Fedorov O V, Khechinashvili N N, Kamiya R, Asakura S
J Mol Biol. 1984 May 5;175(1):83-7. doi: 10.1016/0022-2836(84)90447-9.
Scanning microcalorimetric and circular dichroism studies of the normal and mutant flagellins of Salmonella suggest that they have a multidomain structure in common. Flagellin polymers (flagella) are depolymerized irreversibly into monomers as the temperature is raised, and the monomers undergo denaturation reversibly when cooled and heated again. The calorimetric enthalpy of this reversible process is twice as large as the van't Hoff enthalpy, suggesting that flagellin monomers contain two co-operative regions that melt independently at the same temperature. In all flagellin specimens examined, the ellipticity at the same temperature. In all flagellin specimens examined, the ellipticity at 222 nm of polymers at room temperature is 1.6 times as large as that of monomers, and the dependence of ellipticity on temperature takes place in the same temperature intervals in which calorimetric effects take place. From these results, we propose that flagellin molecules consist of several domains, two of which are distinctly structured in monomers at room temperature, while the others acquire more regular structures during polymerization.
对沙门氏菌正常和突变鞭毛蛋白的扫描量热法和圆二色性研究表明，它们具有共同的多结构域结构。随着温度升高，鞭毛蛋白聚合物（鞭毛）不可逆地解聚为单体，当冷却并再次加热时，单体可逆地发生变性。这个可逆过程的量热焓是范特霍夫焓的两倍，这表明鞭毛蛋白单体包含两个在相同温度下独立熔化的协同区域。在所有检测的鞭毛蛋白样本中，相同温度下的椭圆率。在所有检测的鞭毛蛋白样本中，室温下聚合物在222nm处的椭圆率是单体的1.6倍，并且椭圆率对温度的依赖性发生在与量热效应相同的温度区间内。根据这些结果，我们提出鞭毛蛋白分子由几个结构域组成，其中两个在室温下的单体中具有明显的结构，而其他结构域在聚合过程中获得更规则的结构。
