A Miniature Protein Stabilized by a Cation-π Interaction Network

Journal of the American Chemical Society
Timothy W CravenKent Kirshenbaum

Abstract

The design of folded miniature proteins is predicated on establishing noncovalent interactions that direct the self-assembly of discrete thermostable tertiary structures. In this work, we describe how a network of cation-π interactions present in proteins containing "WSXWS motifs" can be emulated to stabilize the core of a miniature protein. This 19-residue protein sequence recapitulates a set of interdigitated arginine and tryptophan residues that stabilize a distinctive β-strand:loop:PPII-helix topology. Validation of the compact fold determined by NMR was carried out by mutagenesis of the cation-π network and by comparison to the corresponding disulfide-bridged structure. These results support the involvement of a coordinated set of cation-π interactions that stabilize the tertiary structure.

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Citations

Apr 11, 2017·Physical Chemistry Chemical Physics : PCCP·Jorge A Carrazana-GarcíaJesús Rodríguez-Otero
May 23, 2017·Nature Chemical Biology·Emily G BakerDerek N Woolfson
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Feb 6, 2021·Nature Chemical Biology·Alan JohnEthan D Goddard-Borger
Mar 9, 2021·Biochemical and Biophysical Research Communications·Tanuja JoshiSabyasachi Rakshit
Feb 20, 2021·Annual Review of Biophysics·Tamar SchlickEva Xue
Jul 9, 2021·Bioorganic & Medicinal Chemistry·Maria Ngu-SchwemleinDaniel Todd
Aug 6, 2021·Bioinorganic Chemistry and Applications·Elliot SpringfieldMaria Ngu-Schwemlein
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