The Musgaard lab uses a variety of computational tools to enhance our understanding of protein structure and function. Many proteins undergo conformational changes as part of their functional cycle, and it is therefore important to understand their dynamics in order to understand their function in detail. One of the most used methods in the lab is molecular dynamics (MD) simulations, which can predict protein motion at atomistic detail as a function of time. This provides detailed insight into protein conformational changes, and hence function and modulation. The predicted dynamics can further reveal potential binding sites for novel modulators, which can be developed into new drugs. The lab is particularly interested in ligand-gated ion channels, focusing on acid-sensing ion channels and ryanodine receptors, and collaborates with experimental experts for most projects.
Selected publications
- Steered Molecular Dynamics Simulations Predict Conformational Stability of Glutamate Receptors; M Musgaard, PC Biggin, Journal of Chemical Information and Modeling 56 (9), 1787-1797, 2016
- Kainate receptor pore‐forming and auxiliary subunits regulate channel block by a novel mechanism; PMGE Brown, MRP Aurousseau, M Musgaard, PC Biggin, D Bowie, The Journal of physiology 594 (7), 1821-1840, 2016
- Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes; GB Dawe, M Musgaard, MRP Aurousseau, N Nayeem, T Green, PC Biggin, D Bowie, Neuron 89 (6), 1264-1276, 2016
- Defining the structural relationship between kainate-receptor deactivation and desensitization; GB Dawe, M Musgaard, ED Andrews, BA Daniels, MRP Aurousseau, PC Biggin, D Bowie, Nature Structural and Molecular Biology 20 (9), 1054, 2013