We describe a new methodology that combines high resolution magic angle spinning (HR-MAS) techniques with saturation transfer difference (STD) NMR spectroscopy. This approach significantly improves the versatility of the STD experiment, and expands its use for samples containing living cells derived from solid tissues

Airoldi, C., Giovannardi, S., LA FERLA, B., Jiménez Barbero, J., Nicotra, F. (2011). 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. CHEMISTRY-A EUROPEAN JOURNAL, 17(48), 13395-13399 [10.1002/chem.201102181].

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

AIROLDI, CRISTINA;LA FERLA, BARBARA;NICOTRA, FRANCESCO
2011

Abstract

We describe a new methodology that combines high resolution magic angle spinning (HR-MAS) techniques with saturation transfer difference (STD) NMR spectroscopy. This approach significantly improves the versatility of the STD experiment, and expands its use for samples containing living cells derived from solid tissues
Articolo in rivista - Articolo scientifico
HR-MAS; ligand–receptor interactions; membrane proteins; NMR spectroscopy; SGLT1 co-transporter
English
2011
17
48
13395
13399
none
Airoldi, C., Giovannardi, S., LA FERLA, B., Jiménez Barbero, J., Nicotra, F. (2011). 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. CHEMISTRY-A EUROPEAN JOURNAL, 17(48), 13395-13399 [10.1002/chem.201102181].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/25594
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