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• W2048606419 endingPage "535" @default.
• W2048606419 startingPage "526" @default.
• W2048606419 abstract "The structure and flexibility of the biologically important alpha-spectrin amino terminal region was examined by the use of fluorescence and EPR spectroscopy. The region studied has been previously demonstrated to be essential for the alpha-spectrin:beta-spectrin association of the tetramerization site. Appropriate spectroscopic probe moieties were coupled to this region in a recombinant fragment of human erythroid alpha-spectrin. There was good agreement between the EPR and fluorescence techniques in most of this region. Mobility determinations indicated that a portion of the region was relatively immobilized. This is significant, since although predictive methods have indicated that this region should be alpha-helical, previous experimental evidence obtained on smaller synthetic peptides had indicated that this region was disordered. Observed rigidity appears to be incompatible with such a disordered state, and has important ramifications for the flexibility of this molecule that is so integral to its role in stabilizing erythrocyte membranes." @default.
• W2048606419 created "2016-06-24" @default.
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• W2048606419 date "2000-07-01" @default.
• W2048606419 modified "2023-09-26" @default.
• W2048606419 title "Flexibility of the α-Spectrin N-Terminus by EPR and Fluorescence Polarization" @default.
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• W2048606419 doi "https://doi.org/10.1016/s0006-3495(00)76314-4" @default.
• W2048606419 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1300956" @default.
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