Publication | Closed Access
Solvation Dynamics of DCM in Human Serum Albumin
109
Citations
52
References
2001
Year
Protein ChemistrySolvation DynamicsMolecular SpectroscopyDcm BoundBiophysical ModelingBiochemistryProtein FoldingNatural SciencesExperimental BiophysicsBiophysical AspectHuman Serum AlbuminMolecular BiophysicsAnalytical UltracentrifugationMedicineBiophysicsSolution (Chemistry)
Solvation dynamics of 4-(dicyanomethylene)-2-methyl-6-(p-dimethylaminostyryl) 4H-pyran (DCM) in aqueous solution of a protein, human serum albumin (HSA), is studied using picosecond time-resolved emission spectroscopy. The solvation dynamics of DCM bound to HSA is found to be biexponential with one component of 600 ± 100 ps (25%) and a very long component of 10 ± 1 ns (75%). This indicates that the motion of the water molecules in the vicinity of the protein is highly constrained.
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