Graphical abstract for pre-print showing a) theoretical model for thermostability, b) a GUI based analysis platform, c) protein denaturation data of mini-binders assessed by nanoDSF and d) a correlation plot that shows the de novo designed mini-binders have a much lower deltaCp than expected for a protein of their size.
Why are de novo designed proteins so extremely thermostable?
We try to answer this question by dissecting the thermodynamics of unfolding of mini-binders emerging from our protein design pipeline โ and establish a convenient GUI for data analysis in the process.
doi.org/10.64898/202...