Liang Jie
Department of Bioengineering, University of Illinois at Chicago, Chicago, IL 60612, USA.
Annu Int Conf IEEE Eng Med Biol Soc. 2009;2009:2324-7. doi: 10.1109/IEMBS.2009.5335112.
Proteins contain thousands or more atoms and have complex shapes. We discuss here the computation of protein packing defects, in the form of voids and pockets, from experimentally resolved protein structures, and the nature of their distribution and scaling behavior, as well as their origin. We further discuss how evolutionary selection pressure due to biological function unaltered by selection pressure due to constraints from folding and stability can be isolated and estimated, and how such information can be used to predict protein function and characterize binding properties of enzymes.
蛋白质含有数千个或更多原子，且形状复杂。我们在此讨论从实验解析的蛋白质结构中计算以空隙和口袋形式存在的蛋白质堆积缺陷，以及它们的分布性质、标度行为及其起源。我们还将讨论如何分离和估计由于生物学功能产生的进化选择压力（这种压力不受折叠和稳定性限制所产生的选择压力影响），以及如何利用这些信息来预测蛋白质功能并表征酶的结合特性。
