Figure 3.

Identification of intermolecular NOEs for R3‐GI. A) Amino acid sequence and labeling scheme for R3‐GI. Residues labeled in green are uniformly enriched with ¹³C and ¹⁵N. For the NMR experiment, labeled and non‐labeled peptide was mixed in a 1:1 ratio. B) ¹H,¹³C correlation spectrum of R3‐GI*. C) ¹H (ω₁),¹H (ω₃) correlation spectrum extracted from the 3D NOESY experiment. During ω₁, protons were selected that are directly bonded to ¹²C, whereas ¹³C‐bound protons were filtered during ω₃. In addition to trivial sequential connectivities (e.g., H11β–V10α) that appear only on one side of the diagonal, a number of symmetric cross‐peaks (in red) were observed that are due to intermolecular interactions.