Structure and Properties of Keratin Protein Model Gel

It has already been mentioned that the properties of hair depend on the higher-order structure of the amorphous r ion of protein. Also, it was 

O Hair in which SSj is reduced with TGA, then further oxidized. 

Polymorphed to irreversible protein (Destruction of domain structure) 

Wool is reduced by 0.3 M TGA aqueous solution (pH 11) that contains 8.0 M urea, neutralized to pH 7 by acetic acid, and oxidized by 1.5 M NaBr03 aqueous solution in the presence of a sufficient amount of unreacted TGA. After filtration of the insoluble component, a water soluble protein is obtained [65]. This protein is (1) fix m amino acid analysis, the SH group that is chemically treated with S-carbox5rmethyl-alanyl disulfide (CMAD —SSCH2COOH) (2) from SDS-polyacrylamide electrophoresis, the mixture of type-1 and type-11 LS keratin proteins and (3) from the CD spectrum, a polymer with a-helix (Fig. 16). This is called carboxymethylalanyl disulfide keratin (CMADK). 

When 4% CMADK aqueous solution was heated at 100°C, opaque aggregates were formed as shown in Fig. 17. These aggregates quickly dissolved into a transparent solution in a dilute TGA aqueous solution. Therefore, in these aggregates, a part of CMAD is thought to return to the 

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