[en] Previous NMR studies on surfactin proposed two γ or β-turn-containing conformers while recent CD studies described β-sheets and α-helices in surfactin. Since these data were not obtained in the same conditions, the conformation of surfactin was reinvestigated by FTIR spectroscopy, a diagnostic method for β-sheets. In trifluoroethanol, the FTIR spectra of surfactin and its diester are compatible with γ and/or β-turn(s) and the differences in their CD spectra show the importance of the Glu¹ and Asp⁵ COOH groups in stabilizing the lipopeptide conformation. The calcium-induced spectral changes of both lipopeptides suggest a first binding of the divalent ions to the surfactin COOH groups (until calcium-lipopeptide mole ratio reached 1) followed by bulk conformational changes (at higher mole ratios). In Tris buffer at pH 8.5, the FTIR amide I band shape, without the typical 1610-1628 and 1675-1695 cm^-1 bands, ascertains the absence of β-sheets