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Viktoria Bågenholm from Sweden

Viktoria previously completed her Master’s in Protein Science, a programme at �۶���Ƶ that utilised the same courses as the new Biochemistry specialisation. She has since completed her PhD in the same department at Lund.
 
Why do you think it’s important to study Biochemistry?

“I think it is an important field because it has such an increasing number of important applications. Everyone works with proteins these days! A lot of the past research has been related to topics like medicine, DNA, understanding how living things work, and how we can make medicine or food products better. But these days biochemistry is starting to be used for so many other things as well. In the research group where I did my PhD, we were using proteins and biochemistry methods to develop new materials in a way that you wouldn’t have been able to do a few years ago. We’re reprogramming proteins to do what we want them to do, like make plastic for example. I think there is going to be a lot of need for biochemists in the future!”
 
What did you think of the teaching style and way of studying here at �۶���Ƶ?

“I really liked it. There were some significant improvements from how it was in England, where I did my Bachelor’s. In England, you take all courses in parallel, and you have all exams for all courses at the same time at the end. But here at �۶���Ƶ, you take only one course at a time. I had free weekends for the first time in three years. It was great! I like the combination of different types of exercises, lectures and labs. I enjoyed that there was a lot of laboratory work in all of the courses.”
 
What did you think of the learning environment and the relationship to professors and other students in your courses?

“I generally remember it as quite good overall. I always found the environment at the department good and helpful. It’s very easy to talk to the professors. I think my course mates always had very good cohesion and were easy to work with. Occasionally, in labs, we would mix up the lab groups. That, of course, helped you talk to everyone and learn more from everyone.”
 
How international were your courses?

“It was a bit of a mix of international students and Swedish students. At least, the people I hung out with certainly were a mix.”
 
Do you feel that having a lot of practical lab time helped prepare you more for your career?

“Yes, definitely! For example, the course Advanced Biochemistry has a whole project that you have to design and carry out yourself. It was enormously helpful towards learning how to plan and organise your work. There are a lot of different aspects of important biochemistry methods that you learn about in your courses. I think it definitely helped to prepare me a lot for future research.”
 
What was your favourite course?

“I think it was Advanced Biochemistry, because of that intensive project. I personally liked the Structural Biology course more in terms of content, because that’s what I find interesting and that’s the field that I work in. But I liked the Advanced Biochemistry course the most because of that project and all the things you learn from it. It was really hard, but really fun to try your hand at so many things.”
 
Do you think there is a lot of flexibility in the Biochemistry programme?

“Well, there is a plan. But it’s a recommended plan. There is always the option of switching things around if you want to take courses differently or want to study a specific topic. As long as you meet the prerequisites of the courses you want to take, there is always flexibility in the system.”
 
What is it like to be a student at �۶���Ƶ?

“I really like it here! There are a lot of things to do, especially if you’re a student. The student life is really vibrant. I was in Spex, which is a theatre group, and there are so many things you can get involved in and so much to choose from.”
 
Do you have any advice for prospective students coming to �۶���Ƶ to study Biochemistry?

“Don’t be afraid to talk to your lecturers. They’re generally very happy to answer questions. Also, don’t be afraid to go ask them questions to find inspiration for your Master’s thesis topic. You can literally just go knock on their door and ask what their research is about, and they’re usually quite happy to tell you about it. That’s the best way to find your project. It’s perfectly acceptable to approach them. Also, try and get as much as you can out of the labs. They cover a lot of methods that are really useful. You will use them a lot later in your career.”
 
What kind of student do you think would really enjoy the Biochemistry programme?

“You should choose this programme if you really want to focus on lab work and do something practical. We do a lot of that. The department here is very good, and it has a lot of cutting-edge research areas. That makes this a great programme to network with for future positions.”
 
What are some of those cutting-edge topics?

“We have a group that works on amyloid fibrils, which cause Alzheimer’s. They are also branching into nanoparticles and the effects they have on proteins and living beings, which is a really hot topic right now. Nanoparticles come off of plastics and they’re everywhere. It happens when plastic gets broken down into microscopic pieces. What effect they have on us is largely unknown right now. It’s a sustainability issue as well. Another group does research on carbohydrate chemistry. That topic is very big because there is a lot of green chemistry about rebuilding carbohydrates to make plastic, coatings, and a large number of functional chemicals.”
 
What did you write your Master’s thesis on?

“I studied a protein called ribonucleotide reductase which converts the letters in RNA [ribonucleotides] to the letters in DNA [dioxyribonucleotides]. This means it is an enzyme that removes one oxygen. That is very complicated and hard to do, and this is the only enzyme that can do it. Every living thing has a version of this enzyme. We were studying one from a bacteria that lives on the deep sea vents. When I started, the research team had determined the protein structure using X-ray crystallography. This protein binds the ribonucleotides and the dioxyribonucleotides with two binding sites. One that tells it which letter to make and the other one that actually makes it. They determined the structure, but we wanted to see what it would look like if molecules were bound in these sites. I made eight different protein structures with different combinations of the two factors using X-ray crystallography. In the end, it was a great project to learn that method since it is a method I wanted to work with a lot in the future.”