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Data have been confirmed by binding studies with the N\u2010terminal truncated 180\u2010195 variant that displays a dissociation constant of 483 \u00b1 30 n<jats:italic>M<\/jats:italic>. Remarkably, TC does not influence the structure of the N\u2010terminally fluoresceinated peptides that both show \u03b1\u2010helical conformations. Docking calculations and molecular dynamics simulations suggest a direct, strong interaction of the antibiotic with exposed side chain functional groups of threonines 190\u2010193 on the solvent\u2010exposed surface of helix 2. Proteins 2007 \u00a9 2006 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.21204","type":"journal-article","created":{"date-parts":[[2006,12,6]],"date-time":"2006-12-06T23:47:33Z","timestamp":1165448853000},"page":"707-715","source":"Crossref","is-referenced-by-count":26,"title":["Does tetracycline bind helix 2 of prion? 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