My research uses protein separation and analysis techniques to investigate degraded tissues ranging from archaeological and palaeontological burial environments to processed foods.
Despite early research into the survival of non-collagenous bone proteins such as the small mineral-binding protein osteocalcin, most of my research focuses on type 1 collagen which is the major protein in bone and one of the most abundant in the animal kingdom. ZooMS, after 'Zooarchaeology by Mass Spectrometry', is what we call our approach to using protein fingerprints to differentiate between different taxa, which is particularly useful for fragmentary archaeological bone or the remains of juvenile individuals from morphologically similar species, such as sheep and goat. In archaeological applications we typically use the species identifications to investigate likely animal husbanding practises in the past, where my research has mainly focused on early Near Eastern agriculture including work in Cyprus and south-east Turkey.
My current research uses high-throughput ZooMS to investigate how vertebrate biodiversity has changed in Britain over the past few million years, but I am also investigating how collagen sequencing can aid our understanding of phylogenetic relationships among long extinct taxa from palaeontological sites worldwide.
I am currently a Royal Society University Research Fellow investigating the information content of the bone proteome, with a particular interest in protein decay in the extracellular matrix.
In 2008 I completed my NERC-funded PhD entitled ‘Species identification in ancient and degraded bone fragments using protein mass spectrometry’ in the Department of Biology, University of York which initially focussed on sequencing the small non-collagenous bone protein osteocalcin by LC-ESI-qTOF-MS and LC-MALDI-TOF-TOF-MS. I then re-directed this research to the study of bone collagen (I), because of its greater persistence in fossilised remains, and developed ZooMS (‘Zooarchaeology by Mass Spectrometry’), in which collagen peptides are fractionated by SPE and fingerprinted using MALDI-TOF-MS. Typical archaeological applications are to distinguish between morphologically-similar taxa such as the caprine species, sheep and goats, or the identification of taxa in limited but highly assemblages spanning much of the Pleistocene. During my postdoctoral research I refined this methodology to work on other collagen-based samples, ranging from mummified skin and leathers, meat and bone meal and gelatine-containing food products, as well as other mineralised tissues such as ostrich eggshell.
In 2010 I moved to the Faculty of Life Sciences here at the University of Manchester to take up a NERC-funded postdoctoral research fellowship on the assessment of biodiversity in Pleistocene Britain through comprehensive small-scale microsampling of vertebrate fossil remains. In 2013 I was awarded my Royal Society University Research Fellowship (until 2018) on 'Molecular Timers'.