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

Seiji Sakamoto; Ikuo Obataya; Akihiko Ueno; Hisakazu Mihara

doi:10.1039/a903320c

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

Seiji Sakamoto, Ikuo Obataya, Akihiko Ueno, Hisakazu Mihara

Division of Organic- and Biomaterials Research

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	1111-1112
Number of pages	2
Journal	Chemical Communications
Issue number	12
DOIs	https://doi.org/10.1039/a903320c
Publication status	Published - 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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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.",

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