Membrane protein folding and stability

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There’s no doubt: membrane proteins are difficult to work with. They don’t express to very high levels in heterologous systems. Once expressed they are often tricky to extract from the membrane fraction (and even more difficult to solubilize and fold if expressed as inclusion bodies), and have an annoying tendency to aggregate and become inactivated. Finally, getting them to fold reversibly in a bona fide membrane environment is a real challenge. But all these challenges are also in a sense exhilarating: we can learn so much about what really makes proteins “tick” by comparing their properties with those of water-soluble proteins – almost like wising up to our own understanding of life by studying alien life forms. So although membrane protein structures only make up around 2% of the protein structure data base (and roughly the same can be said about biophysical studies), all such insights are bound to make a real impact. The pace is picking up, and we can cheerfully estimate that we are only 30 years behind our water-soluble colleagues in structural determination. The present collection of articles, contributed by leading experts in the field, is an attempt to present some of the insights we already have and point out ways in which to direct our future explorations
Original languageEnglish
JournalArchives of Biochemistry and Biophysics
Pages (from-to)262-264
Number of pages3
Publication statusPublished - 15 Dec 2014


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