title: Phase-fluorimetry study on dielectric relaxation of human serum albumin.
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.
authors.affiliation: Department of Experimental Physics, Institute of Physics, University of Pécs, Hungary. buzady@fizika.ttk.pte.hu
authors.forename: A
authors.initials: A
authors.lastname: Buzády
authors.forename: J
authors.initials: J
authors.lastname: Erostyák
authors.forename: B
authors.initials: B
authors.lastname: Somogyi
mesh_terms: D005453:Fluorescence; D005470:Fluorometry; D005990:Glycerol / Q000737:chemistry; D006801:Humans; D012709:Serum Albumin / Q000737:chemistry*; D013696:Temperature; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D012709:Serum Albumin; C016952:N-acetyltryptophanamide; D014364:Tryptophan; D005990:Glycerol