In-Cell Protein Structures from 2D NMR Experiments

Müntener, Thomas and Häussinger, Daniel and Selenko, Philipp and Theillet, Francois-Xavier. (2016) In-Cell Protein Structures from 2D NMR Experiments. Journal of Physical Chemistry Letters, 7 (14). pp. 2821-2825.

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Official URL: http://edoc.unibas.ch/51859/

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In-cell NMR spectroscopy provides atomic resolution insights into the structural properties of proteins in cells, but it is rarely used to solve entire protein structures de novo. Here, we introduce a paramagnetic lanthanide-tag to simultaneously measure protein pseudocontact shifts (PCSs) and residual dipolar couplings (RDCs) to be used as input for structure calculation routines within the Rosetta program. We employ this approach to determine the structure of the protein G B1 domain (GB1) in intact Xenopus laevis oocytes from a single set of 2D in-cell NMR experiments. Specifically, we derive well-defined GB1 ensembles from low concentration in-cell NMR samples (∼50 μM) measured at moderate magnetic field strengths (600 MHz), thus offering an easily accessible alternative for determining intracellular protein structures.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Nuclear Magnetic Resonance (Häussinger)
UniBasel Contributors:Müntener, Thomas and Häussinger, Daniel
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
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edoc DOI:
Last Modified:07 Jul 2020 07:46
Deposited On:11 Jan 2017 12:48

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