https://www.selleckchem.com/products/oxidopamine-hydrobromide.html Due to mechanisms such as proteolytic processing or alternative translation starts, in vivo proteoforms do not necessarily correspond directly to those encoded in the genome. Therefore, the knowledge of protein termini is an indispensable prerequisite to understand protein functions. So far, sequencing of protein N- and C-termini has been limited to single purified protein species, while the proteome-wide identification of N- and C-termini relies on the generation of single, terminal proteotypic peptides followed by chemical enrichment or depletion strategies to facilitate their detection via mass spectrometry (MS). To overcome the numerous limitations in such approaches, we present an alternative concept that readily enables unbiased ladder sequencing of protein N- and C-termini. The approach combines exopeptidase digestions of the proteome with two-dimensional chromatographic separation and tandem-MS. We demonstrate the potential of the methodology by analyzing the N- and C-terminome of S. cerevisiae, identifying 2190 N-termini and 1562 C-termini. In conclusion, the presented method largely expands the proteomics toolbox enabling N- and C-terminal sequential characterization of entire proteomes.The "Zeeman effect" offers unique opportunities for magnetic manipulation of the spin degree of freedom (DOF). Recently, valley Zeeman splitting, referring to the lifting of valley degeneracy, has been demonstrated in two-dimensional transition metal dichalcogenides (TMDs) at liquid helium temperature. However, to realize the practical applications of valley pseudospins, the valley DOF must be controllable by a magnetic field at room temperature, which remains a significant challenge. Magnetic doping in TMDs can enhance the Zeeman splitting; however, to achieve this experimentally is not easy. Here, we report unambiguous magnetic manipulation of valley Zeeman splitting at 300 K (geff = -6.4) and 10 K (geff =