Fig. 2From: Engineered mosaic protein polymers; a simple route to multifunctional biomaterialsCharacterisation of the Caf1A5I low stability mutant. (a) Near-UV circular dichroism thermal melt of the Caf1WT (adapted from [13]) and Caf1A5I proteins. Circular dichroism at 290 nm was followed as 1 mg/mL protein was heated between 25 and 95 °C, and the signal converted into fraction of protein folded. Data represent the average of three independent replicates. (b) SDS-PAGE analysis of Caf1WT and Caf1A5I proteins heated for 5 min in SDS containing sample buffer at the indicated temperatures. The position of the monomeric species is denoted by a star, with oligomeric breakdown products seen as a ladder within the region bounded by the bracketBack to article page