Single-protein spin resonance spectroscopy under ambient conditions

Science  06 Mar 2015:
Vol. 347, Issue 6226, pp. 1135-1138
DOI: 10.1126/science.aaa2253

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Single-protein spectroscopy

The spin of a single nitrogen-vacancy (NV) center in diamond is a highly sensitive magnetic-field sensor. Shi et al. used the NV center to detect a nitroxidelabeled protein through electron spin resonance under ambient conditions (see the Perspective by Hemmer and Gomes). The strength of the interaction and the details of the hyperfine interaction between the electron and nitrogen spin revealed the position and orientation of the spin label relative to the NV center. The findings also elucidate the dynamical motions of the protein on the diamond surface.

Science, this issue p. 1135; see also p. 1072


Magnetic resonance is essential in revealing the structure and dynamics of biomolecules. However, measuring the magnetic resonance spectrum of single biomolecules has remained an elusive goal. We demonstrate the detection of the electron spin resonance signal from a single spin-labeled protein under ambient conditions. As a sensor, we use a single nitrogen vacancy center in bulk diamond in close proximity to the protein. We measure the orientation of the spin label at the protein and detect the impact of protein motion on the spin label dynamics. In addition, we coherently drive the spin at the protein, which is a prerequisite for studies involving polarization of nuclear spins of the protein or detailed structure analysis of the protein itself.

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