Proteins are the building blocks of life. They build our cells, send signals and transport substances. But they will only work correctly if they attain their exact 3-dimensional form. Gunnar von Heijne is demonstrating at a previously inconceivable level of detail how protein folding is achieved.
Every function in our bodies, from breathing to thinking, is controlled by proteins. These molecules are long chains of amino acids that are strung together in the cell’s protein factories – the ribosomes – based on blueprints from our DNA.
But the chain must be correctly folded if the protein is to work properly. If misfolding occurs, sticky clumps may form. These are associated with diseases such as Alzheimer’s, Parkinson’s and certain cancers.
Researchers have long studied protein folding outside the cell, in test tubes, by first unfolding complete proteins and then allowing them to regain their structure. But this method differs from the way the cell works in real life. Proteins often fold as they emerge, amino acid by amino acid, from ribosomes.
Gunnar von Heijne and his team have developed their own method, called “Force Profile Analysis” (FPA), which provides radical new insights into the protein folding process.
Membrane proteins serve a number of very important functions in both prokaryotic and eukaryotic cells. They are built according to structural principles different from those of globular proteins.
