Fig. 6: Folding and stability characterization of synthetic l- and d-monobodies.
From: Development of mirror-image monobodies targeting the oncogenic BCR::ABL1 kinase
a, b Representative analysis of purity of synthetic (a) l- and d-DAM21 and (b) l- and d-DAM27 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (performed at least twice). c, d Averaged far-UV circular dichroism (CD) spectra from three independent measurements of synthetic (c) l- and d-DAM27 and (d) l- and d-DAM21 in comparison with their recombinantly expressed analogues. Mean residue ellipticity (MRE) was calculated from three independent measurements. e Bar graph representation of thermal stability of recombinantly expressed and synthetic l- and d-monobodies assessed by nano differential scanning fluorimetry (nanoDSF). Melting temperatures (Tm) were measured at least three times (depicted as dots) and averaged. Error bars represent the standard deviation (SD). Source data of (a, b and e) are provided as a Source Data file.
