Skip to main content
. Author manuscript; available in PMC: 2016 Oct 6.
Published in final edited form as: Biochemistry. 2015 Oct 6;54(39):6029–6037. doi: 10.1021/acs.biochem.5b00622

Figure 2.

Figure 2

Hydrogen bonding topology/patterns in the G→A peptide. (a) One residue staggering of the triple helix leads to leading (L), middle (M), and trailing (T) chains. (b) Distribution of N-O bond distances between N of the indicated residue and the carbonyl oxygen of the Pro in the neighboring chain. Chains L, M, and T are colored as black, red, and green, respectively.