Profile

I’m called Alex, my pronouns are she/her and I grew up in the south west of England near bristol. In school, I thought I wanted to be a vet or doctor, but during my A Levels (last 2 years of school) I realised I preferred learning about the underlying research and science rather than the diseases. I decided to go to University to study pharmacology (how the body and medicines interact) and loved this degree. I found that understanding how things work on the smallest biologically relevant scale was what really inspired and interested me, and so I started my PhD in this area in October 2018. In addition to my research, I am heavily involved in science communication and public engagement. I have led stalls for university events, as well as international science festivals. My favourite science communication experience to date was having a pen pal with a 6^th Grader in Chicago through the Letters To Prescientists programme.

I do protein structural biology, which is a fancy way of saying “studying what proteins look like”. Proteins are tools cells use to do their jobs – whether its ones in your eyes responding to the light from your screen to read this, or ones in your ears listening to this, or ones in your brain sending messages to understand what I’m saying, or ones in your tummy digesting your food. If we can understand what proteins look like, this can help us understand how they do their jobs – my favourite example is of a hammer and a screwdriver: both can help put up shelves, but one involves hitting things and the other involves twisting and you can match up which is which from their shape (hammer had flat edge to hit and screwdriver has handle to twist). This is really important, because when we get diseases, often proteins are involved and we want to change how they are working to treat the diease.

The protein I am working on is called a “membrane integral pyrophosphatase” (mem-brain int-egg-rall fie-ro-fos-fat-ase), which is a huge long word that basically means “thing in the cell membrane that breaks down a molecule called pyrophosphate”. This protien is found in protozoan parasites, such as malaria, and helps them be infectious. So, the plan is to find out what a membrane integral pyrophosphatase looks like, work out how it works and then stop it from working as a treatment for malaria.

This involves something called x-ray crystallography, where we make crystals out of the protein then shoot them with x-rays to see where the atoms are, computer simulations of how those atoms move over time, and computational chemistry to design chemicals that might stop them from working.

There are 3 main research groups I work in: the biology group, the chemistry group and the computational group.

The biology group involves working in laboratory. I spend my days making the protein I study, often in tiny amounts. I also purify my protein from others and do experiments to test how well it is working and how it is working.

In the chemistry group, I try to design different chemicals that might stop the protein from working. I use a computer for this and look at the data we already have about what the protein looks like and try to add different chemical groups that look like they will fit nicely to the protein – like a key into a lock.

In the computational group, I try to work out how the protein moves. It’s all good knowing what it looks like as a photo, but in cells the protein is constantly jiggling, so it’s better to make movies from the photos we have of them. This can show how the protein moves from step to step of its process.