Mosavi Leila K, Williams Suzanna, Peng Zy Zheng-yu
Department of Biochemistry, University of Connecticut Health Center, MC-3305, 263 Farmington Avenue, Farmington, CT 06030, USA.
J Mol Biol. 2002 Jul 5;320(2):165-70. doi: 10.1016/S0022-2836(02)00441-2.
Proteins containing stretches of repeating amino acid sequences are prevalent throughout nature, yet little is known about the general folding and assembly mechanisms of these systems. Here we propose myotrophin as a model system to study the folding of ankyrin repeat proteins. Myotrophin is folded over a large pH range and is soluble at high concentrations. Thermal and urea denaturation studies show that the protein displays cooperative two-state folding properties despite its modular nature. Taken together with previous studies on other ankyrin repeat proteins, our data suggest that the two-state folding pathway may be characteristic of ankyrin repeat proteins and other integrated alpha-helical repeat proteins in general.
含有重复氨基酸序列片段的蛋白质在自然界中普遍存在，但对于这些系统的一般折叠和组装机制却知之甚少。在此，我们提出肌养蛋白作为研究锚蛋白重复序列蛋白折叠的模型系统。肌养蛋白在较大的pH范围内折叠，并且在高浓度下可溶。热变性和尿素变性研究表明，尽管该蛋白具有模块化性质，但它仍表现出协同的两态折叠特性。结合先前对其他锚蛋白重复序列蛋白的研究，我们的数据表明两态折叠途径可能是锚蛋白重复序列蛋白和其他整合α-螺旋重复蛋白的一般特征。
