Abstract
The dielectric relaxation (DR) of human serum albumin (HSA) was studied by the method of phase-fluorometry. The protein environment of the single tryptophan in HSA shows a relatively low-speed DR of sub-ns characteristic time. This relaxation can be measured as a decaying red-shift of the time-resolved fluorescence emission spectra. The details of calculations of time–emission matrices (TEM) and comparison to the fluorescence data of the reference solution of N-acetyl- l-tryptophanamide (NATA) are also presented.
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