Figure 1.

Characterisation of the structural and dynamic properties of CAHS‐8 in solution. A) The ¹⁵N‐¹H correlation spectrum is characteristic of an intrinsically disordered protein. B, C) Secondary ¹³Ca and ¹³C′ chemical shifts showing strong α‐helical propensities from 95–195, divided into two distinct helices, α₁ (E95‐F150) and α₂ (V167‐L194). ¹⁵N relaxation (D; 850 MHz, E; 600 MHz), ¹⁵N‐¹H RDCs (F), and PREs (see Figure S1) suggest the protein acts as a disordered chain comprising two highly populated α‐helices (303 K) and no persistent tertiary structure. The NMR spectrum was recorded at 350 μm (9.3 mg mL⁻¹). The NMR assignments are deposited in BMRB (accession code 51115).