
%0 Journal Article
%A Perich, JW 
%A Johns, RB 
%A Thompson, AR 
%A Botto, RB 
%T Solid-State <sup>31</sup>P Nuclear Magnetic Resonance Spectroscopic Study of Phosphorylated Peptide-Resins and Phosphorylated Wool Keratin
%J Australian Journal of Chemistry
%D 1995/12/01
%V 48
%N 12
%P 1925-1932
%K 
%R https://doi.org/10.1071/CH9951925
%U https://www.publish.csiro.au/paper/CH9951925 
%X Solid-state 31P n.m.r. spectroscopy was found to be a useful method for the analysis of phosphorylated peptide-polystyrene resins and permitted the monitoring of chemical modifications of the phosphate moiety whilst the phosphorylated peptide was bound to the polystyrene support. Solid-state 31P n.m.r. spectroscopy was also applied to the analysis of phosphorylated wool keratin samples and showed that (A) different phosphate functionalities could be identified from the use of particular phosphorylation treatments, and (B) the majority of the phosphorylative modifications was located on the surface of wool keratin. This technique was found to be useful for monitoring the effectiveness of secondary chemical modification treatments on phosphorus trichloride-treated wool fabric samples. 
