Posted on 7 March 2005
The York groups, headed by biomolecular archaeologist Dr Matthew Collins and Chair of Analytical Science, Professor Jane Thomas-Oates, used the University’s Applied Biosystems 4700 Proteomics Analyzer mass spectrometer to investigate bone protein osteocalcin from the Neanderthal, the oldest fossil protein ever sequenced.
Protein sequences can be used in a similar way to DNA to provide information on the relationships between extinct and living species. They also have huge potential for the archaeological study of disease, diet, evolution and even the wine trade.
The research, which is published in the Proceedings of the National Academy of Sciences of the USA (PNAS), was initiated in York by Dr Christina Nielsen-Marsh before moving to the Department of Human Evolution at the Max Planck Institute for Evolutionary Anthropology in Leipzig, Germany. Doctor Nielsen-Marsh and Doctor Collins worked on the project at the University of York in collaboration with Professor Thomas-Oates. The York researchers have also collaborated with colleagues at Michigan State University.
The exciting point to come out of this project has been to establish that it is possible to sequence ancient proteins
Dr Matthew Collins
Dr Collins, who runs the University of York's BioArch research facility, said: "This work was enabled by the unique organization of the Technology Facility in the Department of Biology at York. This provides the archaeology department through BioArch with seamless access to three floors of state of the art analytical instrumentation.
"The exciting point to come out of this project has been to establish that it is possible to sequence ancient proteins. Because proteins are typically the most abundant molecules in most living tissues and are directly encoded by the genome, the applications in archaeology are huge. Proteins are everywhere in archaeology.
"Archaeology, Biology and Chemistry work closely at York and we have just received £190,000 from NERC to develop new methods and widen the scope of this work on ancient proteins."
Professor Thomas-Oates, who contributed to the approaches used to acquire the mass spectrometric data, and to interpretation and presentation carried out in York, said the analytical instrumentation allowed detailed structural information to be obtained from minute amounts of protein.
"This is something that would be extremely difficult to do without the excellent instrumentation and expertise available in the Biology Department's Technology Facility, coupled with the vision and skill of the various members of the BioArch group, and the analytical expertise provided by the Chemistry Department," she added.