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Publication Abstract from PubMed

Abundant n --> pi* interactions between adjacent backbone carbonyl groups, identified by statistical analysis of protein structures, are predicted to play an important role in dictating the structure of proteins. However, experimentally testing the prediction in proteins has been challenging due to the weak nature of this interaction. By amplifying the strength of the n --> pi* interaction via amino acid substitution and thioamide incorporation at a solvent exposed beta-turn within the GB1 proteins and Pin 1 WW domain, we demonstrate that an n --> pi* interaction increases the structural stability of proteins by restricting the varphi torsion angle. Our results also suggest that amino acid side-chain identity and its rotameric conformation play an important and decisive role in dictating the strength of an n --> pi* interaction.

Increasing protein stability by engineering the n --> pi* interaction at the beta-turn.,Khatri B, Majumder P, Nagesh J, Penmatsa A, Chatterjee J Chem Sci. 2020 Jul 30;11(35):9480-9487. doi: 10.1039/d0sc03060k. PMID:34094214^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.