Human proteins have not been reported to survive in free nature, at ambient temperature, for long periods. Particularly, the human brain rapidly dissolves after death due to auto-proteolysis and putrefaction. The here presented discovery of 2600-year-old brain proteins from a radiocarbon dated human brain provides new evidence for extraordinary long-term stability of non-amyloid protein aggregates. Immunoelectron microscopy confirmed the preservation of neurocytoarchitecture in the ancient brain, which appeared shrunken and compact compared to a modern brain. Resolution of intermediate filaments (IFs) from protein aggregates took 2–12 months. Immunoassays on micro-dissected brain tissue homogenates revealed the preservation of the known protein topography for grey and white matter for type III (glial fibrillary acidic protein, GFAP) and IV (neurofilaments, Nfs) IFs. Mass spectrometry data could be matched to a number of peptide sequences, notably for GFAP and Nfs. Preserved immunogenicity of the prehistoric human brain proteins was demonstrated by antibody generation (GFAP, Nfs, myelin basic protein). Unlike brain proteins, DNA was of poor quality preventing reliable sequencing. These long-term data from a unique ancient human brain demonstrate that aggregate formation permits for the preservation of brain proteins for millennia.

Patient artefacts in dental cone beam CT scans can happen for various reasons. These range from artefacts from metal restorations to movement. An audit was carried out in the Glasgow Dental Hospital analysing how many scans showed signs of "motion artefact", and then to assess if there was any correlation between patient age and movement artefacts. Specific age demographics were then analysed to see if these cohorts were at a higher risk of "movement artefacts". Dentomaxillofacial Radiology ( Keywords: hospital radiology departments; cone beam computed tomography Patient artefacts in dental cone beam CT (CBCT) scans can happen for various reasons. These range from artefacts from metal restorations to movement.

Raman spectra of mammoth ivory specimens have been recorded using near-infrared excitation, and comparisons made with modern Asian and African elephant ivories. Whereas the most ancient mammoth ivory (60-65 ky) showed no evidence for an organic collagen component, more recent samples of mammoth ivory indicated that some preservation had occurred, although with biodeterioration of the protein structure exhibited by the amide I and III bands in the 1200-1700 cm(-1) region of the Raman spectrum. The consequent difficulties encountered when applying chemometrics methods to ancient ivory analysis (which are successful for modern specimens) are noted. In the most ancient mammoth ivory specimens, which are extensively fragmented, evidence of mineralization is seen, with the production of gypsum, calcite and limonite; Raman microscopic analysis of crystalline material inside the fissures of the mammoth ivory shows the presence of gypsum as well as cyanobacterial colonisation. The application of Raman spectroscopy to the nondestructive analysis of archaeological materials in order to gain information of relevance to their preservation or restoration is highlighted.

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Despite being widely utilized in the production of cultural objects, keratinous hard tissues, such as horn, baleen, and tortoiseshell, rarely survive in archaeological contexts unless factors combine to inhibit biodeterioration. Even when these materials do survive, working, use, and diagenetic changes combine to make identification difficult. This paper reviews the chemistry and deterioration of keratin and past approaches to the identification of keratinous archaeological remains. It describes the formation of horn, hoof, baleen, and tortoiseshell and demonstrates how identification can be achieved by combining visual observation under low-power magnification with an understanding of the structure and characteristic deterioration of these materials. It also demonstrates how peptide mass fingerprinting of the keratin can be used to identify keratinous tissues, often to species, even when recognizable structural information has not survived.