Structural analysis of large protein complexes using solvent paramagnetic relaxation enhancements

Tobias Madl; Thomas Güttler; Dirk Görlich; Michael Sattler

doi:10.1002/anie.201007168

Structural analysis of large protein complexes using solvent paramagnetic relaxation enhancements

Tobias Madl, Thomas Güttler, Dirk Görlich, Michael Sattler

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Abstract

The solvent helps out: Conventional protocols for structural analysis of protein complexes often fail if only sparse experimental data are available. NMR-spectroscopy-derived solvent paramagnetic relaxation enhancements (PREs) from a soluble spin label (picture) significantly improve the structural quality of a 150 kDa protein complex. This general protocol is an efficient approach for structural analysis of large protein complexes in solution.

Original language	English
Pages (from-to)	3993-3997
Number of pages	5
Journal	Angewandte Chemie International Edition in English
Volume	50
Issue number	17
DOIs	https://doi.org/10.1002/anie.201007168
State	Published - 18 Apr 2011

Keywords

NMR spectroscopy
paramagnetic relaxation enhancement
proteins
structural biology

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10.1002/anie.201007168

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abstract = "The solvent helps out: Conventional protocols for structural analysis of protein complexes often fail if only sparse experimental data are available. NMR-spectroscopy-derived solvent paramagnetic relaxation enhancements (PREs) from a soluble spin label (picture) significantly improve the structural quality of a 150 kDa protein complex. This general protocol is an efficient approach for structural analysis of large protein complexes in solution.",

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AU - Güttler, Thomas

AU - Görlich, Dirk

AU - Sattler, Michael

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KW - NMR spectroscopy

KW - paramagnetic relaxation enhancement

KW - proteins

KW - structural biology

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Structural analysis of large protein complexes using solvent paramagnetic relaxation enhancements

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Keywords

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