Issue 35, 2020

Increasing protein stability by engineering the n → π* interaction at the β-turn

Abstract

Abundant n → π* 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 → π* interaction via amino acid substitution and thioamide incorporation at a solvent exposed β-turn within the GB1 proteins and Pin 1 WW domain, we demonstrate that an n → π* interaction increases the structural stability of proteins by restricting the ϕ 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 → π* interaction.

Graphical abstract: Increasing protein stability by engineering the n → π* interaction at the β-turn

Supplementary files

Article information

Article type
Edge Article
Submitted
01 jun 2020
Accepted
30 jul 2020
First published
30 jul 2020
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2020,11, 9480-9487

Increasing protein stability by engineering the n → π* interaction at the β-turn

B. Khatri, P. Majumder, J. Nagesh, A. Penmatsa and J. Chatterjee, Chem. Sci., 2020, 11, 9480 DOI: 10.1039/D0SC03060K

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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