Department of Chemical Engineering, Columbia University, 500 W. 120th St., 801 Mudd Bldg., New York, NY 10027, United States.
Arch Biochem Biophys. 2013 Oct 1;538(1):6-15. doi: 10.1016/j.abb.2013.07.025. Epub 2013 Aug 8.
Allosteric regulation of protein function is key in controlling cellular processes so its underlying mechanisms are of primary concern to research in areas spanning protein engineering and drug design. However, due to the complex nature of allosteric mechanisms, a clear and predictive understanding of the relationship between protein structure and allosteric function remains elusive. Well established experimental approaches are available to offer a limited degree of characterization of mechanical properties within proteins, but the analytical capabilities of computational methods are evolving rapidly in their ability to accurately define the subtle and concerted structural dynamics that comprise allostery. This review includes a brief overview of allostery in proteins and an exploration of relevant experimental methods. An explanation of the transition from experimental toward computational methods for allostery is discussed, followed by a review of existing and emerging methods.
蛋白质功能的变构调节是控制细胞过程的关键，因此其潜在机制是蛋白质工程和药物设计等领域研究的首要关注点。然而，由于变构机制的复杂性，人们对蛋白质结构与变构功能之间的关系仍然难以清晰地进行预测和理解。现有的成熟实验方法可在一定程度上对蛋白质内的力学特性进行特征描述，但计算方法的分析能力在准确定义构成变构的细微协同结构动力学方面发展迅速。本综述包括对蛋白质变构的简要概述和对相关实验方法的探讨。讨论了从实验方法向变构计算方法的转变，并对现有和新兴方法进行了综述。
