Fig. 2: β-helix folding and assembly.
From: A self-assembled protein β-helix as a self-contained biofunctional motif
a XRD patterns for SaBeH (black) and a non-assembly control peptide (green). X-ray counts are shown versus both 2θ (left) and d-spacings (right). b Ramachandran plot for SaBeH as in Fig. 1f. c FT-IR spectrum (upper) and its 2nd derivative (lower) for SaBeH. d CD spectra for SaBeH at different concentrations. e Electron and f atomic force micrographs of SaBeH. Scale bars are 200 nm. Colour (height) scale bar is 34 nm. g Atomic force micrographs of individual SaBeH cylinders highlighting a left-handed twist with a pitch of 28.5 ± 7.3 nm indicated by a double-headed arrow. Scale bars are 5 nm. Colour (height) scale bar is 6 nm. Assembly conditions: 100 μM (unless stated otherwise) in 10 mM 3-(Morpholin-4-yl)propane-1-sulfonic acid (MOPS), pH 7.4, at room temperature. Images in (e–g) are representative of at least 3 independent experiments.
