Expanding the genetic code for site-directed spin-labeling
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Date
2019
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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.
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Keywords
Noncanonical amino acids, Bioorthogonal chemistry, Spin labeling, Protein conformation, EPR spectroscopy, Macromolecular dynamics