Dresden 2017 – wissenschaftliches Programm
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MA: Fachverband Magnetismus
MA 64: Poster 1
MA 64.15: Poster
Freitag, 24. März 2017, 09:30–13:00, P2-EG
Measuring the spin-spin interaction on few doubly labeled proteins using NV-centers in diamonds — •Bastian Kern1, Lukas Schlipf1, Kebiao Xu1,2,3, Amit Finkler3, Markus Ternes1, Jörg Wrachtrup1,3, and Klaus Kern1,4 — 1MPI for Solid State Research, D-70569 Stuttgart, Germany — 2CAS Key Laboratory of Microscale Magnetic Resonance, USTC, 230026 Hefei, China — 33. Physikalisches Institut, Universität Stuttgart, D-70569 Stuttgart, Germany — 4Institut de Physique de la Matière Condensée, EPFL, CH-1015 Lausanne, Switzerland
Electron Paramagnetic Resonance (EPR) measurements of proteins labeled with two nitroxide spins have enabled the structural analysis of these proteins with sub-nm spatial resolution [1], with the main drawback of of large numbers of spins required for the experiment (∼1010 spins). Using an atomic scale sensor can lower this limit significantly. A system perfectly suited for this task are single nitrogen vacancy (NV) centers in diamonds [2]. For the first we time measure the interaction between nitroxide spin labels on doubly labeled proteins while only probing few (∼1-100) molecules with a triple electron resonance scheme at cryogenic temperatures: The dipolar interaction between the two spins on the protein, which is related to their distance, is detected using a nearby third electron spin of an NV center. These results show the capability of NV spin spectrometry in determining the distance between spin labels, using only few molecules.
[1] O. Duss et al, Nat. Comm. 5, 3669 (2014); [2] F. Jelezko, J. Wrachtrup, Phys. Stat. Sol. 203, 13, 3207-3225 (2006)