Keeping proteins on the straight and narrow: Molecular chaperones in the Archaea

For many years, studies on protein folding were done by biochemists and biophysicists using purified components and defined conditions. More recently, attention has shifted to thinking about protein folding in the messier internal environment of the cell. Here, proteins are faced with many hazards not encountered in the test tube: other proteins are present at high concentrations, the cell is full of membranes that need to be crossed, and conditions that can have a large effect on protein folding may not be constant. Proteins are often not well suited for these vagaries of cellular life, and a host of accessory proteins need to be present to assist the process of protein folding. These accessory proteins are referred to as molecular chaperones, and they use various mechanisms to make sure that their client proteins stay on the straight and narrow path to the folded active state.