Description: Selective Protein Hyperpolarization in Cell Lysates Using Targeted Dynamic Nuclear Polarization

This title appears in the Scientific Report : 2016

Selective Protein Hyperpolarization in Cell Lysates Using Targeted Dynamic Nuclear Polarization

Nuclear magnetic resonance (NMR) spectroscopy has the intrinsic capabilities to investigate proteins in native environments. In general, however, NMR relies on non-natural protein purity and concentration to increase the desired signal over the background. We here report on the efficient and specifi...

Personal Name(s):	Viennet, Thibault
	Viegas, Aldino / Kuepper, Arne / Arens, Sabine / Gelev, Vladimir / Petrov, Ognyan / Grossmann, Tom N. / Heise, Henrike / Etzkorn, Manuel (Corresponding author)
Contributing Institute:	Strukturbiochemie; ICS-6
Published in:	Angewandte Chemie / International edition, 55 (2016) 36, S. 10746 - 10750
Imprint:	Weinheim Wiley-VCH 2016
DOI:	10.1002/anie.201603205
PubMed ID:	27351143
Document Type:	Journal Article
Research Program:	Functional Macromolecules and Complexes
	Publikationsportal JuSER

Please use the identifier: http://dx.doi.org/10.1002/anie.201603205 in citations.

Nuclear magnetic resonance (NMR) spectroscopy has the intrinsic capabilities to investigate proteins in native environments. In general, however, NMR relies on non-natural protein purity and concentration to increase the desired signal over the background. We here report on the efficient and specific hyperpolarization of low amounts of a target protein in a large isotope-labeled background by combining dynamic nuclear polarization (DNP) and the selectivity of protein interactions. Using a biradical-labeled ligand, we were able to direct the hyperpolarization to the protein of interest, maintaining comparable signal enhancement with about 400-fold less radicals than conventionally used. We could selectively filter out our target protein directly from crude cell lysate obtained from only 8 mL of fully isotope-enriched cell culture. Our approach offers effective means to study proteins with atomic resolution in increasingly native concentrations and environments.