ArticleJournal of fluorescence2015
Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.
Article in Journal of fluorescence, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.Journal of the Royal Society, Interface · 2023Article
- Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach.Emerging topics in life sciences · 2021Review
- Multiple Functions of Spectrin: Convergent Effects.The Journal of membrane biology · 2020Review
- Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift.The Biochemical journal · 2020Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brain spectrin enjoys overall structural and sequence similarity with erythroid spectrin, but less is known about its function. We utilized the fluorescence properties of tryptophan residues to monitor their organization and dynamics in brain spectrin. Keeping in mind the functional relevance of hydrophobic binding sites in brain spectrin, we monitored the organization and dynamics of brain spectrin bound to PRODAN. Results from red edge excitation shift (REES) indicate that the organization of tryptophans in brain spectrin is maintained to a considerable extent even after denaturation. These results are supported by acrylamide quenching experiments. To the best of our knowledge, these results constitute the first report of the presence of residual structure in urea-denatured brain spectrin. We further show from REES and time-resolved emission spectra that PRODAN bound to brain spectrin is characterized by motional restriction. These results provide useful information on the differences between erythroid spectrin and brain spectrin.
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