Publikation: A Genetically Encoded Spin Label for Electron Paramagnetic Resonance Distance Measurements
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We report the genetic encoding of a noncanonical, spin-labeled amino acid in Escherichia coli. This enables the intracellular biosynthesis of spin-labeled proteins and obviates the need for any chemical labeling step usually required for protein electron paramagnetic resonance (EPR) studies. The amino acid can be introduced at multiple, user-defined sites of a protein and is stable in E. coli even for prolonged expression times. It can report intramolecular distance distributions in proteins by double-electron electron resonance measurements. Moreover, the signal of spin-labeled protein can be selectively detected in cells. This provides elegant new perspectives for in-cell EPR studies of endogenous proteins.
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SCHMIDT, Moritz J., Julia BORBAS, Malte DRESCHER, Daniel SUMMERER, 2014. A Genetically Encoded Spin Label for Electron Paramagnetic Resonance Distance Measurements. In: Journal of the American Chemical Society. 2014, 136(4), pp. 1238-1241. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/ja411535qBibTex
@article{Schmidt2014-01-29Genet-27808,
year={2014},
doi={10.1021/ja411535q},
title={A Genetically Encoded Spin Label for Electron Paramagnetic Resonance Distance Measurements},
number={4},
volume={136},
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journal={Journal of the American Chemical Society},
pages={1238--1241},
author={Schmidt, Moritz J. and Borbas, Julia and Drescher, Malte and Summerer, Daniel}
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<dcterms:abstract xml:lang="eng">We report the genetic encoding of a noncanonical, spin-labeled amino acid in Escherichia coli. This enables the intracellular biosynthesis of spin-labeled proteins and obviates the need for any chemical labeling step usually required for protein electron paramagnetic resonance (EPR) studies. The amino acid can be introduced at multiple, user-defined sites of a protein and is stable in E. coli even for prolonged expression times. It can report intramolecular distance distributions in proteins by double-electron electron resonance measurements. Moreover, the signal of spin-labeled protein can be selectively detected in cells. This provides elegant new perspectives for in-cell EPR studies of endogenous proteins.</dcterms:abstract>
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