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A Miniature Protein Stabilized by a Cation−π Interaction Network

Craven, Timothy W., Cho, Min-Kyu, Traaseth, Nathaniel J., Bonneau, Richard and Kirshenbaum, Kent (2016) A Miniature Protein Stabilized by a Cation−π Interaction Network. Journal of the American Chemical Society, 138 (5). pp. 1543-1550. ISSN 0002-7863


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.

Item Type: Article
Date Deposited: 21 Mar 2019 00:45
Last Modified: 21 Mar 2019 00:45


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