Journal
SCIENCE
Volume 347, Issue 6226, Pages 1135-1138Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaa2253
Keywords
-
Categories
Funding
- 973 Program [2013CB921800, 2012CB917202]
- National Natural Science Foundation of China [11227901, 91021005, 31470835, 11275183, 21103199]
- Chinese Academy of Sciences
- Max Planck Society
- European Union (via the ERC grant SQUTEC)
- European Union (via the ERC grant DIADEMS)
- Baden-Wurttemberg Stiftung
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available