AI Article Synopsis
- Time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) is introduced as a method for measuring inter-residue distances in proteins during their mechanical cycles at 240 GHz.
- The technique utilizes Gd-sTPATCN spin labels, offering advantages like a spin-7/2 EPR-active center and low anisotropy, making it more effective than conventional nitroxide labels.
- TiGGER findings revealed that in the protein AsLOV2, light activation causes rapid separation of its termini in under a second, with a recovery to equilibrium occurring over about 60 seconds, and changes in motion were observed in a variant of the protein, linking it to chromophore behavior.
Article Abstract
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein's mechanical cycle in the solution state. TiGGER makes use of Gd-sTPATCN spin labels, whose favorable qualities include a spin-7/2 EPR-active center, short linker, narrow intrinsic linewidth, and virtually no anisotropy at high fields (8.6 T) when compared to nitroxide spin labels. Using TiGGER, we determined that upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature. TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
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| http://dx.doi.org/10.1002/anie.202212832 | DOI Listing |
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