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Protein analysis can reveal which animal supplied the material in an artifact—even when its appearance cannot settle the question. Techniques such as Zooarchaeology by Mass Spectrometry (ZooMS) identify characteristic protein sequences, often in collagen. Results depend on what survives, how the sample is analyzed, and whether contamination and other evidence are carefully considered. Some methods can avoid sampling, but many analyses require material to be taken from an object.
What can protein analysis reveal about a museum object?
Proteins are biological molecules that can survive in archaeological, historic, and paleontological remains. By analyzing preserved proteins, researchers may identify the biological source of an object’s material or learn about its historical and biological context. The same field also contributes to research on ancient diets, health, evolution, and past environments. These are related applications, but they require different questions and interpretations; detecting protein alone does not identify a species.
For museum collections, the method can help answer practical questions such as whether an object is made from one animal material or another, or what kinds of protein-based materials are present in a complex artwork. The Smithsonian Museum Conservation Institute describes proteomics research on bone and teeth, keratin-based tissues, collagen-based materials, and proteinaceous binders in art samples. Smithsonian Museum Conservation Institute: Proteomics
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ZooMS stands for Zooarchaeology by Mass Spectrometry. It compares characteristic protein sequences—especially patterns in collagen—with reference patterns to identify an animal taxon. It is a form of paleoproteomics, the study of ancient proteins using approaches that include mass spectrometry. The University of York describes ZooMS as a rapid, low-cost method for archaeological and historic materials, but that description does not mean every object can be identified or that results are equally precise in all cases. University of York BioArCh: Palaeoproteomics and ZooMS
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Researchers use protein methods on materials including bone, teeth, parchment, leather, hair, wool, and horn. The suitable method depends on the material and the question: identifying a taxon from selected sequences is different from establishing that a sample contains protein, and neither is the same as reconstructing an entire ancient proteome.
What did protein analysis reveal about ancient ivory?
On March 15, 2024, The Metropolitan Museum of Art announced a collaboration with the French National Center for Scientific Research and the University of Bordeaux that developed a proteomic method to characterize ivory in museum objects. The work addressed sequence uncertainties and identified species across objects from several regions; the Met reported that the method differentiated elephant and hippopotamus ivory in Ancient Egyptian material. This is a specific reported result, not a guarantee that every ivory object can be resolved in the same way. The Metropolitan Museum of Art: ivory research announcement
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That distinction matters: a laboratory result is evidence to interpret alongside an object’s context and other material evidence, not a free-standing answer to every question about its origin or history.
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Which methods do researchers use?
Protein analysis is not one test. Researchers select an approach based on the question, the material’s preservation, and the amount of sampling that is acceptable.
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- Mass-spectrometry-based proteomics and protein sequencing: examines protein fragments or sequences to characterize preserved biological material. It can support questions about materials or biological sources, subject to preservation and authentication.
- ZooMS: uses characteristic protein sequences, commonly collagen, to distinguish animal taxa in archaeological and historic materials.
- Immunoassays: target particular proteins and can test for a specified biological signal; a targeted result is not equivalent to broad species identification.
- Amino-acid analysis: examines amino acids in a sample and can contribute to material analysis, but the interpretation depends on the analytical question and evidence available.
Methods for in-situ analysis have also been developed. A 2017 study reported analysis of proteins and small molecules from ancient objects without microsampling, leaving the tested object unchanged. That demonstrates a noninvasive option, not that all protein analysis avoids sampling. Analytical Chemistry (2017): method for noninvasive analysis of proteins and small molecules from ancient objects
Does protein analysis damage the object?
It depends on the method and the object. Some approaches are designed for in-situ analysis without microsampling; other techniques require a sample. Even a small sample is a material intervention, so conservators and researchers must weigh the value of the question against the object’s condition, significance, and sampling risks. The existence of a noninvasive method for one study should not be taken as evidence that a particular museum investigation will be noninvasive.
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Before analysis, researchers need to consider whether proteins are sufficiently preserved and whether contamination could affect the result. Human handling and microbial material can complicate ancient biomolecular work. The American Museum of Natural History says its Ancient Biomolecular Lab, which opened in fall 2022, uses decontamination practices for research on ancient and historic biomolecules. American Museum of Natural History: Ancient Biomolecular Lab
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How do scientists assess whether a result is reliable?
A protein signal must be authenticated and interpreted in context. Researchers need to account for preservation and degradation, possible contamination, the limits of the selected method, and whether the finding fits other evidence about the object. In a 2018 methodological guide, Jessica Hendy and coauthors noted that there was then no explicit consensus on reporting, validation, or contamination controls for ancient protein studies. They called for precautions and standards throughout the process, from sample selection to interpretation. That statement describes the field as characterized in 2018; it should not be read as a claim about the current state of consensus. Hendy and colleagues: A guide to ancient protein studies (2018)
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For readers, the useful distinction is between what the analysis directly detected and what researchers infer from it. A protein’s presence, a match to a particular animal taxon, and a broader explanation of an artifact’s history are different levels of conclusion. The broader claim needs evidence beyond a raw signal.
Why do museums use protein research?
Protein analysis gives curators and researchers another way to investigate materials that visual examination alone may not resolve. The result can refine understanding of an object’s biological source, material composition, or context, while contributing to wider research on ancient life. Museum-based laboratories provide the specialized facilities and contamination controls needed for this work; the American Museum of Natural History’s lab is one example. The method is most useful when its limits are made clear and the analysis answers a defined question about the object.
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