title: Large-scale production of functional membrane proteins.
abstract: The preparation of sufficient amounts of high-quality samples is still the major bottleneck for the characterization of membrane proteins by in vitro approaches. The hydrophobic nature, the requirement for complicated transport and modification pathways, and the often observed negative effects on membrane properties are intrinsic features of membrane proteins that frequently cause significant problems in overexpression studies. Establishing efficient protocols for the production of functionally folded membrane proteins is therefore a challenging task, and numerous specific characteristics have to be considered. In addition, a variety of expression systems have been developed, and choice of appropriate techniques could strongly depend on the desired target membrane proteins as well as on their intended applications. The production of membrane proteins is a highly dynamic field and new or modified approaches are frequently emerging. The review will give an overview of currently established processes for the production of functionally folded membrane proteins.
authors.affiliation: Centre for Biomolecular Magnetic Resonance, University of Frankfurt/Main, Institute for Biophysical Chemistry, Frankfurt/Main, Germany.
authors.forename: F
authors.initials: F
authors.lastname: Junge
authors.forename: B
authors.initials: B
authors.lastname: Schneider
authors.forename: S
authors.initials: S
authors.lastname: Reckel
authors.forename: D
authors.initials: D
authors.lastname: Schwarz
authors.forename: V
authors.initials: V
authors.lastname: Dötsch
authors.forename: F
authors.initials: F
authors.lastname: Bernhard
mesh_terms: D000818:Animals; D002474:Cell-Free System; D015870:Gene Expression; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007313:Insecta / Q000166:cytology; D008565:Membrane Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D015394:Molecular Structure; D011487:Protein Conformation; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D015003:Yeasts / Q000166:cytology / Q000502:physiology
chemical_list: D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins