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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
Author(s) -
Airoldi Cristina,
Giovannardi Stefano,
La Ferla Barbara,
JiménezBarbero Jesús,
Nicotra Francesco
Publication year - 2011
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201102181
Subject(s) - magic angle spinning , saturation (graph theory) , spinning , membrane , chemistry , analytical chemistry (journal) , magic angle , nuclear magnetic resonance spectroscopy , biological system , materials science , stereochemistry , chromatography , biochemistry , polymer chemistry , biology , mathematics , combinatorics
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).