Charged single α-helix

A versatile protein structural motif

Dániel Süveges, Z. Gáspári, Gábor Tóth, L. Nyitray

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

A few highly charged natural peptide sequences were recently suggested to form stable α-helical structures in water. In this article we show that these sequences represent a novel structural motif called "charged single α-helix" (CSAH). To obtain reliable candidate CSAH motifs, we developed two conceptually different computational methods capable of scanning large databases: SCAN4CSAH is based on sequence features characteristic for salt bridge stabilized single α-helices, whereas FT-CHARGE applies Fourier transformation to charges along sequences. Using the consensus of the two approaches, a remarkable number of proteins were found to contain putative CSAH domains. Recombinant fragments (50-60 residues) corresponding to selected hits obtained by both methods (myosin 6, Golgi resident protein GCP60, and M4K4 protein kinase) were produced and shown by circular dichroism spectroscopy to adopt largely α-helical structure in water. CSAH segments differ substantially both from coiled-coil and intrinsically disordered proteins, despite the fact that current prediction methods recognize them as either or both. Analysis of the proteins containing CSAH motif revealed possible functional roles of the corresponding segments. The suggested main functional features include the formation of relatively rigid spacer/connector segments between functional domains as in caldesmon, extension of the lever arm in myosin motors and mediation of transient interactions by promoting dimerization in a range of proteins.

Original languageEnglish
Pages (from-to)905-916
Number of pages12
JournalProteins: Structure, Function and Genetics
Volume74
Issue number4
DOIs
Publication statusPublished - Mar 2009

Fingerprint

Amino Acid Motifs
Myosins
Proteins
Intrinsically Disordered Proteins
Circular dichroism spectroscopy
Calmodulin-Binding Proteins
Dimerization
Water
Circular Dichroism
Computational methods
Protein Kinases
Spectrum Analysis
Salts
Databases
Scanning
Peptides

Keywords

  • Circular dichroism spectroscopy
  • Coiled coil
  • Fourier transformation
  • Intrinsically disordered proteins
  • Myosin
  • Protein kinase
  • Salt bridges
  • Structure prediction

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Charged single α-helix : A versatile protein structural motif. / Süveges, Dániel; Gáspári, Z.; Tóth, Gábor; Nyitray, L.

In: Proteins: Structure, Function and Genetics, Vol. 74, No. 4, 03.2009, p. 905-916.

Research output: Contribution to journalArticle

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