Dr Sarah Shammas graduated from the University of Cambridge with a BA/MSci degree in physics in 2005. During her PhD with Prof. Chris Dobson, and a short post-doctoral position with Prof. David Klenerman, she researched the conversion of soluble (intrinsically disordered) protein monomers (including Aβ and tau) into amyloid fibrils using a range of biophysical techniques including circular dichroism and single molecule fluorescence. Her major research interest is in protein-protein association and interactions, which she is currently pursuing in Prof. Jane Clarke's laboratory in the Chemistry Department of the University of Cambridge. This group has traditionally specialized in fundamental protein folding studies, and is now expanding into the study of coupled folding and binding reactions. In the last couple of years Dr Shammas has been involved in multiple projects in this area; in particular, the mechanism of assembly of the spectrin tetramerization domain, and of the interactions between the ('model') KIX domain of the transcriptional co-activator CBP and several of its ligands. Studying the kinetics of these processes will be fundamental to understanding the mechanism of coupled folding and binding, and also how these proteins interact in vivo.