Intermediate states of globular proteins during temperature-induced folding and unfolding studied using small angle x-ray scattering

The ability of proteins to change their conformation in response to changes in their environment has consequences in biological processes like metabolism, chemical regulation in cells, and is believed to play a role in the onset of several neurodegenerative diseases. Factors such as concentration, degree of crowding from other entities, and solvent medium affect how a protein folds. As a protein unfolds, the ratio of nonpolar to polar groups exposed to water changes, affecting a protein's thermodynamic properties. Using small angle x-ray scattering (SAXS), we are currently studying the intermediate protein conformations that arise during the folding/unfolding process as a function of temperature for a series of globular proteins. The temporal stability of these ensembles is also under investigation. Trends in the scattering profiles, along with correlations with protein thermodynamics, may help elucidate shared characteristics between all proteins in their folding behavior.