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. 2015 Oct 28;5:15776. doi: 10.1038/srep15776

Figure 1. Structural characterization of BoNT/A peptide HN519-845.

Figure 1

(a) Amino acid sequence of the recombinant peptide HN519–845 prepared in the present work. The peptide consists partial belt sequence (519–546) along with two α-helical loops containing the full transmembrane region (618–661). (b) SDS-PAGE analysis of purified peptide HN519–845 showed a high yield of purified peptide (>95%) obtained from the inclusion bodies, purified using denaturing conditions. The peptide was refolded using 0.5% (w/v) sodium lauryl sarcosine. Lane M, Bio-Rad Precision Plus ProteinTM Dual Xtra Standard; Lane 1, purified HN519–845. (c) (i) The 3-dimensional structure of whole BoNT/A with individual domains marked (ii) the HN domain of BoNT/A with yellow region showing the part of belt region expressed in HN519–845.