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Substrates induce conformational changes in human anion exchanger 1 (hAE1) as observed by fluorescence resonance energy transfer

Authors :
Pal, Prithwish
Lebedev, Dmitry
Salim, Sara
Knauf, Philip A.
Source :
Biochemistry. May 23, 2006, Vol. 45 Issue 20, p6279, 17 p.
Publication Year :
2006

Abstract

Steady-state and time-resolved resonance energy transfer (FRET) techniques were used to determine the distance of the binding site for diTBA (bis-(1,3-diethylothiobarbituric acid)trimethine oxonol). The analysis indicates that diTBA binding site comes closer to the FM site by ~7 A in chloride buffer as compared to that in citrate because of the effects of anion binding.

Details

Language :
English
ISSN :
00062960
Volume :
45
Issue :
20
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.147457527