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Single-protein spin resonance spectroscopy under ambient conditions

Single-protein spectroscopyThe 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).... Full description

Journal Title: Science March 6, 2015, Vol.347(6226), pp.1135-1138
Main Author: Shi, Fazhan
Other Authors: Zhang, Qi , Wang, Pengfei , Sun, Hongbin , Wang, Jiarong , Rong, Xing , Chen, Ming , Ju, Chenyong , Reinhard, Friedemann , Chen, Hongwei , Wrachtrup, Jorg , Wang, Junfeng , Du, Jiangfeng
Format: Electronic Article Electronic Article
Language: English
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ID: ISSN: 0036-8075 ; DOI: 10.1126/science.aaa2253
Link: http://search.proquest.com/docview/1904210649/?pq-origsite=primo
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title: Single-protein spin resonance spectroscopy under ambient conditions
format: Article
creator:
  • Shi, Fazhan
  • Zhang, Qi
  • Wang, Pengfei
  • Sun, Hongbin
  • Wang, Jiarong
  • Rong, Xing
  • Chen, Ming
  • Ju, Chenyong
  • Reinhard, Friedemann
  • Chen, Hongwei
  • Wrachtrup, Jorg
  • Wang, Junfeng
  • Du, Jiangfeng
subjects:
  • Labels
  • Magnetic Resonance
  • Proteins
  • Electron Paramagnetic Resonance
  • Diamonds
  • Biomolecules
  • Spectroscopy
  • Dynamics
  • Miscellaneous Sciences (So)
  • (An)
ispartof: Science, March 6, 2015, Vol.347(6226), pp.1135-1138
description: Single-protein spectroscopyThe 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...
language: eng
source:
identifier: ISSN: 0036-8075 ; DOI: 10.1126/science.aaa2253
fulltext: no_fulltext
issn:
  • 00368075
  • 0036-8075
url: Link


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titleSingle-protein spin resonance spectroscopy under ambient conditions
creatorShi, Fazhan ; Zhang, Qi ; Wang, Pengfei ; Sun, Hongbin ; Wang, Jiarong ; Rong, Xing ; Chen, Ming ; Ju, Chenyong ; Reinhard, Friedemann ; Chen, Hongwei ; Wrachtrup, Jorg ; Wang, Junfeng ; Du, Jiangfeng
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identifierISSN: 0036-8075 ; DOI: 10.1126/science.aaa2253
subjectLabels ; Magnetic Resonance ; Proteins ; Electron Paramagnetic Resonance ; Diamonds ; Biomolecules ; Spectroscopy ; Dynamics ; Miscellaneous Sciences (So) ; (An)
descriptionSingle-protein spectroscopyThe 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...
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titleSingle-protein spin resonance spectroscopy under ambient conditions
descriptionSingle-protein spectroscopyThe 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...
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abstractSingle-protein spectroscopyThe 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...
doi10.1126/science.aaa2253
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date2015-03-06