The trials and tribulations of membrane protein folding in vitro.
Membrane proteins are hard to handle and consequently the purification of functional protein in milligram quantities is a major problem. One reason for this is that once integral membrane proteins are outside their native membrane, they are prone to aggregation, are unstable and are frequently only partially functional. Knowledge of membrane protein folding mechanisms in vitro can help to understand the causes of these problems and work toward strategies to disaggregate and fold proteins correctly. Kinetic and stability studies are emerging on membrane protein folding, mainly on bacterial proteins. Mutagenesis methods have also been used to probe specific structural features or bonds in proteins. In addition, manipulation of lipid properties can be used to improve the efficiency of folding as well as the stability and function of the protein.
Booth
Paula J
PJ
Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, UK. paula.booth@bristol.ac.uk
D001426:Bacterial Proteins / Q000737:chemistry*; D003902:Detergents; D066298:In Vitro Techniques; D007700:Kinetics; D008563:Membrane Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011489:Protein Denaturation; D017510:Protein Folding; D012997:Solvents; D013816:Thermodynamics
D001426:Bacterial Proteins; D003902:Detergents; D008563:Membrane Lipids; D008565:Membrane Proteins; D012997:Solvents