Department of Informatics, University of Bergen, N-5020 Bergen, Norway.
Protein Sci. 2011 Jan;20(1):197-209. doi: 10.1002/pro.558.
Normal mode analyses of homologous proteins at the family and superfamily level show that slow dynamics are similar and are preserved through evolution. This study investigates how the slow dynamics of proteins is affected by variation in the protein architecture and fold. For this purpose, we have used computer-generated protein models based on idealized protein structures with varying folds. These are shown to be protein-like in their behavior, and they are used to investigate the influence of architecture and fold on the slow dynamics. We compared the dynamics of models having different folds but similar architecture and found the architecture to be the dominant factor for the slow dynamics.
同源蛋白的正常模式分析在家族和超家族水平上表明，慢动力学相似，并通过进化得以保留。本研究调查了蛋白质的慢动力学如何受到蛋白质结构和折叠变化的影响。为此，我们使用了基于具有不同折叠的理想化蛋白质结构的计算机生成的蛋白质模型。这些模型在行为上表现出类蛋白质的特征，并且用于研究结构和折叠对慢动力学的影响。我们比较了具有不同折叠但相似结构的模型的动力学，发现结构是慢动力学的主要因素。
