Abstract
We study the ultrafast solvation dynamics of protein-precipitant complexes. Protein subtilisin carlsberg (SC) was mixed with several polyethylene glycol (PEG) precipitants for protein crystallization. Picosecond-resolved emission spectra from single intrinsic tryptophan residue (Trp-113) are recorded to construct solvation correlation functions. For precipitant concentrations with various crystallization effects, we observe drastically different solvation relaxation processes. These differences in solvation dynamics are correlated with the local protein structural integrity and water-network stability upon interaction with the precipitants. The solvation dynamics at the protein surface is proposed as a new perspective to study precipitant-protein interactions.
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