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

Khatri, B and Majumder, P and Nagesh, J and Penmatsa, A and Chatterjee, J (2020) Increasing protein stability by engineering the n � �* interaction at the β-turn. In: Chemical Science, 11 (35). pp. 9480-9487.

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Abstract

Abundant n � �* 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 � �* interactionviaamino acid substitution and thioamide incorporation at a solvent exposed β-turn within theGB1proteins and Pin 1 WW domain, we demonstrate that an n � �* interaction increases the structural stability of proteins by restricting the�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 � �* interaction. © The Royal Society of Chemistry 2020.

Item Type:	Journal Article
Publication:	Chemical Science
Publisher:	Royal Society of Chemistry
Additional Information:	Copyright to this article belongs to Royal Society of Chemistry
Keywords:	Stability, Backbone carbonyl; Beta turns; Protein stability; Protein structures; Side-chains; Structural stabilities; Thioamides; Torsion angle, Proteins
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Solid State & Structural Chemistry Unit
Date Deposited:	26 Nov 2020 10:12
Last Modified:	26 Nov 2020 10:12
URI:	http://eprints.iisc.ac.in/id/eprint/66820

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