Scientists determine 3D structure of proteins in living cells

A University of Glasgow scientist was part of a team of researchers, which has, for the first time, been able to determine the three-dimensional structure of protein in living cells.

The discovery, published in the latest edition of Nature, means scientists can now prove correct previous assumptions about the structure of proteins and how they change due to mutations and interactions with each other, as well as helping to find ways of correcting damage.

Since the 1950s, scientists have only been able to closely examine the structures of proteins in their extracted and purified form (in vitro) but these conditions are very different from those inside living cells (in vivo).

Using a nuclear magnetic resonance (NMR) spectrometer - a machine that allows the distances between the nuclei of atoms within a molecule to be measured - researchers were able to work out the three-dimensional shape of an example protein called TTHA1718, which was being produced in living cells of the bacterium E.coli.

Dr Brian Smith of the division of molecular and cellular biology at the University of Glasgow provided expertise that helped the Japan-based and funded international team to carry out the study.

Smith said: "Most proteins don"t exist in isolation; instead they live in a very crowded environment inside cells where they interact with other molecules and, critically, a large of class of proteins don"t have a definite three-dimensional structure when you take them out of living cells."

Using NMR spectroscopy means scientists can now establish the structure of proteins while still in live cells, which will tell them much more about how they work, and how they change when mutated.

Smith added: "Ultimately, it could help us discover whether drugs to correct damaged or mutated proteins are working and find new methods of fixing them."