Journal
JOURNAL OF LUMINESCENCE
Volume 131, Issue 2, Pages 316-321Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2010.10.022
Keywords
Tryptophan; FRET; Relaxation dynamics; Transport protein
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Funding
- CSIR [01(2057)/06/EMR-II]
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This present investigation has revealed that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors for exploring the interaction of fluorescent probe 1-anthracene sulphonate (1-AS) with model transport proteins bovine serum albumin (BSA) and human serum albumin (HSA) We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to 1-AS for the study of relaxation dynamics of biological molecules (C) 2010 Elsevier BV All rights reserved
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