Prof. Frederik Lermyte presents > Proteoforms in 3D – Conformations and Interactions
In recent years, there has been a tremendous advance in characterising the primary structure of proteoforms. Ultimately, these different proteoforms are important because they interact differently with each other and/or other molecules in vivo. Ultimately, this modulation of interactions is due to changes in folding and/or ability to participate in noncovalent interactions such as salt bridges or hydrogen bonds. Once the purview of methods such as crystallography or NMR, structural biology today benefits from a variety of mass spectrometry methods. In this seminar, the development and application of such MS-based methods for the study of folding and interactions of proteoforms will be discussed.