Hydrophobic interactions urea-denatured unfolded proteins

When a protein is adsorbed to a hydrophobic surface, denaturation is often not an instantaneous phenomenon. Thus, the extent of unfolding will increase with increasing time of adsorption. Both Karger and Hearn et al. [40] have monitored this residency effect on reversed-phase and hydrophobic interaction columns using a combination of techniques including derivative spectroscopy. The Hearn group also studied denaturation kinetics in size exclusion chromatography in the presence of the powerful denaturant urea. 

---