3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy-Reference-Cited by-同舟云学术

3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy

Published:2016 Issue:67 Volume:52 Page:10237-10240
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Pan Bin-Bin¹²³⁴⁵,Yang Feng¹²³⁴⁵,Ye Yansheng⁶⁷⁸⁹¹⁰,Wu Qiong⁶⁷⁸⁹¹⁰,Li Conggang⁶⁷⁸⁹¹⁰,Huber Thomas¹¹¹²¹³¹⁴,Su Xun-Cheng¹²³⁴⁵

Affiliation:

1. State Key Laboratory and Research Institute of Elemento-Organic Chemistry

2. Collaborative Innovation Center of Chemical Science and Engineering (Tianjin)

3. Nankai University

4. Tianjin 300071

5. China

6. Key Laboratory of Magnetic Resonance in Biological Systems

7. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics

8. National Center for Magnetic Resonance in Wuhan

9. Wuhan Institute of Physics and Mathematics

10. Chinese Academy of Sciences

11. Research School of Chemistry

12. Australian National University

13. Canberra

14. Australia

Abstract

The integration of site-specific labeling of proteins with a stable lanthanide binding tag, paramagnetic NMR spectroscopy and the GPS-Rosetta program presents an effective and fast way of determining the three-dimensional structure of a protein in living cells.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CC/C6CC05490K

Reference44 articles.

1. High-Resolution Macromolecular NMR Spectroscopy Inside Living Cells

2. Methyl Groups as Probes for Proteins and Complexes in In-Cell NMR Experiments

3. In-cell NMR spectroscopy of proteins inside Xenopus laevis oocytes

4. Differential Dynamical Effects of Macromolecular Crowding on an Intrinsically Disordered Protein and a Globular Protein: Implications for In-Cell NMR Spectroscopy

5. In-cell NMR for protein-protein interactions (STINT-NMR)

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