Saturation Transfer Difference NMR Experiments of Membrane Proteins in Living Cells under HR-MAS Conditions: The Interaction of the SGLT1 Co-transporter with Its Ligands

被引：34
作者：
Airoldi, Cristina [1 ]
Giovannardi, Stefano [2 ]
La Ferla, Barbara [1 ]
Jimenez-Barbero, Jesus [1 ,3 ]
Nicotra, Francesco [1 ]
机构：
[1] Univ Milano Bicocca, Dept Biotechnol & Biosci, I-20126 Milan, Italy
[2] Univ Insubria, Dept Biotechnol & Mol Sci, I-21100 Varese, Italy
[3] CSIC, Ctr Invest Biol, Madrid 28040, Spain
来源：
CHEMISTRY-A EUROPEAN JOURNAL | 2011年 / 17卷 / 48期
关键词：
HR-MAS; ligand-receptor interactions; membrane proteins; NMR spectroscopy; SGLT1; co-transporter; MOLECULAR RECOGNITION; STD-NMR; BINDING; SPECTROSCOPY; AFFINITY; INHIBITORS; TRANSPORTER; RECEPTOR; HSGLT1;
D O I：
10.1002/chem.201102181
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
With the magic roundabout: A new methodology that combines high-resolution magic angle spinning (HR-MAS) techniques with saturation transfer difference (STD) NMR spectroscopy is described. This approach significantly improves the versatility of the STD experiment, and expands its use for samples containing living cells derived from solid tissues (see figure). Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码：13395 / 13399
页数：5
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