9. May 2007

Important protein-folding problem solved

Media Releases Biology Human Health

Coiled coils comprise two to five polypeptide chain helices that wrap around each other to form a supercoiled protein structure. They are implicated in a wide range of fundamental biological processes including DNA transcription, signal transduction, and intracellular transport. Furthermore, more than 7 percent of all amino acids encoded by the human genome are thought to be engaged in coiled-coiled interactions. Using a multidisciplinary approach, researchers at PSI, in collaboration with groups in the UK, USA and University of Zurich, discovered and characterized a short amino acid sequence, termed the trigger sequence, that is indispensable for the folding of coiled coils. The work represents a major advance in understanding of how coiled coils assume their specific three-dimensional structure, opening opportunities for the design of bioactive proteins based on coiled-coil motifs. The results were recently published in the renowned journal PNAS.

PNAS publication Molecular basis of coiled-coil formation, Vol. 104, No. 17 (Download PDF)