Regulation of α/β-folding of a designed peptide by haem binding

Seiji Sakamoto, Ikuo Obataya, Akihiko Ueno, Hisakazu Mihara

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

A designed peptide H2α17-I bound Fe(III)-mesoporphyrin (haem); and the haem-binding prevented the peptide forming β-sheet aggregates by facilitating the formation of an α-helix tetramer, indicating that the folding state of artificially designed peptides could be regulated by cofactor binding.

Original languageEnglish
Pages (from-to)1111-1112
Number of pages2
JournalChemical Communications
Issue number12
DOIs
Publication statusPublished - 1999 Jun 21

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

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