In vitro selection of self-interacting transmembrane segments--membrane proteins approached from a different perspective.
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.
Langosch
Dieter
D
Lehrstuhl für Chemie der Biopolymere, TU München, D-85354 Freising-Weihenstephan, Germany. biopolymere@bl.tum.de
Lindner
Eric
E
Gurezka
Rolf
R
D020650:Combinatorial Chemistry Techniques; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*
D008565:Membrane Proteins