Triplet States Reveal Slow Local Dynamics in the Solvation Shell of Biomolecules.

Protein hydration shell dynamics plays a pivotal role in biochemical processes such as protein folding, enzyme function, molecular recognition and interaction with biological membranes. Thus, it is crucial to understand the mobility of the solvation shell at the surface of biomolecules. Triplet state solvation dynamics can reveal the slow dynamics of the solvation shell. This is done in the present work without adding separate dye molecules but instead by using a phosphorescent subgroup of the biomolecule itself. In particular, we study a small heptapeptide in a glycerol-water mixture under cryoconservation conditions so that the system can be supercooled without crystallization. We find a significant slowing of molecules in the solvation shell in the millisecond range compared to the bulk. This opens up the possibility to unravel the nature of relaxation processes in the solvation shell usually overlapping at room temperature.