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![[Figure 2]](ol5291fig2mag.jpg)
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Figure 2
Synthesis, oxidative folding and disulfide mapping of conkunitzin-S1. (a) HPLC analysis of polypeptide fragments before chemical ligation (top trace) and after 10 h of chemical ligation (bottom trace). As ligation proceeded, peptides corresponding to amino acids 1–31 (aa 1–31) and 32–60 (aa 32–60) were covalently linked by a peptide bond to form the linear conkunitzin-S1 polypeptide (aa 1–60). The species labeled aa 1–31* is an intermediate encountered after transthioesterification of aa 1–31 with thiophenol. (b) HPLC analysis of intermediates encountered during oxidative folding of conkunitzin-S1. The fully reduced polypeptide (Linear, top trace) folded via single-disulfide (IA, IB, IC, ID) and non-native double-disulfide (IIA, IIB) intermediates to form one predominant fully oxidized product (Native, bottom trace). (c) Disulfide mapping confirms I–VI and III–V disulfide linkages in natively folded conkunitzin-S1. Peptide fragments were identified by mass spectrometry (Table 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) ). Peptides in peak b are related to peptides in peak a through the removal of two residues (NS) from the NSARKQCLRF peptide. Peptides in peak d are related to peptides in peak e through the removal of six N-terminal residues (KDRPSL). |
![[Figure 2]](ol5291fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
