Applies advanced single-molecule biosensing to study the cyanobacterial circadian clock — the only fully reconstitutable in vitro biochemical oscillator. Directions: (1) single-molecule FRET and fluorescence imaging to track conformational states of KaiC ATPase during clock cycles with single-protein resolution; (2) single-molecule reconstitution of the complete KaiA/KaiB/KaiC oscillator; (3) mathematical modeling of biochemical oscillation. Technique focus: single-molecule fluorescence as quantitative biosensing tool for protein conformational dynamics. Joint appointment Microbiology.

Sierecki co-developed the cell-free single-molecule interaction platform with Gambin and runs a group applying it to protein interaction networks: mapping which proteins bind which, with what affinity and in what stoichiometry, at throughput high enough to screen rather than characterise one pair at a time. Recent applications include viral protein-host interactions and transcription factor complexes. Positioned against the established body of NV-ensemble quantum sensing work — DEER, nanoscale NMR and T1 relaxometry protocols operating at pT/sqrt(Hz) field sensitivity — the relevance to a quantum-sensing candidate is as a source of well-characterised, quantitatively-defined biological targets: a pT/sqrt(Hz)-class sensor is only useful in biology if someone can tell you exactly what molecular species is present and at what concentration, which is what this platform delivers. Borderline inclusion — no quantum or physics-instrumentation component — kept because single-molecule technique development is the core of the group.