Relation between structure and function in some partially synthetic ribonucleases S'. Enzymic and spectroscopic investigation on [Orn10, Asn14]-RNase S' and 1epsilon, 7epsilon, 10delta-triguanidino-[Orn10, Asn14]-RNase S'.
Some analogues have been prepared of S-peptide, the peptide obtained together with S-protein from subtilisn-modified beef pancreatic R Nase A. The syntheses are described of [Orn10, Asn14]-S-peptide and 1epsilon, 7epsilon, 10delta-triguanidino-[Orn10, Asn14]-S-peptide. The S-peptide analogues are able to activate S-protein at the level of the parent [Orn10]-S-peptide and 1epsilon, 7epsilon-diguanidino-S-peptide respectively, although at high peptide-to-protein molar ratios. After their recombination with S-protein the buried character of Tyr-25 was restored, as judged from difference absorption and circular dichroism spectra in the near-ultraviolet region. These findings indicate that the asparaginyl residue is a possible naturally occurring substituent in the R Nase A sequences whose state of amidation in position 14 has not yet been defined.