Magnus Borup Bloch
Blegdamsvej 3, 2200 København N., 06 Bygning 6, Building: 06-1-10
My research is focused on structural and functional investigation of human membrane proteins involved in various diseases. Using near-native reconstitution of these in nanoparticles in combination with functional assays and biophysical techniques such as cryo electron microscopy, I seek to obtain detailed and biologically relevant structural and functional information about these important, potential drug targets, which may be utilized in rational drug development.
Primary fields of research
Proteins play indispensable roles in virtually all cellular processes, and generally we divide this important class of macromolecules into two categories: Soluble proteins, which are found in aqueous environments, and membrane proteins, which are associated with the lipid bilayer of cellular membranes. Alpha-helical integral membrane proteins (a-IMPs) constitute a highly prevalent class of membrane proteins that play indispensable roles in signalling, transport and other cellular processes. It is estimated that 20-30% of all eukaryotic ORFs encode a-IMPs, and more than half of all presently known drug targets are a-IMPs, underscoring their vast therapeutic potential.
Structural biology plays an important role in drug development, and the combination of cryo electron microscopy and near-native reconstitution of a-IMPs in nanoparticles allows us to obtain detailed and biologically relevant structural information about this important class of membrane proteins, which may be utilized in rational drug design.
I joined the Nicholas Taylor group in September 2018 as a research assistant, and currently my research is focused on investigating the structure and function of human a-IMPs involved in various diseases. The overall objective of my research is to obtain detailed and biologically relevant structural and functional information about these important, potential drug targets, with the purpose of making valuable contributions to downstream rational drug development.