Marty Rogers, ESR 6

Cromarte RogersMarty Rogers is ESR6, works in Trinity College Dublin, studying the Novel lipid environments for use in lipid cubic phase (in meso) crystallization of membrane proteins.

Please tell us about yourself:

I was born and raised in South Carolina in the USA. I played the French horn in school bands and orchestras since I was 10 years old, and music of all forms is still one of my passions. I completed an undergrad degree in Chemistry at the University of Oxford before my time in the RAMP network. My spare time is usually spent listening to music, knitting, and exploring Dublin.

Why are you interested in science?

While science seems to solve a lot of the mysteries that we encounter in the physical world every day, I appreciate science for its ability to create new mysteries. When scientists delve into one unknown, they often uncover several other unknowns. The continual cycle of questioning and discovery is what fascinates me most about science.

Please tell us about your PhD project:

Proteins are molecules found in all forms of life which perform the vast majority of the processes necessary for proper cell function. Many of these proteins are found at the boundaries of cells, in the region called the membrane. These membrane proteins are the major targets of drugs; antibiotics often act on proteins found in bacterial membranes, pain relievers act on nerve cell membrane proteins, etc.

In order to efficiently design new drugs to affect how specific membrane proteins function, it’s helpful to know the structure of the proteins they act on. There are many different methods for figuring out the structure of proteins, and my project looks at the method known as X-ray crystallography. Specifically, our lab deals with the in meso method of producing crystals of proteins in order to determine their structure by X-ray crystallography. More about the history of protein X-ray crystallography, including the pioneering work of two female scientists, can be found here.

The cell membrane is madMembrane-picture-ESR6e up of many types of lipids. Some of these lipids are commonly known, such as cholesterol. Others are more exotic but equally important to the cell, such as sphingolipids and acylglycerols. Acylglycerols (AGs) are the major component of most human and bacterial cells, and it’s on these lipids where my project focuses.

Because AGs make up the natural environment of membrane proteins, they are the ideal starting point for the formation of protein crystals for X-ray crystallography.  I’m using one type of AG, monoacylglycerols (MAGs) to mimic the highly complex, natural mixture of lipids found in most cells. All MAGs have a lot in common chemically, but they show a wide variety of physical properties. My project involves mapping out the physical properties of mixtures of MAG and water at different temperatures. This information will help us determine which MAG will be best for forming good-quality crystals for X-ray crystallography. We will then be able to determine the structures of proteins more quickly, leading to better drug discovery in the future.

What do you or did you enjoy most until now in your position within RAMP network? Why ?

I have really liked getting to know people from all over the world, both at Trinity College Dublin and within the RAMP network. Exploring and learning together with people of such diverse backgrounds has been an unexpected joy.