Mission: We study protein dynamics and disorder with a special interest in signalling complexes involved in memory.
In the long-term, we hope to develop novel therapeutic strategies by manipulating the supra-molecular organisation of proteins.
Most recent paper:
The team: We are a young, international group surrounded by neurobiologists and structural biologists.
Learn more about individual members here.
Methods: We use a range methods from biophysics and mechanistic biochemistry. Our core technical experitises are:
- NMR spectroscopy
- Single molecule FRET
- Kinetic and thermodynamics studies of protein-ligand interactions
- Enzymatic assays
Currently we are working on four major projects:
The role of the intracellular domains of ionotropic glutamate receptors in synaptic plasticity. Ionotropic glutamate receptors are crucial our ability to learn. On their intracellular side, they contain an intrinsically disordered tail, that is crucial for synaptic plasticity, but defies the normal structure-function paradigm. We are studying how these domains control the properties and interactions of the receptor.
The nanoscale organisation of signalling pathways. Signalling proteins are often coordinated into flexible protein assemblies called signalling complexes. These complexes control the efficiency and fidelity of signalling. We develop biophysical models for the effects of the architecture of signalling complexes.
Harnessing avidity in antibody engineering. Bispecific antibodies ar hybrid antibodies that target two antigens at once and have recently become a very succesful category of drugs. When an antibody binds two sites simultaneously, the binding may become stronger than either site alone. This is called avidity and we hope to use it rationally in antibody engineering.
Recent papers and pre-prints:
Dynamics of P-type ATPase ion pumps by smFRET studies. Ion gradients are crucial to cellular communication and arise through active transport by a family of integral membrane proteins called the P-type ATPases. P-type ATPases undergo large domain movements during their pumping cycle, which make them highly suited for single molecule FRET studies.
If you are interested in joining us then please contact Magnus.