Identification of Shallow and Deep Membrane-penetrating Forms of Diphtheria Toxin T Domain That Are Regulated by Protein Concentration and Bilayer Width

The α-helix-rich, hydrophobic transmembrane (T) domain of diphtheria toxin is believed to play a central role in membrane insertion by the toxin and in the translocation of its catalytic domain across membranes. In this report, T domain structure was studied using site-directed single-Cys mutants. T...

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Veröffentlicht in:The Journal of biological chemistry 1997-10, Vol.272 (40), p.25091-25098
Hauptverfasser: Wang, Yang, Malenbaum, Susan E., Kachel, Kelli, Zhan, Hangjun, Collier, R. John, London, Erwin
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Sprache:eng
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