Timothy Cleland & Elena Schroeter

Complexities and innovations in mass spectrometry: strategies for paleoproteomics

Timothy Cleland§, Elena Schroeter£

§ Museum Conservation Institute, Smithsonian Institution, Suitland, MD 20746; £ North Carolina State University, Biological Science Department, Raleigh, NC 27695.

Shortly after the last ancient proteins meeting in 1998, researchers began to investigate preserved intact proteins and peptides using mass spectrometry approaches, including TOF-SIMS, MALDI-MS, and LC-MS. The incorporation of these techniques has changed how ancient proteins are studied, and has shown their preservation is more complicated than previously inferred from amino acid analyses and antibody characterization. However, because mass spectrometry-based proteomics encounters unique challenges when applied to fossilized bone, the characterization of extinct proteomes is a more complex then typical protein analyses, and must account for variable effects from protein extraction, search algorithms, databases, diagenesis, and instrumentation. Despite these issues, continuing advancement in sample preparation methodology and mass spectrometry technology is allowing the investigation of novel questions and a more complete understanding of paleoproteins.