A Miniature Protein Stabilized by a Cation-π Interaction Network

Timothy W. Craven, Min Kyu Cho, Nathaniel J. Traaseth, Richard Bonneau, Kent Kirshenbaum

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)1543-1550
Number of pages8
JournalJournal of the American Chemical Society
Issue number5
StatePublished - Feb 17 2016

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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