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Expanding the Genetic Code for Site-Directed Spin-Labeling

Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy enables studies of the structure, dynamics, and interactions of proteins in the noncrystalline state. The scope and analytical value of SDSL–EPR experiments crucially depends on the employed lab...

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Detalles Bibliográficos
Autores principales: Braun, Theresa, Drescher, Malte, Summerer, Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6359334/
https://www.ncbi.nlm.nih.gov/pubmed/30654584
http://dx.doi.org/10.3390/ijms20020373
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author Braun, Theresa
Drescher, Malte
Summerer, Daniel
author_facet Braun, Theresa
Drescher, Malte
Summerer, Daniel
author_sort Braun, Theresa
collection PubMed
description Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy enables studies of the structure, dynamics, and interactions of proteins in the noncrystalline state. The scope and analytical value of SDSL–EPR experiments crucially depends on the employed labeling strategy, with key aspects being labeling chemoselectivity and biocompatibility, as well as stability and spectroscopic properties of the resulting label. The use of genetically encoded noncanonical amino acids (ncAA) is an emerging strategy for SDSL that holds great promise for providing excellent chemoselectivity and potential for experiments in complex biological environments such as living cells. We here give a focused overview of recent advancements in this field and discuss their potentials and challenges for advancing SDSL–EPR studies.
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spelling pubmed-63593342019-02-06 Expanding the Genetic Code for Site-Directed Spin-Labeling Braun, Theresa Drescher, Malte Summerer, Daniel Int J Mol Sci Review Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy enables studies of the structure, dynamics, and interactions of proteins in the noncrystalline state. The scope and analytical value of SDSL–EPR experiments crucially depends on the employed labeling strategy, with key aspects being labeling chemoselectivity and biocompatibility, as well as stability and spectroscopic properties of the resulting label. The use of genetically encoded noncanonical amino acids (ncAA) is an emerging strategy for SDSL that holds great promise for providing excellent chemoselectivity and potential for experiments in complex biological environments such as living cells. We here give a focused overview of recent advancements in this field and discuss their potentials and challenges for advancing SDSL–EPR studies. MDPI 2019-01-16 /pmc/articles/PMC6359334/ /pubmed/30654584 http://dx.doi.org/10.3390/ijms20020373 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Braun, Theresa
Drescher, Malte
Summerer, Daniel
Expanding the Genetic Code for Site-Directed Spin-Labeling
title Expanding the Genetic Code for Site-Directed Spin-Labeling
title_full Expanding the Genetic Code for Site-Directed Spin-Labeling
title_fullStr Expanding the Genetic Code for Site-Directed Spin-Labeling
title_full_unstemmed Expanding the Genetic Code for Site-Directed Spin-Labeling
title_short Expanding the Genetic Code for Site-Directed Spin-Labeling
title_sort expanding the genetic code for site-directed spin-labeling
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6359334/
https://www.ncbi.nlm.nih.gov/pubmed/30654584
http://dx.doi.org/10.3390/ijms20020373
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