A new protein spin labelling technique

phys.org | 3/19/2019 | Staff
sheenabeanna (Posted by) Level 3
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Site-directed spin labelling (SDSL) used in combination with electron paramagnetic resonance (EPR) spectroscopy has been a tried and trusted technique for elucidating the structure, function and dynamics of proteins and protein complexes. Nitroxide-based spin labels are among the most popular and best established ones because they are small, non-disturbing and exhibit excellent spectroscopic properties. "Ideal spin labelling procedures exhibit high reaction rates and selectivity," explains Professor Malte Drescher, Professor for Spectroscopy of Complex Systems at the University of Konstanz's Department of Chemistry and main author on the study alongside Professor Valentin Wittmann, who specializes in organic synthesis.

"Achieving high reactivity and high selectivity both at the same time can be a problem," continues Drescher. "Conventional spin labels based, for instance, on Gadolinium(III) or trityl, display either very broad spectra and low modulation depths or very narrow spectra that are unsuitable for the kinds of experiments that we want to conduct." A new study published by Drescher, Wittmann and their team of University of Konstanz chemists, which was published online in the journal ChemBioChem Communications on 14 August 2019, introduces a new approach for labelling proteins that features nitroxide-based spin labels and genetically encoded noncanonical amino acids (ncAAs) as targets for SDSL.

Nitroxides - Width - Access - Information - Anandi

"Nitroxides provide ideal spectral width and access to dynamic information," says Anandi Kugele, a doctoral researcher at the Konstanz Research School of Chemical Biology (KoRS-CB) and first author on the study, who received a prestigious travel grant from the National High Magnetic Field Laboratory to present the results at the 2019 Rocky Mountain Conference on Magnetic...
(Excerpt) Read more at: phys.org
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