NMR paper Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis

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[NMR paper] Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis

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Ab initio:

Fragment-based:

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Torsion angles from chemical shifts:

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Promega- Proline

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TALOS

MICS caps, β-turns

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PECAN

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RCI

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ArShift- Aromatic

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11-24-2010, 08:49 PM

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Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis

Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy.

Related Articles Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy.

J Am Chem Soc. 2002 Feb 27;124(8):1778-81

Authors: Luchette PA, Prosser RS, Sanders CR

Oxygen solubility increases toward the hydrophobic interior of membranes. Using NMR, this O(2) solubility gradient gives rise to an exquisite range of position-dependent paramagnetic effects at partial pressures of 100 atm (PO(2)), which may be used to probe membrane protein structure and positioning. In this study, fluorinated probes were introduced at selected positions of the transmembrane 1 domain of the intact homotrimer of the integral membrane protein, diacylglycerol kinase. Using (19)F NMR, O(2)-induced chemical shift perturbations revealed secondary structure, membrane immersion depth, and regions of the helix in contact with the protein or with the micelle.

PMID: 11853456 [PubMed - indexed for MEDLINE]

Source: PubMed

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