Protein Structure Dynamics and Function at Micelle and Particle Interfaces

This work is an investigation into how protein function and structural dynamics are affected by their interactions with detergents and particles. Recent studies have reported the addition of certain non-ionic surfactants increase the catalytic rates of enzymes. This is a departure from the established understanding of surfactant/protein interactions wherein charged-surfactants tend to denature the macro-molecular structure, while other detergents can be used to isolate and preserve protein structures. The mechanism of denaturation by ionic surfactants is well understood, as is the preservation and crystallization of protein structures with detergents. But why should non-ionic surfactants increase observed activity? This question remains unanswered. Furthermore, the explanations provided with previous studies where enzyme activity enhancement via surfactant interactions are inconsistent with each other, and are highly specific to the system in which they are studied. These contradicting conclusions highlight the need to propose a general theory of protein-surfactant interactions which can explain these reported changes in enzyme activity that can be applied to any of these reported