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Conformation of the C-terminal secretion signal of the Serratia marcescens haem acquisition protein (HasA) in amphipols solution, a new class of surfactant

Abstract : The conformation of a peptide, CterH, encompassing the last 56 C-terminal residues of Serratia marcescens haem acquisition protein HasA was examined by Circular Dichroism in amphipols solutions. The peptide, which contains the secretion signal of HasA, is unstructured in aqueous solution and adopts an helical structure upon the amphiphilic polymer addition. Furthermore, the helical content of CterH is modulated by the ionic strengh of the solution. These results are compared to those obtained with CterH in membrane mimetic environments.
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Submitted on : Monday, June 29, 2020 - 4:18:08 PM
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Nicolas Wolff, Muriel Delepierre. Conformation of the C-terminal secretion signal of the Serratia marcescens haem acquisition protein (HasA) in amphipols solution, a new class of surfactant. Journal de Chimie Physique et de Physico-Chimie Biologique, EDP Sciences, 1998, 95 (2), pp.437-442. ⟨10.1051/jcp:1998157⟩. ⟨pasteur-02884076⟩

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