Allemand co-pioneered single-molecule magnetic-tweezer manipulation of DNA and RNA, using calibrated magnetic forces/torques to measure the torsional and stretching mechanics of nucleic acids and the real-time kinetics of the motor proteins (helicases, polymerases, topoisomerases) that act on them. His joint lab with Vincent Croquette continues to develop new magnetic-tweezer instrumentation (including high-throughput and torque-sensing variants) applied to DNA replication, repair, and RNA processing machinery.
Ananthanarayanan was awarded the Royal Microscopical Society Life Sciences Award in 2025 for the use of novel microscopies in cell biology. Her group images individual motor proteins — dynein, kinesin — and the mitochondria they transport, in living cells, at single-molecule sensitivity, combining light-sheet and TIRF-class imaging with particle tracking to ask how organelle positioning and mitochondrial dynamics are controlled. The methodological emphasis is on getting single-molecule sensitivity inside a live cell rather than in vitro, which is the hard version of the problem. 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 — this is the closest thing at UNSW to a biological end-user for an in-cell quantum sensor: the mitochondrial systems she studies are precisely where NV nanodiamond thermometry and free-radical relaxometry at pT/sqrt(Hz) have been aimed, and she has the live-cell imaging infrastructure to validate any such measurement independently.
Uses optical and magnetic tweezers to study single-molecule mechanics and dynamics of molecular motors and nucleic-acid-processing enzymes with piconewton force resolution.
Croquette is a co-inventor of magnetic-tweezer single-molecule biophysics, applying it to helicase/topoisomerase mechanochemistry, DNA replication, and nucleic-acid mechanics; his group also develops complementary single-molecule readouts (stereo darkfield interferometry, mass photometry-adjacent tracking) for sub-nanometer 3D localization. He continues active, well-cited methodological development (e.g., recent reviews of magnetic-tweezer principles) alongside Jean-Francois Allemand.
Curmi is a structural and single-molecule biophysicist whose most-cited work is on the light-harvesting antenna proteins of cryptophyte algae, where he and collaborators reported long-lived electronic coherence at ambient temperature — one of the founding results of the quantum-biology field and still one of its most argued-over. His group determines the structures of these antenna complexes and engineers them, and separately works on protein-based molecular motors and on single-molecule fluorescence and FRET measurements of conformational dynamics. 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 — Curmi supplies the biological systems in which quantum coherence is actually claimed to matter; a pT/sqrt(Hz)-class spin sensor capable of watching radical-pair or exciton dynamics in situ would be aimed at exactly the questions his structures raise. Preferred attribute present: genuine quantum-biology substrate rather than a quantum-flavoured metaphor.
Needleman combines polarized-light microscopy, second-harmonic generation, single-molecule tracking, and fluorescence-lifetime (FLIM) metabolic imaging to study self-organization of the mitotic spindle and, in a clinically translated direction, non-invasive metabolic imaging of human oocytes and embryos for IVF viability assessment — an orientation- and lifetime-resolved imaging program with an active human-trial/clinical translation component.
Pincet uses optical-tweezer single-molecule force spectroscopy and single-molecule imaging to quantify the energetics and kinetics of protein-membrane interactions underlying vesicle docking and fusion (synaptotagmin/SNARE machinery), and — as a 2020 ERC Synergy laureate — is testing whether the secretory pathway is organized as self-assembling 2D liquid-crystalline protein domains. The lab combines force-clamp optical tweezers with real-time single-molecule imaging for unprecedented spatiotemporal resolution of individual protein-membrane binding events.
Rock builds custom single-molecule fluorescence microscopes and optical tweezers to directly watch individual myosin motors move along the actin cytoskeleton in vitro and in living cells, quantifying motor stoichiometry, force generation, and navigation rules that organize cell shape and motility. Where NV-ensemble quantum sensors read out spin ensembles magnetically at pT/sqrt(Hz) sensitivity via DEER/NMR/T1 protocols, Rock's approach achieves single-fluorophore and single-motor mechanical/positional resolution using all-optical single-molecule methods.
Yildiz uses nanometer-precision single-molecule fluorescence and optical/magnetic tweezers (FIONA-type localization) to resolve the stepping mechanisms of cytoskeletal motor proteins such as myosin, kinesin, and dynein in living cells.