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Amide rotation trajectories probed by symmetry
Citation key 168.2017.Kubyshkin
Author Kubyshkin, V. and Budisa, N.
Pages 6764 - 6772
Year 2017
DOI 10.1039/C7OB01421J
Journal Org. Biomol. Chem.
Volume 15
Abstract The amide rotation of peptidyl-prolyl fragments is an important factor in backbone structure organization of proteins. Computational studies have indicated that this rotation preferentially proceeds through a defined transition-state structure (syn/exo). Here, we complement the computational findings by determining the amide bond rotation barriers for the two symmetric proline analogues, meso and racemic pyrrolidine-2,5-dicarboxylic acid. The rotations around these residues represent syn/exo – syn/exo and anti/endo – syn/exo hybrid transition states for the meso and racemic diastereomer, respectively. The rotation barriers are lower for the former rotation by about 9 kJ mol−1 (aqueous medium), suggesting a strong preference for the syn/exo (clockwise) rotation over the anti/endo (anticlockwise). The results show that both hybrid rotation processes are enthalpically driven but respond differently to solvent polarity changes due to the different transition state dipole-dipole interactions.
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