Natalia Grytsyk, Stefan Haacke, Jérémie Léonard
Biomolecules bear a natural flexibility, which leads to the observation that they can exist in multiple conformations, like polymers. Structural heterogeneity and dynamics are an integral part of the biomolecules functional versatility and interactions. Characterizing structural heterogeneity in terms of relative abundance of different conformers, and resolving structural dynamics would allow a mechanistic understanding of biomolecular interactions at the molecular scale. This in turn would enable the rational design of innovative therapeutic strategies targeting specifically these interactions.
Our approach is to apply Time-Resolved Fluorescence (TRF) spectroscopy for the investigation of heterogeneous biomolecular systems tagged with different fluorescent labels, as reporters for the local conformations and transitions between the conformational states.