Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy

Nathaniel J. Traaseth; Raffaello Verardi; Gianluigi Veglia

doi:10.1021/ja711499r

Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy

Nathaniel J. Traaseth, Raffaello Verardi, Gianluigi Veglia

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

We present an asymmetric isotopic labeling strategy for probing unambiguously membrane protein binding interfaces in homo-oligomers. This technique is highly sensitive, rapid, and requires only one ¹³C methyl-edited nuclear Overhauser effect spectroscopy (NOESY) spectrum. As a proof of principle, we apply this technique to the homo-pentameric membrane protein phospholamban, defining the leucine-isoleucine zipper interface between its monomers with atomistic resolution.

Original language	English (US)
Pages (from-to)	2400-2401
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	130
Issue number	8
DOIs	https://doi.org/10.1021/ja711499r
State	Published - Feb 27 2008

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja711499r

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abstract = "We present an asymmetric isotopic labeling strategy for probing unambiguously membrane protein binding interfaces in homo-oligomers. This technique is highly sensitive, rapid, and requires only one 13C methyl-edited nuclear Overhauser effect spectroscopy (NOESY) spectrum. As a proof of principle, we apply this technique to the homo-pentameric membrane protein phospholamban, defining the leucine-isoleucine zipper interface between its monomers with atomistic resolution.",

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AU - Verardi, Raffaello

AU - Veglia, Gianluigi

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N2 - We present an asymmetric isotopic labeling strategy for probing unambiguously membrane protein binding interfaces in homo-oligomers. This technique is highly sensitive, rapid, and requires only one 13C methyl-edited nuclear Overhauser effect spectroscopy (NOESY) spectrum. As a proof of principle, we apply this technique to the homo-pentameric membrane protein phospholamban, defining the leucine-isoleucine zipper interface between its monomers with atomistic resolution.

AB - We present an asymmetric isotopic labeling strategy for probing unambiguously membrane protein binding interfaces in homo-oligomers. This technique is highly sensitive, rapid, and requires only one 13C methyl-edited nuclear Overhauser effect spectroscopy (NOESY) spectrum. As a proof of principle, we apply this technique to the homo-pentameric membrane protein phospholamban, defining the leucine-isoleucine zipper interface between its monomers with atomistic resolution.

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Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy

Abstract

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