Abstract
Reverse micelles are a versatile model system for the study of crowded microenvironments containing limited water, such as those found in various tissue spaces or endosomes. They also preclude protein aggregation. Reverse micelles are amenable to study by linear and nonlinear infrared spectroscopies, which have demonstrated that the encapsulation of polypeptides and enzymatically active proteins into reverse micelles leads to conformational changes not seen in bulk solution. The potential value of this model system for understanding the folding and kinetic behavior of polypeptides and proteins in biologically important circumstances warrants increased study of reverse micelle systems by infrared spectroscopy. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.