中文摘要：

天青蛋白（Azurin简写为Az）是由128个氨基酸残基组成的Ⅰ型铜蓝蛋白,唯一的色氨酸残基（Trp^48）位于由8股β折叠片形成的疏水桶中。文章使用光谱学手段研究了表面活性剂SDS和CTAB诱导的apo-Az以及Cu^Ⅱ-Az的解折叠。结果表明,apo-Az的解折叠过程呈现为典型的两态,平均结构基元解折叠自由能〈ΔG0^element〉约为18.00kJ/mol。铜（Ⅱ）与apo-Az的结合使蛋白质稳定性增加,且SDS诱导的解折叠表现为三态,CTAB仅能使Cu^Ⅱ-Az部分解折叠。

英文摘要：

Azurin （Az） is a small （128 residues） type I blue-copper protein, eight β-strands that fold into a hydrophobic β-barrel and a single tryptophan （Trp^48） buried in it. SDS and CTAB induced unfolding process of apo-Az and Cu -Az was investigated by spectroscopy methods. The results show that the unfolding curve of apo-Az is a typical two-state transition without detectable intermediate state. The average structural element free energy change, 〈ΔG0^element〉, is about 18.00 kJ/mol. The binding of Cu^Ⅱ can increase the stability of protein and the unfolding curve of Cuu -Az induced by SDS shows a three-state transition, but CTAB induced unfolding show a two state transition because only the first structural element was destroyed.