The delicate balance between apolar packing and hydrogen bonding determines membrane protein assembly and function

Abstract

The apolar environs of the lipid membrane changes how the different forces that dictate assembly, such as the hydrophobic burial, apolar packing (e.g. van der Waals interactions), and polar interactions, contribute to the folding of membrane proteins. In the membrane, the hydrophobic burial contributes very little; instead, apolar packing and hydrogen-bonding play significant roles in the assembly, and, ultimately, the function of membrane proteins. In this work, we dissect the contributions of these two forces in mediating the association of transmembrane helices.