Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 44, Issue -, Pages 790-795Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20160025
Keywords
membrane proteins; protein engineering; protein stability; protein structure
Categories
Funding
- Engineering and Physical Sciences Research Council [EP/I032355/2]
- Biotechnology and Biological Sciences Research Council [BB/L013711/1]
- BBSRC [BB/L013711/1] Funding Source: UKRI
- EPSRC [EP/I032355/2] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L013711/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/I032355/2] Funding Source: researchfish
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Membrane proteins play crucial roles in cellular processes and are often important pharmacological drug targets. The hydrophobic properties of these proteins make full structural and functional characterization challenging because of the need to use detergents or other solubilizing agents when extracting them from their native lipid membranes. To aid membrane protein research, new methodologies are required to allow these proteins to be expressed and purified cheaply, easily, in high yield and to provide water soluble proteins for subsequent study. This mini review focuses on the relatively new area of water soluble membrane proteins and in particular two innovative approaches: the redesign of membrane proteins to yield water soluble variants and how adding solubilizing fusion proteins can help to overcome these challenges. This review also looks at naturally occurring membrane proteins, which are able to exist as stable, functional, water soluble assemblies with no alteration to their native sequence.
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