Function in biomolecules is driven by dynamics, but measuring and characterizing motion is not trivial, whereas a static structure may not tell the full story. Nuclear magnetic resonance is uniquely suited to charactize dynamics in biomolecules, providing bond-specific and timescale-specific measurement of dynamics. An array of available experiments allows one to characterize motions ranging from microseconds to milliseconds.
However, experimental data is not always straightforward to correctly interpret. Therefore, we support experimental data with molecular dynamics simulation (MD), allowing one to better understand origin the of the observed dynamics.
We use dynamics detectors for the analysis of experimental and simulated data. Detectors allow timescale-specific parameterization of motional amplitudes, without knowledge of the exact model of motion. This makes them particularly well suited for comparing dynamics between both different experimental conditions (samples, temperature, etc.) and methods (e.g. MD simulation). Additionally, we develop dynamic models for experimental dynamic analysis from experimental and simulated results, with models depending on molecular structure (α-helices, β-sheets, etc.), and verify the robustness of those models under various conditions.
We are particularly interested in membranes and membrane proteins, where we use detectors for comparative dynamics analysis, and determine how different structures can be modeled with different dynamic models. Such models are used to separate dynamics intrinsic to a given structure from functional dynamics– motions allowing signaling, binding etc.