FIGURE 1.

¹⁵N-HSQC NMR spectrum and secondary structure analysis of ^1–84HOP2. A, peaks corresponding to chemical shifts were assigned with a set of three-dimensional NMR experiments. A typical ¹⁵N-HSQC spectrum is shown. B, secondary structures and order parameters predicted using assigned chemical shifts. Negative probabilities indicate propensity for α-helical structures, and positive probabilities indicate β-strands (top panel). Shown is a chemical shift estimation of protein backbone mobility for ^1–84HOP2 (lower panel). RCI, random coil index.