Monday, 10 August, 2009

Single-molecule technique captures calcium sensor in action

Unknown workings of a signaling protein unfold in the hands of biophysicists

It's well known that the protein calmodulin specifically targets and steers the activities of hundreds of other proteins mostly kinases in our cells, thus playing a role in physiologically important processes ranging from gene transcription to nerve growth and muscle contraction But just how it distinguishes between target proteins is not well understood. Methods developed by biophysicists at the Technische Universität München (TUM) have enabled them to manipulate and observe calmodulin in action, on the single-molecule scale. In recent experiments, as they report in the early edition of PNAS, the Proceedings of the National Academy of Sciences, they compared the sequences of structural and kinetic changes involved in binding two different kinases. The results reveal new details of how calmodulin binds and regulates its target proteins. (...)

Press information TUM
Publication: "Single-molecule force spectroscopy distinguishes target binding modes of calmodulin"