The NEOtrap (Nanopore Electro-Osmotic trap) offers an entirely new, electrical and label-free way of protein sensing. A nano-cavity is formed by an origami structure docked onto a nanopore to electro-osmotically trap single proteins. We use it to detect proteins based on their mass & shape, and also to detect protein conformational dynamics. The label-free aspect as well as the vast electrical time bandwidth (microseconds to hours) represent unique advantages of the NEOtrap over alternative techniques.
Single-molecule Förster resonance energy transfer (smFRET) is a popular fluorescence-based technique to study protein conformational dynamics between two specific positions. We use smFRET to trace back the structural and energetic origins of protein conformational dynamics to elucidate the molecular basis of protein function. In addition, we develop new optical sensing schemes to detect and quantify linear & rotational single-molecule dynamics. We work closely together with the Hohlbein Lab at BIP, Wageningen.
Nanopore force spectroscopy
We use protein nanopore sensors to study DNA binding proteins, which allows us to locally apply force at a single un-modified protein. We use this technique to detect binding kinetics, specificity, conformational switching by hormones or mutations, etc. with excellent signal-to-noise ratio & label-free.
Photosynthesis is essential for virtually all life on Earth and powered by photosystems. Photosystem I (PS1) is the most efficient bio-nanomachine known to date. We aim to directly resolve the light-to-electron transfer kinetics (bursts, pauses) of a single PS1, which are inaccessible in bulk due to ensemble averaging.
In collaboration with Dr. Emilie Wientjes.