Protein folding in membranes |
| |
Authors: | Sebastian Fiedler Jana Broecker Sandro Keller |
| |
Institution: | 1. Leibniz Institute of Molecular Pharmacology (FMP), Robert-R?ssle-Str. 10, 13125, Berlin, Germany 2. Molecular Biophysics, University of Kaiserslautern, Erwin-Schr?dinger-Str. 13, 67663, Kaiserslautern, Germany
|
| |
Abstract: | Separation of cells and organelles by bilayer membranes is a fundamental principle of life. Cellular membranes contain a baffling
variety of proteins, which fulfil vital functions as receptors and signal transducers, channels and transporters, motors and
anchors. The vast majority of membrane-bound proteins contain bundles of α-helical transmembrane domains. Understanding how
these proteins adopt their native, biologically active structures in the complex milieu of a membrane is therefore a major
challenge in today’s life sciences. Here, we review recent progress in the folding, unfolding and refolding of α-helical membrane
proteins and compare the molecular interactions that stabilise proteins in lipid bilayers. We also provide a critical discussion
of a detergent denaturation assay that is increasingly used to determine membrane-protein stability but is not devoid of conceptual
difficulties. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|