Single-protein spin resonance spectroscopy under ambient conditions-Reference-Cited by-同舟云学术

Single-protein spin resonance spectroscopy under ambient conditions

Published:2015-03-06 Issue:6226 Volume:347 Page:1135-1138
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Shi Fazhan¹²³,Zhang Qi¹²,Wang Pengfei¹²³,Sun Hongbin⁴,Wang Jiarong⁴,Rong Xing¹²³,Chen Ming¹²,Ju Chenyong¹²³,Reinhard Friedemann⁵,Chen Hongwei⁴,Wrachtrup Jörg⁵,Wang Junfeng⁴,Du Jiangfeng¹²³

Affiliation:

1. Hefei National Laboratory for Physical Sciences at the Microscale and Department of Modern Physics, University of Science and Technology of China (USTC), Hefei 230026, China.

2. Joint Laboratory of Quantum Biophysics, USTC Institute of Biophysics and Chinese Academy of Sciences.

3. Synergetic Innovation Center of Quantum Information and Quantum Physics, USTC, Hefei 230026, China.

4. High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230000, China.

5. 3rd Physics and Integrated Quantum Science and Technology (IQST), University of Stuttgart, 70569 Stuttgart, Germany.

Abstract

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

Funder

Baden-Württemberg Stiftung

National Natural Science Foundation of China

Chinese Academy of Sciences

Max Planck Society

973 Program

European Union

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference36 articles.