Authors: Braun, Theresa
Drescher, Malte
Summerer, Daniel
Title: Expanding the genetic code for site-directed spin-labeling
Language (ISO): en
Abstract: 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.
Subject Headings: Noncanonical amino acids
Bioorthogonal chemistry
Spin labeling
Protein conformation
EPR spectroscopy
Macromolecular dynamics
Issue Date: 2019
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Appears in Collections:Lehrstuhl für Chemische Biologie der Nukleinsäuren

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