Single-protein spin resonance spectroscopy under ambient conditions

Science

Volumn 347, Issue 6226, 2015, Pages 1135-1138

  Shi, Fazhan ^a,b,c   Zhang, Qi ^a,b   Wang, Pengfei ^a,b,c   Sun, Hongbin ^b   Wang, Jiarong ^b   Rong, Xing ^a,b,c   Chen, Ming ^a,b   Ju, Chenyong ^a,b,c   Reinhard, Friedemann ^d   Chen, Hongwei ^b   Wrachtrup, Jörg ^d,e   Wang, Junfeng ^b   Du, Jiangfeng ^a,b,c  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^c UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^d UNIVERSITY OF STUTTGART   (Germany)

^e WALTER SCHOTTKY INSTITUT   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DIAMOND; NITROGEN; POLYLYSINE; PROTEIN; PROTEIN MAD2; SPIN LABELING;

DETECTION METHOD; DIAMOND; ELECTRON SPIN RESONANCE; MAGNETIC FIELD; NITROGEN; ORIENTATION; PROTEIN; SENSOR; SPECTROSCOPY;

ACCELERATION; ARTICLE; BIOSENSOR; ELECTRON SPIN RESONANCE; NUCLEAR MAGNETIC RESONANCE; POLARIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; SPECTROSCOPY; SPIN LABELING; STRUCTURE ANALYSIS; ATOMIC FORCE MICROSCOPY; CHEMISTRY; MOLECULAR IMAGING; MOTION; PROCEDURES;

DIAMOND; ELECTRON SPIN RESONANCE SPECTROSCOPY; MAD2 PROTEINS; MICROSCOPY, ATOMIC FORCE; MOLECULAR IMAGING; MOTION; NITROGEN; POLYLYSINE; PROTEINS; SPIN LABELS;

EID: 84924358581     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaa2253     Document Type: Article

References (33)

1. L. Redecke et al., Science 339, 227-230 (2013).
2. T. R. M. Barends et al., Nature 505, 244-247 (2014).
3. M. C. Scott et al., Nature 483, 444-447 (2012).
4. C. C. Chen et al., Nature 496, 74-77 (2013).
5. P. P. Borbat, A. J. Costa-Filho, K. A. Earle, J. K. Moscicki, J. H. Freed, Science 291, 266-269 (2001).
6. D. Rugar, R. Budakian, H. J. Mamin, B. W. Chui, Nature 430, 329-332 (2004).
7. M. Xiao, I. Martin, E. Yablonovitch, H. W. Jiang, Nature 430, 435-439 (2004).
8. Y. Manassen, R. J. Hamers, J. E. Demuth, A. J. Castellano Jr., Phys. Rev. Lett. 62, 2531-2534 (1989).
9. G. Balasubramanian et al., Nature 455, 648-651 (2008).
10. J. R. Maze et al., Nature 455, 644-647 (2008).
11. J. M. Taylor et al., Nat. Phys. 4, 810-816 (2008).
12. G. Balasubramanian et al., Nat. Mater. 8, 383-387 (2009).
13. N. Bar-Gill, L. M. Pham, A. Jarmola, D. Budker, R. L. Walsworth, Nat. Commun. 4, 1743 (2013).
14. M. S. Grinolds et al., Nat. Phys. 9, 215-219 (2013).
15. B. Grotz et al., New J. Phys. 13, 055004 (2011).
16. A. O. Sushkov et al., Nano Lett. 14, 6443-6448 (2014).
17. L. S. Michel et al., Nature 409, 355-359 (2001).
18. S. Martin-Lluesma, V. M. Stucke, E. A. Nigg, Science 297, 2267-2270 (2002).
19. M. W. Doherty et al., Phys. Rep. 528, 1-45 (2013).
20. F. Z. Shi et al., Phys. Rev. B 87, 195414 (2013).
21. See supplementary materials on Science Online.
22. V. Gaponenko et al., Protein Sci. 9, 302-309 (2000).
23. J. A. Weil, J. R. Bolten, Electron Paramagnetic Resonance: Elementary Theory and Practical Applications (Wiley, New York, ed. 2, 2007), pp. 316-317.
24. K. Jacobsen, S. Oga, W. L. Hubbell, T. Risse, Biophys. J. 88, 4351-4365 (2005).
25. M. A. Hemminga, L. J. Berliner, ESR Spectroscopy in Membrane Biophysics (Springer Science and Business Media, New York, 2007), pp. 133-134.
26. T. Staudacher et al., Science 339, 561-563 (2013).
27. H. J. Mamin et al., Science 339, 557-560 (2013).
28. F. Z. Shi et al., Nat. Phys. 10, 21-25 (2014).
29. C. Müller et al., Nat. Commun. 5, 4703 (2014).
30. M. Schaffry, E. M. Gauger, J. J. L. Morton, S. C. Benjamin, Phys. Rev. Lett. 107, 207210 (2011).
31. A. O. Sushkov et al., Phys. Rev. Lett. 113, 197601 (2014).
32. M. S. Grinolds et al., Nat. Nanotechnol. 9, 279-284 (2014).
33. L. Luan et al., http://arxiv.org/abs/1409.5418 (2014).