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NMR processing:
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Side-chains:
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Ab initio:
GeNMR
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
CSI (via RCI server)
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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From structure:
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PPM
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From sequence:
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Disordered proteins:
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Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
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camGroEL
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Selective Interface Detection: Mapping Binding Site Contacts in Membrane Proteins by NMR Spectroscopy
Suzanne R. Kiihne, Alain F. L. Creemers, Willem J. de Grip, Petra H. M. Bovee-Geurts, Johan Lugtenburg, and Huub J. M. de Groot
J. Am. Chem. Soc.; 2005; 127(16) pp 5734 - 5735

ABSTRACT:
Intermolecular contact surfaces are important regions where specific interactions mediate biological function. We introduce a new magic angle spinning solid state NMR technique, dubbed "selective interface detection spectroscopy" (SIDY). In this technique, 13C-attached protons (1Hlig) are dephased by 1H-13C REDOR. A spin diffusion period is then used to enhance long distance 1H-1H correlations, and the results are detected by a short period of cross polarization to the 13C isotope labels. This SIDY approach allows selective observation of the interface between 13C-labeled and unlabeled moieties. We have used SIDY to probe the ligand-protein binding surface between a uniformly isotopically labeled ligand cofactor, U-13C20-11-cis-retinal, and its binding site in rhodopsin (Rho), an unlabeled, membrane-embedded G-protein coupled receptor (GPCR). The observed 1HGPCR-13Clig correlations indicate multiple close contacts between the protein and the ionone ring of the ligand, in agreement with binding studies. The polyene tail of the ligand displays fewer strong correlations in the SIDY spectrum. Some correlations can be assigned to the protein side chains lining the ligand binding site, in agreement with the crystal structure.
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