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Ground breaking study on membrane protein folding

Most detailed description of how membrane protein folds

The image shows which parts of the GlpG protein are the first to fold in the transition state (TS). The greener it is, the more coloured it gets. White shows that there is no structure in the TS, while red shows that this part of the protein has ‘overfolded’. Left: the actual 3D structure of the protein. Right: here the individual amino acid residues are shown in a model overview of the protein, where all 6 transmembrane helices (TM1–6) are visible, as well as the two helices (H1–2) and the loop, which is sticking out of the cell membrane.

For the last three decades, intense work has been carried out to understand how proteins fold, i.e. how they achieve their fine three-dimensional structure – which is also the basis for their biological function, regardless of whether it concerns metabolism, signal transfer or structure. The greatest progress by far has been made in water-soluble proteins, which are generally quite straightforward to work with.

Read more (in Danish only). 

Authors:

Paslawski, W., Kristensen, J. V., Lillelund, O., Schafer, N., Baker, R., Urban, S., and Otzen, D. E. (2015) Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and non-native loops, Proc. Natl. Acad. Sci. USA8. June 2015.

For more information, please contact

Professor Daniel Otzen
iNANO
dao@inano.au.dk
+45 2072 5238

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Revised 20.11.2024
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Annette Wandahl