Thermal properties of bacteriorhodopsin

In this Feature Article we review the effects of various parameters on the structure and thermal stability of one of the most widely studied membrane proteins, bacteriorhodopsin. This protein has recently been crystallized and its high-resolution structure elucidated to 1.55 Angstrom. This information has proved invaluable in understanding its proton-pumping mechanism. However, the question of why bacteriorhodopsin is so stable over a wide range of conditions, and which factors contribute to this stability, is still largely unanswered. Spectroscopic and calorimetric experiments provide information on the thermodynamics, kinetics and structural changes upon unfolding and refolding the protein under various environmental perturbations. FT-IR spectroscopy has been particularly useful in determining the changes in secondary structure upon heating through its thermal transitions after changing pH and cations, removing and adding lipids and detergents, retinal reduction and removal, and site-directed mutagenesis. These experiments are reviewed, and the information that they have afforded have been brought together to try to understand how nature has controlled the conditions of bR to make it one of the most stable proteins known.