Up to now, scientists were unsure what the protein looks like and how exactly it functions. Privatdozent [senior lecturer] Dr. Michael Schwake from the Faculty of Chemistry at Bielefeld University (Germany) is doing research on the protein - and thereby preparing the way for future therapies. Together with colleagues in Kiel, Toronto, and Boston, he has now discovered that the protein LIMP 2 possesses a novel protein fold together with a nanomicroscopically small transport tunnel. The researchers have published their findings on Sunday (27 October) in the globally renowned scientific journal
Proteins are composed of amino acids. Although these are lined up as if along a string, they produce a twisted three-dimensional structure of helices and sheets. It is only this pleating that enables them to influence biological cells. 'We are decoding the structure and function of proteins in order to find out how biochemical processes within them take place,' says Schwake.
To study LIMP-2, Schwake's colleagues from the Canadian University of Toronto have crystallized the protein. Then they can use X-ray diffraction analysis to ascertain its crystalline structure. 'When analysing the images, we detected a protein fold that has not been described in any other protein up to now,' says Schwake.