Trifluoroethanol reveals helical propensity at analogous positions in cytoplasmic domains of three connexins

Alfredo G. Fort, David C. Spray

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Cytoplasmic domains of gap junction proteins (connexins) are involved in channel gating, voltage and pH sensitivity, and contain binding sites for partner proteins. However, their secondary structure is incompletely characterized and comparisons among the connexins is totally lacking. Circular dichroism (CD) was used to study the conformational properties of synthetic peptides corresponding to the highly divergent amino acid sequences of cytoplasmic domains of connexin (Cx)32, Cx36, and Cx43. We report that whereas peptides were largely unstructured in aqueous buffer, certain peptides in 30% trifluoroethanol (TFE) showed considerable helical content. These structured peptides correspond to analogous regions in each of the three connexin cytoplasmic domains. This first comparative study of conformational properties of connexin cytoplasmic domains reveals protein domains that may play similar roles in channel function and protein-protein interactions.

Original languageEnglish (US)
Pages (from-to)173-182
Number of pages10
JournalBiopolymers
Volume92
Issue number3
DOIs
StatePublished - 2009

Fingerprint

Trifluoroethanol
Connexins
Peptides
Proteins
Connexin 43
Dichroism
Binding sites
Circular Dichroism
Amino acids
Amino Acid Sequence
Buffers
Binding Sites
Amino Acids
Electric potential

Keywords

  • Circular dichroism
  • Gap junctions
  • Peptides
  • Secondary structure
  • Spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Biomaterials
  • Organic Chemistry

Cite this

Trifluoroethanol reveals helical propensity at analogous positions in cytoplasmic domains of three connexins. / Fort, Alfredo G.; Spray, David C.

In: Biopolymers, Vol. 92, No. 3, 2009, p. 173-182.

Research output: Contribution to journalArticle

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