Distance Determination in Proteins inside Xenopus laevis Oocytes by Double Electron−Electron Resonance Experiments-Reference-Cited by-同舟云学术

Distance Determination in Proteins inside Xenopus laevis Oocytes by Double Electron−Electron Resonance Experiments

Published:2010-06-01 Issue:24 Volume:132 Page:8228-8229
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Igarashi Ryuji¹,Sakai Tomomi¹,Hara Hideyuki¹,Tenno Takeshi¹,Tanaka Toshiaki¹,Tochio Hidehito¹,Shirakawa Masahiro¹

Affiliation:

1. Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan, CREST, JST, Saitama 332-0012, Japan, Mitsubishi Kagaku Institute of Life Sciences, Tokyo 194-8511, Japan, Bruker Biospin K.K., Kanagawa 221-0022, Japan, Graduate School of Medicine, Kobe University, Hyogo 650-0017, Japan, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa 226-8501, Japan, and RIKEN, Yokohama Institute, Kanagawa 230-0045, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja906104e

Reference15 articles.

1. Protein Structure Determination Using Long-Distance Constraints from Double-Quantum Coherence ESR: Study of T4 Lysozyme

2. High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

3. In-Cell NMR Spectroscopy

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

5. Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)

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