Leveraging the Power of Mass Spectrometry-Based Proteomics to Reveal Novel Biological Insights

Mass spectrometry-based proteomics has the potential to offer new qualitative and quantitative insights into a wide array of biological questions. The work presented in this thesis, including the associated submitted papers, evidences my contribution to this field. Paper 1 demonstrates the successful identification of post translational modifications imparted upon histones following DNA damage. Papers 2-4 employ a label-free quantification approach to study the immunomodulation molecules endemic parasites use to impair host resistance. Paper 5 uses an isobaric tagging approach to quantify changes in immune response when dendritic cells are exposed to medically important antigens. Paper 6 displays the power of mass spectrometry in identifying a novel co-factor, which could not be identified by X-ray crystallography. In paper 7 mass spectrometry is used to show that the remaining unidentified enzyme in the morphinan biosynthetic pathway is expressed as a fusion protein composed of two distinct enzymes. These studies are all linked in their reliance on my use of mass spectrometry-based proteomics to make original contributions to knowledge and understanding within their fields.