Thermodynamic stability of de novo designed protein mini-binders as assessed by combined thermal and chemical denaturation - Data set

Experimental data for the paper: "Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins" by Vili Lampinen; Osvaldo Burastero; Iara Plácido Guazzelli; Florian Vögele; Francisca Pinheiro; Jan S. Nowak; Maria M. Garcia Alai; Magnus Kjaergaard.The data set contains nanoscale differential scanning fluorimetry (nanoDSF) data for unfolding of 15 de novo designed protein mini-binders. The nanoDSF data is recorded at different concentrations of chemical denaturant (GdmCl) to allow global fitting of the unfolding data. The data set contains screening data for 35 proteins at 3 denaturant concentrations, and titration data for 15 proteins that showed measurable unfolding transition in the initial screen.Additionally, data set also contains CD spectra recorded for 5 proteins that did not show a detectable unfolding curve recorded at 25 and 95 degres Celsius at 0 and 6M GdmCl.The parent folder contains index files describing the experimental data, and spreedsheet with thermodynamics fitting parameters (ΔH, ΔCp, and Tm) determined from CheMelt.