Dr. Hannah Koon

Biography

Hannah Koon joined the department in 2012 as a lecturer in Archaeological Science. Her background is in collagen chemistry and biomolecular archaeology. From her Master’s degree onwards, she has been actively involved in research relating to archaeological bone. She uses multiple approaches (e.g. electron microscopy (TEM), calorimetry (DSC), amino acid racemisation, light stable isotopes and proteomics) to probe the structure and composition of bone collagen in order to address archaeological questions. Her NERC funded PhD research (Detecting cooked bone in the archaeological record) focused on examining the deterioration of mineralised collagen. In particular she has examined how the presence of mineral and covalent cross-linking can each minimise the extent to which thermal alteration affects collagen. This work has led to two new theories to explain the mechanisms of collagen degradation ‘all-or-nothing’ and link-lock. The link-lock hypothesis was developed with her CASE partner, the British School of Leather Technology, and is now part of the curriculum taught to leather chemists at the school to explain the stabilization of collagen under different tanning agents. Hannah’s work using electron microscopy (TEM) to assess degraded collagen has led to a collaboration with English Heritage to inform on the future management of archaeological sites; TEM was successfully used to identify accelerated degradation of bone following the re-watering of an iron-age archaeological site (Fiskerton, Lincoln) and to interpret a possible “jelly bone” from Star Carr. In addition her methods to detect artificially cross-linked bone collagen have been used by the US Armed Forces DNA Laboratories (JPAC-CIL). With this microscopy approach Hannah has also been able to find direct evidence of cooked bone in the archaeological record. The technique has been tested on 9th-10th century bovine bone from a processing site at Coppergate, York. The technique is currently the only method able to detect low-temperature cooked bone from archaeological sites and has received media attention through a National Geographic documentary (‘Lost cannibals of Europe’, Jan 2011). In recent years Hannah has expanded her research on archaeological bone collagen to include cutting edge proteomic and isotopic techniques. She has recently developed a new method to detect sub-clinical scurvy in archaeological populations as part of a Wellcome Research Fellowship. Using mass spectrometry to identify site specific hydroxylation-modifications on pathological and non-pathological collagens she has been able to identify biomarkers for sub-clinical scurvy. Hannah has also recently collaborated with the Tuross lab (Harvard) where she used O and H isotopes to pin-point potential pathological collagen in individuals who, because of seasonal migration, have spent periods nutritionally stressed. The results, though preliminary, suggest that this combination of stable isotope and proteomic analysis of collagen could have great potential for studying diet and health among early migrating populations.

Research

Hannah’s research interests focus on two related areas; the first is understanding the mechanisms by which biological materials degrade as a result of taphonomic or diagenetic processes, and how these can impact on our ability to retrieve molecular information from archaeological remains. Secondly, she is broadly interested in the study of human biological remains from historic time periods, in particular how evidence of food processing and of disease on bones can be used to provide insights into past diet and health. Most of her research to date has focused on exploring the bone protein, collagen, at different orders of magnitude from the gross to the molecular scale. The findings from this work have been used; to detect low temperature cooked bone and embalmed bone, to study how bone degrades in different burial environments and to develop a new model for the thermal stabilization of collagen. Most recently she has used mass-spectrometric analysis of collagen to identify a disease biomarker using proteomics and to track the seasonal movement of 16th-17th century European seafarers using stable isotopes.

Professional activities

Publications