Extended Data Fig. 4: Generality of hydrogen-bonding patterns across dominant rotor-containing macrocycles.
From: Illuminating the dark conformational space of macrocycles using dominant rotors
a, Structural scope of dominant rotor peptides with Ra-(red) and Sa-(grey) average backbone solution structures superimposed on the three consecutive natural amino acid residues. Root mean-squared deviation (RMSD) shown for macrocycle backbone atoms. The type II αRU-turn was detected in every Ra-well except for 12h, which exhibited a left-handed helical turn. Apart from 12g, the Sa-wells are variable and access a variety of different turn types and conformations containing non-hydrogen bonded amides. Dominant rotor omitted for clarity. Gibbs free energy differences in kcal mol−1 are shown in brackets.
