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 |
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Pages (from-to) | 1111-1112 |
Number of pages | 2 |
Journal | Chemical Communications |
Issue number | 12 |
DOIs | |
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