作者: Andrea Buzády , János Erostyák , Béla Somogyi
DOI: 10.1016/S0301-4622(00)00210-6
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摘要: The dielectric relaxation (DR) of human serum albumin (HSA) was studied by the method phase-fluorometry. protein environment single tryptophan in HSA shows a relatively low-speed DR sub-ns characteristic time. This can be measured as decaying red-shift time-resolved fluorescence emission spectra. details calculations time-emission matrices (TEM) and comparison to data reference solution N-acetyl-L-tryptophanamide (NATA) are also presented.