Yamauchi A, Yomo T, Tanaka F, Prijambada I D, Ohhashi S, Yamamoto K, Shima Y, Ogasahara K, Yutani K, Kataoka M, Urabe I
Department of Biotechnology, Faculty of Engineering, Osaka University, Suita, Japan.
FEBS Lett. 1998 Jan 9;421(2):147-51. doi: 10.1016/s0014-5793(97)01552-4.
The structural and catalytic properties of two soluble random proteins, RP3-42 and RP3-45, of 141 amino acid residues were investigated. Although no marked secondary structure was detected by CD spectrum, sedimentation equilibrium and small-angle X-ray scattering studies showed that they form an oligomeric structure and are as compact as the molten globule. The random proteins have low but distinct esterase activity; the values of the second-order rate constant for the hydrolysis of p-nitrophenol were 0.78 and 1.39 M(-1) s(-1) for RP3-42 and RP3-45, respectively. The differences in the properties of the random and the native proteins are discussed from the evolutionary point of view.
对两个由141个氨基酸残基组成的可溶性无规蛋白RP3 - 42和RP3 - 45的结构和催化特性进行了研究。虽然圆二色光谱未检测到明显的二级结构，但沉降平衡和小角X射线散射研究表明它们形成了寡聚结构，并且与熔球态一样致密。这些无规蛋白具有较低但明显的酯酶活性；对于RP3 - 42和RP3 - 45，对硝基苯酚水解的二级速率常数分别为0.78和1.39 M⁻¹ s⁻¹。从进化的角度讨论了无规蛋白和天然蛋白性质上的差异。
