Solvation dynamics of DCM in human serum albumin
The Journal of Physical Chemistry B, 2001•ACS Publications
Solvation dynamics of 4-(dicyanomethylene)-2-methyl-6-(p-dimethylaminostyryl) 4 H-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.
(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.
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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