Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5402324 | Journal of Luminescence | 2010 | 5 Pages |
Abstract
The present work deals with fluorescence studies of adult porcine odorant binding protein at pH=7.5. At this pH, the protein is a dimer, each monomer contains one tryptophan residue. Our results show that tryptophan residue displays significant motions and emits with three fluorescence lifetimes. Decay associated spectra showed that the three lifetime's components emanate from sub-structures surrounded by the same microenvironment.
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Authors
Jihad René Albani,