Over recent years, much progress has been made in the identification and characterization of factors involved in the biosynthesis of integral membrane proteins of the helix-bundle type. In addition, our knowledge of membrane protein structure and the forces stabilizing helix—helix interactions in a lipid environment is expanding rapidly. However, it is still not clear how a membrane protein folds into its final form in vivo, nor what constraints there are on the folded structure that results from the mechanistic details of translocon-mediated assembly rather than simply from the thermodynamics of protein—lipid interactions.
Felix Nicolaus, Ane Metola, Daphne Mermans, Amanda Liljenström, Ajda Krč, Salmo Mohammed Abdullahi, Matthew Zimmer, Thomas F. Miller, Gunnar Von Heijne
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