Issue 12, 1999

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

Abstract

A designed peptide H2α17-I bound FeIII–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.

Article information

Article type
Paper

Chem. Commun., 1999, 1111-1112

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

S. Sakamoto, I. Obataya, A. Ueno and H. Mihara, Chem. Commun., 1999, 1111 DOI: 10.1039/A903320C

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