The DyCTheMS project proposes a new experimental approach to the conformational dynamics and thermodynamics of micro-solvated biomolecules, based on ion mobility spectrometry (IMS) and mass spectrometry (MS). The thermodynamics of structural transitions in those systems will be probed using an original calorimetry technique based on IMS measurements. Complementary temperature-dependent isomerization dynamics data will also be collected from tandem-IMS measurements. An originality of the proposal lies in the attempt to bridge the gap between solution and gas-phase measurements by probing how the conformational landscape of a molecular system is modified upon solvation. In particular we will shed light on the extent of solvation required for a biomolecule to exhibit “native” conformational properties. After a validation phase on well-characterized systems, the above procedures will be used to gain insight in the binding-induced structuration of an intrinsically disordered peptide.