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

多元物質科学研究所・有機・生命科学研究部門

研究成果: Article › 査読

12 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	1111-1112
ページ数	2
ジャーナル	Chemical Communications
号	12
DOI	https://doi.org/10.1039/a903320c
出版ステータス	Published - 1999 6 21

ASJC Scopus subject areas

触媒
電子材料、光学材料、および磁性材料
セラミックおよび複合材料
化学 (全般)
表面、皮膜および薄膜
金属および合金
材料化学

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10.1039/a903320c

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

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