Department of Physics, University of Houston, Houston, Texas 77204, USA.
Department of Chemistry, Umeå University, Umeå 90187, Sweden.
Int J Mol Sci. 2009 Feb;10(2):572-588. doi: 10.3390/ijms10020572. Epub 2009 Feb 13.
How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on protein properties. We have found that folded forms of proteins become more compact in the presence of macromolecular crowding agents; if the protein is aspherical, the shape also changes (extent dictated by native-state stability and chemical conditions). It was also discovered that the shape of the macromolecular crowding agent modulates the folding mechanism of a protein; in addition, the extent of asphericity of the protein itself is an important factor in defining its folding speed.
细胞内拥挤的环境如何影响蛋白质的折叠、稳定性和结构，这是一个至关重要的问题，因为大多数蛋白质都是在细胞内合成并发挥功能的。在这里，我们描述了如何在体外和计算机中创建拥挤的条件，以及我们如何利用这些条件来探测对蛋白质性质的影响。我们发现，在大分子拥挤试剂存在的情况下，蛋白质的折叠形式变得更加紧凑；如果蛋白质是非球形的，形状也会发生变化（变化程度由天然状态稳定性和化学条件决定）。还发现，大分子拥挤试剂的形状会调节蛋白质的折叠机制；此外，蛋白质本身的非球形程度也是决定其折叠速度的一个重要因素。
