Sam Knight, a staff writer at The New Yorker wrote a wonderful piece on the rise of palaeoproteomics, and as a side effect he helped to advance the mainstream understanding on what high-throughput mass spec proteomics (AgeCurve’s main method) can deliver.
Proteomics is the study of the interaction of proteins in living things. Where genomics studies humans’ roughly twenty thousand genes, proteomics is concerned with the shifting array of proteins assembled by those genes—our biological content, more or less, from albumin, which makes up sixty per cent of our blood proteins, to beta-amyloid, a family of brain molecules that can be a potential sign of Alzheimer’s disease. Proteomics aims for completeness. The proteome of a single human cell, which might contain billions of proteins, is sometimes compared to an atlas. It can guide geneticists or drug companies to early markers of a disease, or to the precise mechanism of aging, or to promising targets for cancer treatment. The field has been made possible by spectacular advances in data analysis and in lab instruments, which become cheaper and more powerful each year. Top-of-the-line mass spectrometers now allow chemists to sort through thousands of types of proteins in a sample, and to study them, one molecule at a time.
and then here’s a quote on how palaeoproteomics came into being
Since 2000, proteomics has attracted the attention of a small clutch of scientists who believe that it has the potential to immensely expand our knowledge of the past. Under the right conditions, proteins can survive for millions of years. In recent years, proteomic studies of art works and archeological remains have yielded biological information of startling clarity, revealing gossamer-thin layers of fish glue on seventeenth-century religious sculptures and identifying children’s milk teeth from pits of previously unrecognizable Neolithic bones. In 2008, researchers were able to sequence the proteins of a harbor seal that remained on the surface of six-hundred-year-old cooking pots found at an Inuit site in northern Alaska. Three years later, chemists found a hundred and twenty-six different proteins in a mammoth femur. With new proteomic techniques emerging constantly, the field has a heady, chaotic atmosphere of possibility. At a four-day conference called Ancient Proteins, held this summer in Copenhagen, presentations had titles such as “Biologics in Art: Whaaat???,” “Palaeoproteomic Analysis of Binding Media and Adhesives in Ancient Egypt,” and “Through the Looking Glass, and What Amino Acids Found There.”
We highly recommend reading the whole piece.