Fig. 3: DAFS residue variants retain Vt structure and stability.
From: Molecular basis and cellular functions of vinculin-actin directional catch bonding
a Ribbon diagram of Vt with residues predicted to form DAFS interactions highlighted in blue and a key actin binding residue (I997) in grey licorice. b Far-UV CD spectral profiles of DAFS variants. c Near-UV spectral overlay of DAFS variants. d Melting temperature (TM) of DAFS variants calculated from CD thermal melt curves. Representative far-UV and near-UV CD spectral profiles shown are from N = 3 independent experiments. The CD thermal melt profiles are presented as an average of 3 scans from N = 3 independent experiments. Error in TM is shown with standard errors.
