FitFoldData: A Web-Based Toolkit for Circular Dichroism and Differential Scanning Calorimetry Data Analysis of Protein Thermal Denaturation.

This work presents FitFoldData, a novel web-based tool for the analysis and interpretation of thermal denaturation data collected from circular dichroism (CD) and differential scanning calorimetry (DSC) experiments. The analytical method employed is based on the recently reported modified Zimm-Bragg model, which includes hydrogen-binding interactions with solvent water. It leverages an intuitive interface, enabling users to efficiently analyze experimental data on heat-induced protein unfolding, interactively visualize results, and collect the relevant parameters. Detailed requirements of the data input format, preprocessing steps, fitting procedure, and visualization are described. One advantage of this approach is that it offers insights into the hydrogen-bonding energies, including both intramolecular and intermolecular contributions within the protein structure and with the surrounding water molecules. To assist users in effectively using and navigating the software tool, example pages and additional resources are also provided. FitFoldData provides researchers in molecular biology and biophysics with a fresh approach to the analysis of protein denaturation studied by CD or DSC and supplies new insights into the roles and energetics of hydrogen bonding in the temperature-dependent structural stability of protein molecules.