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 journalArticle

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.

Original languageEnglish (US)
Pages (from-to)1543-1550
Number of pages8
JournalJournal of the American Chemical Society
Volume138
Issue number5
DOIs
StatePublished - Feb 17 2016

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Cations
Positive ions
Proteins
Mutagenesis
Arginine
Tryptophan
Disulfides
Self assembly
Nuclear magnetic resonance
Topology

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

A Miniature Protein Stabilized by a Cation-π Interaction Network. / Craven, Timothy W.; Cho, Min Kyu; Traaseth, Nathaniel J.; Bonneau, Richard; Kirshenbaum, Kent.

In: Journal of the American Chemical Society, Vol. 138, No. 5, 17.02.2016, p. 1543-1550.

Research output: Contribution to journalArticle

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