In Vitro Selection of Self‐Interacting Transmembrane Segments‐‐Membrane Proteins Approached from a Different Perspective

Abstract
The principles underlying the folding of integral membrane proteins are uncovered in an increasingly detailed way. Experimental determination of high‐resolution structures followed by analysis of packing reveal structural similarities as well as differences to soluble globular proteins. At the same time, protein/protein interactions at the level of membrane‐embedded domains have been investigated for different model proteins. More recently, self‐interacting transmembrane helices have been selected from combinatorial libraries in vitro to study the mechanistic basis of protein/protein interaction in membranes in a systematic way. With an emphasis on the latter approach, this review discusses insights emerging from an integrated view on the recent advances.

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