Raman spectroscopic study of Streptomyces subtilisin inhibitor

Abstract

AbstractRaman spectra of Streptomyces subtilisin inhibitor (SSI) in H2O and D2O solutions were observed for the first time. Information obtained regarding the conformations of polypeptide backbone, disulphide bridge and methionyl side chain was largely consistent with the results derived from other methods. As for the microenvironments of the three tyrosyl residues, the Raman spectrum suggested that none of these residues were involved in a specific interresidue interaction as proposed by nuclear magnetic resonance study for Tyr‐93. The Raman spectrum was shown to be useful for studying the binding of the sulphate ion to SSI.