Edinburgh Research Explorer

Dr Joseph Marsh

Chancellor's Fellow

Profile photo

Willingness to take Ph.D. students: Yes

Education / Academic qualification

Bachelor of Science, University of British Columbia
Doctor of Philosophy (PhD), University of Toronto
Structural Characterization of Disordered States of Proteins

Biography

I joined the MRC Human Genetics Unit as a Chancellor’s Fellow in 2014 in order to start an independent research group. We use computational methods to study the role of protein complexes in normal biological process and in human disease.

Prior to this, I was a postdoc in the group of Dr Sarah Teichmann at the MRC Laboratory of Molecular Biology and the EMBL European Bioinformatics Institute, supported by HFSP and EMBO fellowships. My postdoctoral research focused on using structural bioinformatic approaches to study protein flexibility and the structure, assembly and evolution of protein complexes.

I completed my PhD in 2009 in the group of Dr Julie Forman-Kay at the University of Toronto and the Hospital for Sick Children. My research there involved both experimental and computational characterisation of the structure and dynamics of intrinsically disordered proteins, and how these properties are related to their interactions with other proteins.

My research in a nutshell

The ultimate manifestation of biological function often involves the assembly of proteins into complexes. Recently, the emergence of new experimental and computational techniques, along with the increasing availability of diverse structural, genomic and proteomic datasets, have created huge potential for investigating protein complex structure and assembly on a large scale.

Our research can be divided into two related parts. First, we are interested in the normal biological roles of protein complex assembly. In particular, we seek to understand how assembly occurs within cells, how it is regulated, and how it contributes to biological function.

Second, we are also interested in how the location of a mutation within a protein complex, i.e. its quaternary structure context, influences its propensity to be associated with disease. Our early work strongly suggests that incorporating quaternary structural information can substantially improve methods for predicting mutation pathogenicity and prioritising causative variants.

Research activities & awards

  1. Scientific Reports (Journal)

    Activity: Publication peer-review and editorial workEditorial activity

View all (1) »

ID: 14907505