The Interdisciplinary Nanoscience Center at Aarhus University: Ground breaking study on membrane protein folding

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.

10 June 2015 by Rebeca Suarez Alvarez Thostrup

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.