The brand-new Jean Jeener Bio-NMR Center at the VIB Department of Molecular and Cellular Interactions, Vrije Universiteit Brussel, has already played a role in a scientific breakthrough that made it into the leading science journal Cell. Thanks to NMR technology, it is possible to determine the dynamic structure of proteins. So Flemish scientists put it to use to find out how the activity of certain proteins involved in the stress physiology of bacteria is regulated. This is a first in every way.
Proteins, major players in the body
Proteins play a major role in the billions of processes that occur in the body, including the development of muscle and skin, the digestion of food, the growth of cells and the generation of human emotions. Our cells continuously produce proteins, but how these complex molecules exactly function is by and large not well understood.
Not only the chemical composition but also the spatial structure of proteins is important for the performance of their functions. The ways in which they fold and unfold in three-dimensional space help determine the function of the molecules. So, without detailed knowledge about their structure, our understanding of their function usually remains partial. However, studying the spatial structure of proteins is anything but easy.
Determination of protein structure necessary for understanding function
NMR is a promising technique for determining the structure of proteins in solution. Unlike X-ray diffraction long the standard for determining the structure of proteins NMR equipment can provide dynamic structure information. Even vibrations and rotations of molecules on an atomic scale can be visualized. The Bio-NMR center at the VIB Department of Molecular and Cellular Interactions, Vrije Universiteit Brussel, only opened May 7, 2010, but its 600-MHz and 800-MHz spectrometers have already helped produce a first article in a top journal.'/>"/>
|Contact: Joris Gansemans|
VIB (the Flanders Institute for Biotechnology)