This biomolecular method, developed for the identification of bone collagen about a decade ago by M. Buckley and M. Collins at the University of York, is a fast and cheap approach for a first-level identification of bones.
Collagen is the most abundant and often best preserved protein amongst vertebrates. Only a few milligrams of bone powder is sampled, collagen is then extracted, digested to peptides and the peptides are measured using mass spectrometry (Maldi-ToF-MS) to produce a collagen peptide mass fingerprint. This fingerprint is unique for deeply-diverged taxonomic groups hence the observed Maldi patterns are compared and matched against a reference database consisting of known-origin peptide fingerprints.
In this project we use collagen peptide mass fingerprinting as a first step identification of bones belonging to the Hominidae. The fragments are then 3D-scanned, CT-scanned and photographed before proceeding to the second level of specialised analyses that consist of: