Researchers at, among others, the University of Gothenburg and Linnaeus University have found evidence that wave mechanics determines what structure is possible in a protein molecule. The results increase the understanding of protein dynamics and may be important for protein design which, in turn, is important for medicine and biotechnology.
Proteins are large molecules that play an essential role to life. The dynamics of proteins, i.e. how their structure develops and changes, is crucial for their activity, but difficult to follow experimentally. In particular, the role of low frequency vibrations of individual atoms, which are rather subtle on protein dynamics, has been unknown. To understand how the process that results in a final shape for a protein molecule works is important, in order to design and produce proteins for e.g. medicines.
Through the use of new instrumentation and elegant experimental preparation, a group of scientists led by professor Gergely Katona of the University of Gothenburg have managed to follow on the atomic displacements in a protein crystal. This was done following irradiation by a so-called Terahertz radiation source, which emits low frequency radiation in the interval between microwaves and infrared light.
Ran Friedman, associate professor and computational chemist at Linnaeus University, participated in the theoretical analysis of the results.
"This study pushes the boundary of experimental detection of protein dynamics", he says. "At this point, we need to work hard and further develop a theoretical framework to enable better analysis of such experiments. Fortunately, we managed to secure support from the LINXS, Lund Institute of advanced Neutron and X-ray Science, for this purpose, for which we are very grateful."
- Read more in the press release from the University of Gothenburg (in Swedish)
- Read the entire article Clustering of atomic displacement parameters in bovine trypsin reveals a distributed lattice of atoms with shared chemical properties at Scientific Reports