The inherent hydrophobicity of membrane proteins is a major barrier to membrane protein research and understanding. Their low stability and solubility in aqueous environments coupled with poor expression levels make them a challenging area of research. For many years, the only way of working with membrane proteins was to optimise the environment to suit the protein, through the use of different detergents, solubilising additives, and other adaptations. However, with innovative protein engineering methodologies, the membrane proteins themselves are now being adapted to suit the environment. This mini-review looks at the types of adaptations which are applied to membrane proteins from a variety of different fields, including water solubilising fusion tags, thermostabilising mutation screening, scaffold proteins, stabilising protein chimeras, and isolating water-soluble domains.
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December 2018
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Dysfunctional cytoskeleton and neurodegeneration: novel pathways in Parkinson's disease? This image represents the degeneration of the neuronal tree during the aging process. In this issue Civiero et al. discuss the consequence of impaired cytoskeletal dynamics on neurite morphology and neuronal physiology in Parkinson's disease. For further details see pages 1653–1663.
Review Article|
October 31 2018
Membrane protein engineering to the rescue
Andrea E. Rawlings
1Department of Chemistry, The University of Sheffield, Sheffield, U.K.
Correspondence: Andrea E. Rawlings (a.rawlings@sheffield.ac.uk)
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Publisher: Portland Press Ltd
Received:
August 04 2018
Revision Received:
September 03 2018
Accepted:
September 05 2018
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem Soc Trans (2018) 46 (6): 1541–1549.
Article history
Received:
August 04 2018
Revision Received:
September 03 2018
Accepted:
September 05 2018
Citation
Andrea E. Rawlings; Membrane protein engineering to the rescue. Biochem Soc Trans 17 December 2018; 46 (6): 1541–1549. doi: https://doi.org/10.1042/BST20180140
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