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以蛋白质酪氨酸磷酸酶为模型，通过序列和结构的比较，对蛋白质序列、结构的保守性与其功能和进化的关系问题进行了研究。结果显示，虽然在酪氨酸磷酸酶超家族分子的序列中，仅有３个与其催化功能密切相关的残基是高度保守的，但它们功能结构域的核心拓扑结构却明显类似，其中存在着βαβ和βαβα２个保守的结构单元；此外，它们活性位点的拓扑结构也极其相似。因此，在保持蛋白质功能方面具有重要作用的残基是高度保守的，而具维持蛋白质结构作用的残基则是相对保守的。在进化过程中，蛋白质三维拓扑结构的保守性，似乎主要是体现在保持某些共同的特有二级结构单元和共同的折叠方式上。
Protein tyrosine phosphatase as a model, through the comparison of sequence and structure, protein sequence, the structure of the conservation and its function and evolution of the relationship between the issue. The results showed that although only three residues closely related to its catalytic function are highly conserved in the tyrosine phosphatase superfamily, the core topological structures of their functional domains are obviously similar, among which are βαβ and βαβα2 conserved structural units; in addition, their active site topology is also very similar. Thus, residues that play an important role in maintaining protein function are highly conserved, whereas residues with a role in maintaining protein structure are relatively conserved. During evolution, the conservation of the three-dimensional topology of proteins seems to be mainly manifested in maintaining certain common unique secondary structure units and common folding modes.