Data from: Biologically and diagenetically derived peptide modifications in Moa collagens

The modifications that occur on proteins over time in natural environments are not well studied. It is necessary to understand these modifications to correctly interpret sequence data recovered from fossils. Bone from the relatively recently extinct moa (Dinornithidae) provides an excellent candidate for understanding the preservation of proteins and their post-translational modifications (PTMs) on proteins as well as protein degradation. Using mass spectrometry, we were able to detect peptides from both collagen I alpha chains, collagen II alpha 1, and three collagen V chains. Additionally, we were able to identify biologically derived PTMs (i.e., methylation, di-methylation, alkylation, hydroxylation, fucosylation) retained on the amino acid that they are commonly found in extant taxa. In addition to these in vivo modifications, we also detected modifications that are likely diagenetically derived; including previously observed deamidation, as well as loss of hydroxylation, advanced glycation end-products (AGEs), and peptide backbone cleavage. The collagen sequences and modifications derived from this relatively recently extinct organism will form a baseline for other studies of proteins recovered from other fossils. It will also provide a framework for interpreting the molecular phylogenetic placement of moa and other closely related paleognath taxa.