Literature DB >> 11744192

Phase-fluorometry study on dielectric relaxation of acrylodan-labeled human serum albumin.

A Buzády1, J Erostyák, B Somogyi.   

Abstract

Dielectric relaxation (DR) of acrylodan-labeled human serum albumin (HSA/AC) was studied by phase-fluorometry. A non-monoexponential behavior of both the total fluorescence--and the DR decays has been found. The protein environment of the fluorescent marker shows DR times ranging from the pico to nanosecond timescale. In fluorescence emission decays measured on the red side of the fluorescence spectrum a time constant (<10 ps) affected by a negative preexponential was found supporting the existence of DR of the excited states.

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Year:  2001        PMID: 11744192     DOI: 10.1016/s0301-4622(01)00212-5

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  1 in total

1.  Ultrafast hydration dynamics in protein unfolding: human serum albumin.

Authors:  J K Amisha Kamal; Liang Zhao; Ahmed H Zewail
Journal:  Proc Natl Acad Sci U S A       Date:  2004-09-07       Impact factor: 11.205

  1 in total

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