From Interactions of Single Transmembrane Helices to Folding of α-Helical Membrane Proteins: Analyzing Transmembrane Helix-Helix Interactions in Bacteria

Dirk      Schneider; Carmen      Finger; Alexander      Prodohl; Thomas      Volkmer

Abstract

Despite a wide variety of biological functions, α-helical membrane proteins display a rather simple transmembrane architecture. Although not many high resolution structures of transmembrane proteins are available today, our understanding of membrane protein folding has emerged in the recent years. Now we begin to develop a basic understanding of the forces that guide folding and interaction of α-helical membrane proteins. Some structural requirements for transmembrane helix interactions are defined, and common motifs have been discovered in the recent years which can drive helix-helix interactions. Nevertheless, many open questions remain to be addressed in future studies. One general problem with investigating transmembrane helix interactions is the limited number of appropriate tools, which can be applied to investigate membrane protein folding. Only recently several new techniques have been developed and established, including genetic systems, which allow measuring transmembrane helix interactions in vitro and in vivo.

Keywords: Protein folding, GALLEX, helix interactions, membrane protein, helix packing, TOXCAT, transmembrane helix, Two-Stage-Model