| Amide-Exchange-Rate-Edited NMR （AERE-NMR） Experiment： A Novel Method for Resolving Overlapping Resonances |
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| 引用本文： | 刘雪辉,林东海.Amide-Exchange-Rate-Edited NMR （AERE-NMR） Experiment： A Novel Method for Resolving Overlapping Resonances[J].中国化学,2007,25(3):411-416. |
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| 作者姓名： | 刘雪辉 林东海 |
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| 作者单位： | [1]School of Pharmaceutical Sciences, Peking University, Beijing 100083, China [2]Shanghai Institute ofMateria Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, China |
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| 基金项目： | Project supported by the National Natural Science Foundation of China （No. 30470351）.Acknowledgement We would like to thank Prof. Zhu G. and Dr. Sze K. H. for help with this work. We also thank Mr. Cheung K. K. for help with the backbone resonance assignment of the TCS protein. |
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| 摘 要： | This paper describes an amide-exchange-rate-edited （AERE） NMR method that can effectively alleviate the problem of resonance overlap for proteins and peptides. This method exploits the diversity of amide proton exchange rates and consists of two complementary experiments： （1） SEA （solvent exposed amide）-type NMR experiments to map exchangeable surface residues whose amides are not involved in hydrogen bonding, and （2） presat-type NMR experiments to map solvent inaccessibly buried residues or nonexchangeable residues located in hydrogen-bonded secondary structures with properly controlled saturation transfer via amide proton exchanges with the solvent. This method separates overlapping resonances in a spectrum into two complementary spectra. The AERE-NMR method was demonstrated with a sample of ^15N/^13C/^2H（70%） labeled ribosome-inactivating protein trichosanthin of 247 residues.
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| 关 键 词： | 酰胺交换速率编辑 核磁共振实验 NMR 重叠共振 解决办法 溶剂接触酰胺型 |
| 修稿时间： | 2006-04-102006-11-20 |
Amide-Exchange-Rate-Edited NMR （AERE-NMR） Experiment： A Novel Method for Resolving Overlapping Resonances |
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| LIU Xue-Hui, LIN Dong-Hai.Amide-Exchange-Rate-Edited NMR （AERE-NMR） Experiment： A Novel Method for Resolving Overlapping Resonances[J].Chinese Journal of Chemistry,2007,25(3):411-416. |
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| Authors: | LIU Xue-Hui LIN Dong-Hai |
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| Institution: | a School of Pharmaceutical Sciences, Peking University, Beijing 100083, China; b Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, China |
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| Abstract: | This paper describes an amide‐exchange‐rate‐edited (AERE) NMR method that can effectively alleviate the problem of resonance overlap for proteins and peptides. This method exploits the diversity of amide proton exchange rates and consists of two complementary experiments: (1) SEA (solvent exposed amide)‐type NMR experiments to map exchangeable surface residues whose amides are not involved in hydrogen bonding, and (2) presat‐type NMR experiments to map solvent inaccessibly buried residues or nonexchangeable residues located in hydrogen‐bonded secondary structures with properly controlled saturation transfer via amide proton exchanges with the solvent. This method separates overlapping resonances in a spectrum into two complementary spectra. The AERE‐NMR method was demonstrated with a sample of 15N/13C/2H(70%) labeled ribosome‐inactivating protein trichosanthin of 247 residues. |
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| Keywords: | NMR resonance overlapping amide-exchange-rate-edited SEA presat TROSY |
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