Protein equilibrium population snapshot hydrogen deuterium exchange electrospray ionization mass spectrometry measurements of the stability of wildtype human acidic fibroblast growth factor and the R136D variant

Methods for probing protein unfolding, which can compare the stability of wildtypes with variants, may contribute significantly to our understanding of protein structure and provide data for evaluating predictive tools or folding mechanisms. Methods have been developed for this, each with limitations, constraints, or biases. Additional methods probing the same properties but using different principles or approaches could help mitigate the limitations of individual methods, especially if they demonstrate comparable results.