REDOR Applications in Biology: An Overview
作者： Orsolya Toke , Lynette Cegelski
DOI: 10.1002/9780470034590.EMRSTM1152
关键词: Resonance (particle physics) 、 Chemical physics 、 Magic angle spinning 、 Protein–protein interaction 、 Heteronuclear molecule 、 Molecular systems 、 Direct measure 、 Chemistry 、 Magnetic dipole–dipole interaction 、 Nuclear magnetic resonance
摘要: Rotational echo double resonance (REDOR) is a solid-state NMR technique that provides direct measure of heteronuclear dipolar coupling typically between isolated pairs labeled nuclei under magic angle spinning conditions. The couplings contain information on both distance and orientation; therefore REDOR can serve as spectroscopic ruler protractor in the study molecular systems. In addition, it be used selection tool to filter spectra based couplings. Over past 20 years, has been employed around world obtain site-specific atomic-level metabolic pathways, protein-ligand interactions, analysis noncrystalline, poorly soluble heterogeneous systems such synthetic polymers, membrane proteins, intact plant leaves, bacterial cells cell walls. this review, we provide survey recent applications illustrate problem-solving versatility biological systems. Keywords: REDOR; dipolar couplings; magic-angle spinning; CPMAS; whole-cell NMR; antimicrobial peptides; protein–protein interaction; membrane proteins
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sci-hub.se 参考文章(80)
A James Mason, George J Turner, Clemens Glaubitz, None, Conformational heterogeneity of transmembrane residues after the Schiff base reprotonation of bacteriorhodopsin: 15N CPMAS NMR of D85N/T170C membranes. FEBS Journal. ,vol. 272, pp. 2152- 2164 ,(2005) , 10.1111/J.1742-4658.2005.04633.X
Chad M. Rienstra, Mary E. Hatcher, Leonard J. Mueller, Sun, Stephen W. Fesik, Robert G. Griffin, Efficient Multispin Homonuclear Double-Quantum Recoupling for Magic-Angle Spinning NMR: 13C−13C Correlation Spectroscopy of U-13C-Erythromycin A Journal of the American Chemical Society. ,vol. 120, pp. 10602- 10612 ,(1998) , 10.1021/JA9810181
Fernando Porcelli, Bethany Buck, Dong-Kuk Lee, Kevin J. Hallock, Ayyalusamy Ramamoorthy, Gianluigi Veglia, Structure and Orientation of Pardaxin Determined by NMR Experiments in Model Membranes Journal of Biological Chemistry. ,vol. 279, pp. 45815- 45823 ,(2004) , 10.1074/JBC.M405454200
Anil K. Mehta, Yuda Shayo, Hariprasad Vankayalapati, Laurence H. Hurley, Jacob Schaefer, Structure of a quinobenzoxazine--G-quadruplex complex by REDOR NMR. Biochemistry. ,vol. 43, pp. 11953- 11958 ,(2004) , 10.1021/BI049697H
Yasuto Todokoro, Ikuko Yumen, Kei Fukushima, Shin-Won Kang, Jang-Su Park, Toshiyuki Kohno, Kaori Wakamatsu, Hideo Akutsu, Toshimichi Fujiwara, Structure of Tightly Membrane-Bound Mastoparan-X, a G-Protein-Activating Peptide, Determined by Solid-State NMR Biophysical Journal. ,vol. 91, pp. 1368- 1379 ,(2006) , 10.1529/BIOPHYSJ.106.082735
Wei Liu, Jeffrey Z. Fei, Toru Kawakami, Steven O. Smith, Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52. Biochimica et Biophysica Acta. ,vol. 1768, pp. 2971- 2978 ,(2007) , 10.1016/J.BBAMEM.2007.10.011
Daniel R. Studelska, Lynda M. McDowell, Marc Adler, Robert D. O'Connor, Anil K. Mehta, William J. Guilford, Jerry L. Dallas, Damian Arnaiz, David R. Light, Jacob Schaefer, Conformation of a bound inhibitor of blood coagulant factor Xa. Biochemistry. ,vol. 42, pp. 7942- 7949 ,(2003) , 10.1021/BI027369G
Garry D. Dotson, Rajesh K. Dua, James C. Clemens, E. Wrenn Wooten, Ronald W. Woodard, Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR. Journal of Biological Chemistry. ,vol. 270, pp. 13698- 13705 ,(1995) , 10.1074/JBC.270.23.13698
Tsyr-Yan Yu, Jacob Schaefer, REDOR NMR Characterization of DNA Packaging in Bacteriophage T4 Journal of Molecular Biology. ,vol. 382, pp. 1031- 1042 ,(2008) , 10.1016/J.JMB.2008.07.077
Sung Joon Kim, Lynette Cegelski, Daniel R. Studelska, Robert D. O'Connor, Anil K. Mehta, Jacob Schaefer, Rotational-echo double resonance characterization of vancomycin binding sites in Staphylococcus aureus. Biochemistry. ,vol. 41, pp. 6967- 6977 ,(2002) , 10.1021/BI0121407