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.
 
                



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