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鲱精蛋白和鲱精酮蛋白的拉曼光谱研究表明它们的结构有明显的不同之处：（１）鲱精蛋白的二级结构以α－螺旋为主，鲱精酮蛋白以α－螺旋和β－折叠为主。（２）两者有不同之处除构象灵敏的酰胺Ⅲ，Ｃ－Ｃ，Ｃ－Ｎ基团以外还有构象不灵敏的与Ｏ＝Ｃ－Ｎ，Ｎ－Ｈ和Ｃ＝Ｏ有关的酰胺Ⅳ，Ⅴ，Ⅵ。（３）属于甲基、亚甲基的一系列谱线的变化明显。上述３点均说明了鲱精蛋白转氨后发生了构型的变化。与“蛋白质Ｎ端除去氨基以后生成ＲＣＯＣＯＮＨ酮肽相联基团”的研究结果一致
Raman spectroscopy of herring protamine and herring keratin showed that there were significant differences in their structures: (1) the secondary structure of herring protamine was dominated by alpha-helix, and the herring essence protein was expressed as alpha-helix and β-fold based. (2) The difference between the two is that in addition to the conformationally sensitive amides III, C-C and C-N groups, there are conformationally insensitive amides IV associated with O = C-N, N-H and C = O , Ⅴ, Ⅵ. (3) A series of spectra belonging to methyl and methylene changed obviously. The above 3 points illustrate the change in configuration of herring protamine transamination. The results of the study with “RCOCONH ketopeptide associated groups after removal of amino group at the N-terminus of the protein”