Figure 4. Structural characterization of DNA/Peptide co-assemblies.

(A) ¹³C{¹⁵N}REDOR measurements of ¹³C-¹⁵N distances for pep-KG ¹³C enriched at the leucine carbonyl ([1-¹³C]L) and ¹⁵N-enriched alanine ([¹⁵N]A) in both neat assemblies (black) and templated with DNA(A)₁₀ (blue). Both assemblies have β-sheets with leucine H-bonded to alanine from adjacent strands indicating antiparallel, in-register β-strands with 37±1.5% of the peptides adopting this orientation in pep-KG assemblies, whereas 92±1.5% of the peptides in pep-KG/DNA(A)₁₀ co-assemblies have this orientation. (B) ¹³C DQF-DRAWS measurement of ¹³C-¹³C distances in neat pep-KG assemblies assigned the ~60% of the [1-¹³C]Leu, not detected in the ¹³C{¹⁵N}REDOR experiment as parallel out-of-register by one amino acid β-sheets. (C) Models of peptide orientation and registry and their associated population from solid-state NMR measurements. Red triangles indicate position of [1-¹³C] and blue circles indicate ¹⁵N. (D) ¹³C{³¹P} REDOR of pep-KG/DNA(A)₁₀ show that all of the [1-¹³C]L nuclei are proximal to at least one ³¹P nucleus and fit to a single distance of 8.6Å with a Gaussian distribution of 2.2Å (inset). Unless shown, error bars are the size of the data points and represent standard deviation.