Profile

I live in Oxford with my husband and my daughter who is 2 1 /2.  I’m a massive fan of all things science fiction and fantasy (I love star trek and star wars, Lord of the Rings, Marvel films, anime and comic books and many many more!).  I’m also a big fan of role playing games like dungeons and dragons – both tabletop and live action. I love writing stories although they’re not very good and I like sewing (mostly clothes and costumes for the live action role playing games I play in).

I love cycling and although I’m not a good runner, I enjoy going for a jog every now and then too. I’m an enthusiastic but terrible dancer.

My pronouns are she/her.

As a structural biologist, I look at proteins – these are like little molecular machines in your cells that help your cells do everything they need to do. When these proteins go wrong, they can cause disease. To help treat a disease we need medicines. Medicines are small molecules (smaller than a protein) that will stick to the protein (like fitting a key into a lock) and fix the problem, like turning a car engine on or off with the right key. Finding the right ‘key’ or medicine is important because you need it to bind tightly to the broken protein and not to anything else – otherwise it either won’t work or it will turn off lots of other proteins and cause lots of side effects.

More specifically I work on a disease called Fibrodysplasia Ossificans Progressiva (or FOP for short) which causes muscle around your joints to turn into bone. This can’t be removed and causes permanent disability. It’s also super rare – only 1 in 1.5 million people are born with it (you can’t catch it!) and so there are only about 40 people in the UK with it. FOP is caused by only one protein which has broken in such a way that it is too active. My job is to help find a medicine that might switch the protein off and stop excess bone formation.

To do this I use at technique called ‘x-ray crystallography’ which involves taking a sample of pure protein and tricking it into crystallising (this is like leaving salt water to evapourate to leave salt crystals but much more complicated).  Then we take those protein crystals and shoot really high power x-rays at them. The crystal causes the x-rays to scatter and gives us a ‘unique fingerprint’ that we can use to work out what the original protein must have looked like.

My typical day starts around 6.30 when my daughter wakes me up. Once I’ve got us both up, dressed and breakfasted – then into nursery and off to work it’s about 9.30. My days are often very varied – moving between practical lab work and data analysis on my computer. Some days I’ll go into the lab and set something up before going through to my desk to sort out some data before going back to check on my experiment. Sometimes I’ll spend a whole week in the lab purifying protein and experimenting with it or sometimes I’ll spend a whole week analysing some very tricky data.  I really love the variety that my job offers as I can plan my time around what I need to get done and decide for myself exactly what I need to do and when I’m going to do it.

My experiments in the lab tend to be quite messy – growing up e.coli cells to make my protein and then harvesting them before extracting the protein from within them and purifying it. Then I can actually do the interesting bit of the job which is experimenting with it – trying to crystallise it with different potential medicines or testing to see how it behaves under different conditions or what else interacts with it. There’s a lot of sloshing around of different liquids to get test conditions right and using robots to set up the experiments.

If I’m at my desk then I’ll be analysing my data to try and work out the structure of a protein. Or I’ll be drawing graphs to try and work out patterns to how my protein behaved in a different experiment or I’ll be writing up my results and making figures to explain what I’ve been doing to other people. Sometimes I’ll spend time creating outreach activities to explain what I’ve been doing to the general public as clearly as possible and sometimes I’ll spend time answering questions from patient groups (such as FOPFriends) about how my research into FOP is going.

Every now and then I’m lucky enough to get to go to the Diamond Light Source – a particle accelerator in Didcot where we use their high power x-rays to shoot our crystals and get the data we need to solve the structure. It’s a lot of fun but I only get to do this about twice a year.