The body's proteins carry out numerous functions and play a crucial role in the growth, repair and workings of cells. Sheena Radford, Professor of Structural Molecular Biology at the University of Leeds, says: "There's a fine balance between a protein folding into the correct shape so that it can carry out its job efficiently and it folding incorrectly, which can lead to disease. Just one wrong step can tip that balance."
Proteins are made of amino acids arranged in a linear chain and the sequence of these amino acids is determined by the gene producing them. How these chains of amino acids are preprogrammed to fold into their correct protein structure is one of the mysteries of life.
The culmination of many years' work, the collaborative study looked at the Im7 protein, a simple protein which is present in bacteria and has a crucial role to play in ensuring that bacteria do not kill themselves with the toxins they produce.
"Im7 is like an anti-suicide agent," says Professor Radford. "We studied it partly because of its simplicity and partly because of the known evolutionary pressure on the protein to fold correctly to enable the bacteria to survive."
The study has revealed that these proteins misfold en route to their intended structure, and importantly, has shown the forces at work during the folding process. While the chain of amino acids determines which shape a protein needs to take, the researchers discovered that it was the very amino acids central to the protein's function that were causing the misfolding.
"This breakthrough could have huge implications for understanding the evolution of today's protein sequences and in determining the balance between heath and disease," says Professor Radford. "It's fundamental science, but significant for our understanding of the mechanisms at work in the human body."
Jo Kelly | EurekAlert!
Cryo-electron microscopy achieves unprecedented resolution using new computational methods
24.03.2017 | DOE/Lawrence Berkeley National Laboratory
How cheetahs stay fit and healthy
24.03.2017 | Forschungsverbund Berlin e.V.
Astronomers from Bonn and Tautenburg in Thuringia (Germany) used the 100-m radio telescope at Effelsberg to observe several galaxy clusters. At the edges of these large accumulations of dark matter, stellar systems (galaxies), hot gas, and charged particles, they found magnetic fields that are exceptionally ordered over distances of many million light years. This makes them the most extended magnetic fields in the universe known so far.
The results will be published on March 22 in the journal „Astronomy & Astrophysics“.
Galaxy clusters are the largest gravitationally bound structures in the universe. With a typical extent of about 10 million light years, i.e. 100 times the...
Researchers at the Goethe University Frankfurt, together with partners from the University of Tübingen in Germany and Queen Mary University as well as Francis Crick Institute from London (UK) have developed a novel technology to decipher the secret ubiquitin code.
Ubiquitin is a small protein that can be linked to other cellular proteins, thereby controlling and modulating their functions. The attachment occurs in many...
In the eternal search for next generation high-efficiency solar cells and LEDs, scientists at Los Alamos National Laboratory and their partners are creating...
Silicon nanosheets are thin, two-dimensional layers with exceptional optoelectronic properties very similar to those of graphene. Albeit, the nanosheets are less stable. Now researchers at the Technical University of Munich (TUM) have, for the first time ever, produced a composite material combining silicon nanosheets and a polymer that is both UV-resistant and easy to process. This brings the scientists a significant step closer to industrial applications like flexible displays and photosensors.
Silicon nanosheets are thin, two-dimensional layers with exceptional optoelectronic properties very similar to those of graphene. Albeit, the nanosheets are...
Enzymes behave differently in a test tube compared with the molecular scrum of a living cell. Chemists from the University of Basel have now been able to simulate these confined natural conditions in artificial vesicles for the first time. As reported in the academic journal Small, the results are offering better insight into the development of nanoreactors and artificial organelles.
Enzymes behave differently in a test tube compared with the molecular scrum of a living cell. Chemists from the University of Basel have now been able to...
20.03.2017 | Event News
14.03.2017 | Event News
07.03.2017 | Event News
24.03.2017 | Materials Sciences
24.03.2017 | Physics and Astronomy
24.03.2017 | Physics and Astronomy