Despite the profound importance of chaperones to all proteins, the principles of their action remain surprisingly mysterious. We know that polypeptide chains fold into complex structures, but how can another protein help to solve this puzzle? The structure and function of chaperones like Hsp70 and GroEL has been studied extensively, but traditional methods are not well suited to detect the crucial conformational changes of their client proteins. Recently it has become possible to do so. We have pioneered the use of optical tweezers for this purpose, and for instance applied it to the chaperones SecB, Trigger Factor, and Hsp70 (Science 2007, Nature 2013, Nature 2016). We are integrating single-molecule fluorescence visualization at super-resolution precision, and developed methods to probe single actively translating ribosomes and their associated chaperones. In this project, you will measure the conformational and compositional dynamics of key chaperone systems for the first time, and further extend the capabilities of single-molecule detection.
Our research group focusses on three themes:
Past research topics include single-molecule studies on DNA packaging by bacterial viruses, and carbon nanotube-based electronics.
You need to meet the requirements for a doctors-degree and must have research experience in a non-Dutch academic environment. We are looking for an outstanding experimental physicist or chemist with an interest in single-molecule biophysics, and a strong drive to excel in a ambitious international environment.