Protein folding in membranes

作者：Fiedler Sebastian; Broecker Jana; Keller Sandro^*

来源：Cellular and Molecular Life Sciences, 2010, 67(11): 1779-1798.

DOI：10.1007/s00018-010-0259-0

• Hydrophobic effect
• Hydrogen bonds
• van der Waals forces
• Aromatic interactions
• Ion pairs
• Salt bridges
• Two-stage model
• Lateral pressure profile
• Hydrophobic mismatch
• Lipid bilayers
• Detergent micelles

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 alpha-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 alpha-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.

• 出版日期2010-6