Abstrakt:
The analysis and characterization of aging and archaeological proteins are among
the latest challenges in analytical chemistry. In the first part of this dissertation
thesis, aging proteins were studied using LC-MS. The effects of aging on protein
sequences, including amino acid racemization, post-translational modifications,
and protein degradation, were studied. Subsequently, a chiral separation method
was developer to determine the amino acid enantiomer rates. In the second part of
this dissertation thesis, archaeological proteins were studied using nanoLC-MS.
Proteomics, called paleoproteomics in this case, was developed as an alternative
method for osteoarchaeology and genomics. Based on two sex-dependent forms
of amelogenin protein preserved in teeth, both biological sexes were distinguished
by nanoLC-MS because of differences in their protein sequences. The developed
proteomic approach was designed to be minimally-invasive. This was confirmed
by scanning the teeth before and after amelogenin extraction using both scanning
electron microscope and micro-computer tomography.