VATIS UPDATE Article

To help shed light on the workings of proteins, researcher Lukasz Kurgan, at Virginia Commonwealth University, the United States, has developed a series of bioinformatics programs to assist biologists in developing insights into the functions of intrinsically disordered proteins. This group of proteins lacks a fixed structure, which means they are totally or partially flexible and amorphous.

Over the last several decades, scientists have sequenced 85 million unique proteins, structured and unstructured alike, but still don’t know what the vast majority of these proteins do. As more proteins are discovered, more sophisticated computer programs must be developed to help determine their functions. “We have manually curated but understand less than 1% of these proteins, and right now there’s over 80 million to solve,” said Kurgan.

Determining a protein’s function becomes even more challenging when a protein is completely or partially disordered. When a protein does have a defined structure, researchers use prior knowledge and bioinformatics programs to first decipher that structure, which then helps determine function. If the protein is disordered, biologists turn to programs built by Kurgan and team that use predictive models to generate workable hypotheses on the protein’s function.