Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/ijms20020373
Keywords
noncanonical amino acids; bioorthogonal chemistry; spin labeling; protein conformation; EPR spectroscopy; macromolecular dynamics
Funding
- European Research Council (SPICE Project)
- Deutsche Forschungsgemeinschaft [SFB 969]
- Konstanz Research School Chemical Biology (KoRS-CB)
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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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