ABSTRACT
Studies of the denaturation or unfolding of soluble proteins have increased our understanding of the energetics of protein folding and the mechanisms of protein stabilization [1-5]. However, the application of these concepts to transmembrane proteins remains complex. While soluble proteins generally assume a structure that sequesters the polar amino acids from water, membrane proteins must assume a structure that accommodates three different environments. This has implications for both the stability of membrane proteins as well as the folding pathway.
