Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh-202002, India.
Int J Biol Macromol. 2010 Mar 1;46(2):250-4. doi: 10.1016/j.ijbiomac.2009.12.013. Epub 2010 Jan 8.
Little work has been done to understand the folding of proteins at alkaline conditions. BSA acquires a partially reversible unfolded state at pH 13.0, devoid of any native structure. Introduction of methanol, ethanol and 2-propanol with the alkaline unfolded protein resulted in beta-sheet-like structure formation, and 2,2,2-trifluroethanol found to enhance alpha-helical conformations with simultaneous increase in aggregation. The extent of secondary and tertiary structure formation is in the order of methanol < ethanol < 2-propanol < 2,2,2-trifluroethanol. Exposure of hydrophobic core of protein molecules in apolar environment of 2,2,2-trifluroethanol seems to promote intermolecular cluster formation. This is one of the very few reports that alpha-helical structures can also aggregate.
在碱性条件下，对蛋白质折叠的研究还很少。BSA 在 pH 值为 13.0 时获得部分可逆的去折叠状态，没有任何天然结构。在碱性去折叠蛋白中加入甲醇、乙醇和 2-丙醇会导致形成类似β-折叠的结构，而 2,2,2-三氟乙醇被发现可以增强α-螺旋构象，同时增加聚集。二级和三级结构形成的程度按甲醇<乙醇<2-丙醇<2,2,2-三氟乙醇的顺序排列。在 2,2,2-三氟乙醇的非极性环境中，暴露出蛋白质分子的疏水核心似乎促进了分子间簇的形成。这是少数几个报道α-螺旋结构也可以聚集的报告之一。
