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. Author manuscript; available in PMC: 2021 Oct 16.
Published in final edited form as: ACS Chem Biol. 2020 Sep 18;15(10):2752–2765. doi: 10.1021/acschembio.0c00543

Figure 5: 15N/1H-HSQC NMR reveals that the Jα helix is partially unfolded in N414A-AsLOV2.

Figure 5:

(A) Tryptophan indole side-chain chemical shifts of the wild-type protein show a clear shift and broadening from dark to light states (black to gray). (B) The same resonances in N414A AsLOV2 show that W557, which is located on the Jα helix, is partially in the lit state suggesting that the helix is partially unfolded (Dark red to light red). (C) N414Q AsLOV2 does not show partial unfolding, however the peak assigned to W557 is distorted compared to wild-type AsLOV2 (Dark blue to light blue).