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The C-terminal flanking peptide may have an important function since it was well conserved and contained a region of 16 amino acids with only a single, conservative replacement.
This C-terminal peptide contains three pairs of basic amino acids, suggesting that it may be the precursor of multiple processed peptides.
Elucidation of the amino acid composition provided supporting evidence that the peptide was novel and was consistent with a full length peptide of approximately 30 amino acids.
We also show that the peptide staple can be shortened to 24 amino acids still permitting an irreversible combination of functional proteins.
Among the species studied, the five amino acids at the C-terminus of the peptide are totally conserved, suggesting that this region is of major importance.
The first 29 amino acids are hydrophobic and may represent the transit peptide.
Peptides with two N-terminal basic amino acids are more stable than other peptides.
We show that the three amino acids on the C terminus of the peptide analogs bind too weakly to exert a functional effect themselves.
The experiments of single β-amino acid incorporation into a peptide revealed that 13 β-amino acids are compatible with ribosomal translation.
Open accessJournal ArticleDOI
Jan Markussen, Finn Sundby 
01 May 1973-FEBS Journal
13 Citations
It is the first C-peptide shown to contain the amino acids histidine, tyrosine and phenylalanine.

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