This lecture provides an overview of mass spectrometry, focusing on tandem mass spectrometry (MS/MS) and its application in analyzing peptides. It begins by explaining the basic function of a mass spectrometer, which operates under high vacuum to manipulate and detect ions. The instructor describes the process of ionization, where peptides in solution are converted into charged ions, allowing them to be separated based on their mass-to-charge ratio (m/z). The lecture then delves into the tandem MS process, highlighting the steps of ion fragmentation, separation, and detection. The instructor emphasizes the importance of obtaining sequence information from the fragments produced during the analysis. By examining the mass differences between these fragments, one can infer the amino acid sequence of the original peptide. The lecture concludes with a discussion of real MS/MS spectra, illustrating how the data can be interpreted to identify specific peptides and their sequences, showcasing the utility of mass spectrometry in proteomics.