I work at the intersection of biology, physics, and computer science, and am broadly interested in big-picture questions related to protein structure, function, and evolution.
I have a particular interest in protein conformational disorder and self-assembly, with a focus on biological phase separation. Using a combination of numerical simulations and analytical theory, I am working with experimental collaborators to explore and understand how Nature harnesses disorder to achieve function.
I am a postdoctoral research fellow in the Pappu lab at Washington University in St. Louis. I also did my graduate traning in the Pappu lab. While remaining in the same lab is not a typical route, the complete intellectual freedom I've had to explore an enormous range of questions with over thirty different collaborators around the world continues to make the work we do highly variable and consistently stimulating. This, coupled with a geographical family constraint has motivated my decision to stay, although I am pursing various projects with increased independence.
My Ph.D. work focussed on the relationships between primary sequence and conformational behaviour in disordered proteins, and how those ideas can be used to understand biological self-assembly. My postdoctoral work is focussed on the biophysics and polmer physics of biological phase separation and questions associated with evolution in IDPs.
Before my Ph.D. I worked with Michael Linderman at the Icahn Institute of Genomic and Multiscale Biology in New York city, where I developed fast code to analyze massive data-sets in parallel. Before I moved to the United States I did a Masters in Computer Science at Imperial College London, where I worked with Prof. Yike Guo on methods for network integration in systems biology modelling. Prior to that, I did an MBiochem in Biochemistry at the University of Oxford, where I worked with Prof. Mark Sansom to use molecular dynamics simulations to understand membrane proteins, biophysical characterization of IgE with Prof James McDonnell, and biochemical dissection of the cytochrome-C biosynthetic pathway with Prof. James Allen.
My research is focussed on uncovering the general rules that govern how Nature uses protein disorder for function across a variety of length-scales and time-scales.
We often think of proteins as precise molecular machines, yet a substantial faction of naturally occuring proteins are partially or entirely disordered, existing in an ensemble of interconverting states. Can we explain and understand the role of structural disorder in the context of function in disease? My graduate work was split into two distinct but related parts. The first involved understanding how the primary amino acid sequence of disordered proteins determine their conformational and functional behaviour. The second involved understanding how the primary sequence determines the collective behaviour of disordered proteins in aggregation and self-assembly.
Going forward, I am focused on understanding how and why phase separation and gelation are used to achieve functionally relevant protein assemblies. More generally, it appears disordered proteins can achieve types of materials inaccessible to conventional synthetic chemistry, which in turn requires a new set of theoretical advances and numerical tools. Finally, I hope to use the principles uncovered in my graduate training to develop new approaches for understanding evolution in disordered proteins.
I work on these topics using a combination of numerical simulations, analytical theory, and informatics. This has required the development of new approaches, theory, and tools to help answer novel questions. It has also involved substantial collaboration with a range of colleagues, and I have been enormously lucky to work with some of the most exceptional scientists around the world.
Before working on biological disorder, my work involved formal methods for integrating models of distinct signalling networks, the development of high performance and massively parallelized analysis approaches, and understanding how membrane proteins interact with carbon-nanotubes through coarse-grained simulations. I also worked as a corporate due diligence analyst - a very different but very interesting type of work.
In my copious spare time (...) I manage all of the lab's hardware and software (two independent CPU clusters totaling ~800 cores, and ~100 TBs of storage across three independent RAID arrays), play far too much Ultimate Frisbee, and cook for my constantly hungry wife.
If you have questions or just want to bounce ideas, please feel free to get in contact at firstname.lastname@example.org or on Twitter. I'm always interested to learn new things and am a big fan of collaboration, but if I don't get back to you please just shoot me another email. My CV and references are available on request.