it? Well, I guess it looks a bit a bit like an S, but it hasn't got like a bit in the middle. Yes. So it looks a bit out of shape. So yeah we actually call it sigmoid. Sigmoidal curves because they're S shape.


Yeah. Yeah. Now why do you think they might be sigmoid? And let me give you a clue. And, and the clue is just to think back to the fact that it's it's a tetramer. This, this thing haemoglobin. That it's a tetramer. Well, dimer or dimers. But the tetramer. From what you said earlier, I think you said that the binding of oxygen causes like a change in its shape.


Yeah. Protein. Yeah. So maybe instead of it being like a linear curve, maybe it's a sigmoidal shape because the binding of one, one oxygen could affect the binding of another oxygen molecule. If a change, that the protein changes shape. Yeah, yeah yeah. That is true. You mean, so you mean that if one subunit changes shape, you might make the other ones change shape as well.


Yeah. Yeah. That's that's that that's what people think. Yeah. Final thing then let me show you this. So this is another curve. So I've put this in and it's, it's actually, the sort of curve you might get in high carbon dioxide levels. So somebody was breathing in high, high carbon dioxide. That's the kind of effect you might, you might get.

So that is the Bohr effect as you can see, as I've labelled it. So. So, first of all, tell me, you know, how is the curve changed now it's red and, and then can you, can you give me any suggestions about why it's changed like that? So similar to the adult and the fetal haemoglobin, the, the, the Bohr effect curve is shifted to the right.


So I guess from what I said earlier, that would mean that it has a lower affinity for oxygen. Yeah. Yeah, yeah it does. Yeah. Why might it have a lower affinity for oxygen do you think? This is not easy and we don't expect, we don't expect you to know this, it’s just, we’re just working through these. It's an interesting problem to think through, that's all.


So anything you think or suggest is absolutely valid and helpful. Why, why might it kind of be less good at binding oxygen now it's got the carbon dioxide? That might be, I guess, so carbon dioxide is made by the respiration. So, yeah, maybe that if you've got a muscle or like a part of your body which is releasing lots of carbon dioxide, I guess that shows that it needs more oxygen to fuel aerobic respiration.


And so maybe the higher it releases more. So this curve is shifted to the right so that the haemoglobin releases more oxygen where it's, where it's needed. That's quite. Well, yeah. That's sort of interesting. It's kind of thinking kind of like almost physiologically. Yeah. Yeah. But let's think of it more molecularly. So when carbon dioxide, dissolves in, in water, what what will you get?


What does dissolving carbon dioxide do you think have, what effect does it have to think, for example, on the pH of water? Well, I, I remember that carbonate is one of the, that carbonic acid is one of our acids that we got taugtht about. So maybe it would decrease the pH.

Yeah it does decrease the pH. Distinguishable protons. Absolutely. Yeah. Yeah, it does decrease the pH. Now, are any of the bonds in your haemoglobin likely to be pH sensitive or, you know, are they, to think about, you know, do any amino acids have have kind of ionisable groups? I suppose is what I'm asking, acidic groups, for example. Yes. No, I remember that there's some which have a carboxylic acid end so they can lose a proton or I guess gain.


And then there's some which have nitrogen like, I think lysine and histidine, so that they could become carbon protonated. Yeah. Yeah they do, they do. So. So if we’re lowering the pH do you think that might affect the, the, well the ionisation of some of the sidechains? I think, I suppose what you're saying is, yes, it might do.


Yeah. So if I guess if a pH slightly lower, it might make some of the, some of the more basic groups become protonated. Yeah, yeah. And in fact, what people think is it kind of strengthens some of the bonding. Because the, the low pH kind of strengthens some of the bonds we call salt bridges or, but those, those are the kind of bonds formed actually between acidic groups and basic groups.


In the, in the, in the protein. And it's thought that those get, get strengthened because of the, the lower pH. So that's thought to tighten the bonding. So final question. So why might - think, you know, molecularly rather than physiologically - why might, you know, tighter bonding as it were holding the tetramer together, why might that resulting in the red curve do you think, in high carbon dioxide levels?


Well, I guess what we, we talked earlier about the, the changes in the shape leading to the curve having the shape it does. So obviously, I guess if you've got a tighter binding of the tetramers, it might perhaps make it slightly more rigid and if maybe like, prevent or make it harder to change the shape of the protein.

Thank you. Thanks, Kian.


Thank you so much for your time today. And I, Yeah, I

good rest of your day. Thanks, Kian. Thank you.

Nice to meet you. Nice to meet you. Bye.

 
So we should talk a little bit about, how that went. And, well, I. Well, I’d be interested. I’d be very interested to know, obviously I want to know what you thought, Kian, what my, my, what I would say is, when we got into the, the sort of problem solving - benzene and all that onwards to the end. It was very like, actually, what what you might find in a, in an interview, for an undergraduate place. The kinds of problems which are about taking things that people have learned at school, like benzene. And at school, people know about the lipid mosaic model for membranes from school. They know about lipids from school.
 
So taking stuff that we know from school and then just thinking a little bit more with it and putting it together with other ideas that was very like what you might do in an actual undergraduate interview. The, the first part, was quite like it in the sense that we started from something that Kian had, perhaps, mentioned is his personal statement, or he told us he volunteered about being interested in in the cell cycle.


Of course, Kian knows more about the cell cycle than the people generally would at school. So in some sense, there was a lot more detail in that section than you might expect in interview. That said, two things. Firstly, sometimes candidates do know a lot about something or other they've read about, and that's absolutely fine. But secondly, it's not, it's not so much the level of detail that matters to us.

In fact, it's not really the level of detail. It's more the interest that they've shown. So if somebody kind of happens to know a lot about something that they've read about and it could be anything, you know, there are different things people might read about. They might know a lot about it. That's good. But the key interest for us is it shows interest, shows that somebody is engaged in the topic, engaged in the subject, and really wants to study it in detail.


It's not about knowing lots and lots and lots of stuff. It's about, the fact that the reason they know this stuff shows there's an enthusiasm there. So you don't need to know a whole load of detail. You just need to tell us why it is you're interested in Biochemistry, I would say, and it's not about, kind of more and more information kind of makes a stronger and stronger case of being offered a place. That's not how it works. It's more how do you handle problems? How do you think through things? Are you interested in the subject? Can you think on your feet when we slightly change the direction of the conversation? Can you pick up on the, on the sort of, how the direction’s gone and why we've moved from, say, talking about membranes to talking about membrane proteins and why they're different?

And can you make sense of the links, which is all stuff which is based on core information that is not very detailed, but helps us to assess someone's aptitude and potential for studying at Oxford. That's what I would say. I don't know what you think Kian? Yeah. No, I, I definitely agree, but I think the most important part of showing at the start of the interview is just to show that you really care about the subject.

And I remember for my interview, I don't think I knew very much specific Biochemistry in a lot of detail. I remember from my St Hilda's interview at least that they asked me a couple questions about epigenetics because I talked about that in my personal statement. And even though I feel like now I know a lot more about actually how epigenetics works.


And we study it a lot more, but I think it was just more that I could show that I was interested and I'd read this book about it. And, you know, this is why, that's part of reason why I'm really interested in Biochemistry. Absolutely, absolutely. Yeah. Yeah. And and the other thing I'd say is that I think quite often you'll find that in the interview, candidates are shown something in the interview.


So I showed a molecule of a lipid and I showed haemoglobin and those binding curves and it'll vary. Sometimes it's an image of a cell, sometimes, and sometimes the questions are a bit more genetic but it's all around. So what I mean is talk about DNA or or how genes are organised. But the point is that it's not about what you know.

It's about taking information that you already have come across at school and developing it and then giving you new information that you might not have thought about, in order to develop that, take it forward and, and, see what you make of it.