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 | |
| 出版ステータス | Published - 1999 6 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