Bae S J, Chou W Y, Matthews K, Sturtevant J M
Department of Chemistry, Yale University, New Haven, CT 06511.
Proc Natl Acad Sci U S A. 1988 Sep;85(18):6731-2. doi: 10.1073/pnas.85.18.6731.
Differential scanning calorimetry demonstrates that the tryptophan repressor of Escherichia coli is unusually resistant to thermal denaturation. The dimeric protein undergoes reversible dissociative unfolding at pH 7.5 centered at about 90 degrees C. The thermal stability may be due in part to the unusual structure of the protein, which is composed of two identical intertwined polypeptide chains.
差示扫描量热法表明，大肠杆菌的色氨酸阻遏物对热变性具有异常的抗性。这种二聚体蛋白质在pH 7.5、约90℃时经历可逆的解离性解折叠。其热稳定性可能部分归因于该蛋白质的异常结构，它由两条相同的相互缠绕的多肽链组成。
