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Solvation dynamics in protein environments: Comparison of fluorescence upconversion measurements of coumarin 153 in monomeric hemeproteins with molecular dynamics simulations
2007
Journal of Chemical Physics
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The complexes of the fluorescence probe coumarin 153 with apomyoglobin and apoleghemoglobin are used as model systems to study solvation dynamics in proteins.Time-resolved Stokes shift experiments are compared with molecular dynamics simulations, and very good agreement is obtained. The solvation of the coumarin probe is very rapid with approximately 60% occurring within 300fs and is attributed to interactions with water (or possibly to the protein itself). Differences in the solvation
doi:10.1063/1.2753495
pmid:17688362
fatcat:hcsooshyejesla4sfm63umxyoq