Creveld L D, Amadei A, van Schaik R C, Pepermans H A, de Vlieg J, Berendsen H J
Unilever Research Laboratory Vlaardingen, The Netherlands.
Proteins. 1998 Nov 1;33(2):253-64.
The implementation of cutinase from Fusarium solani pisi as a fat-stain removing ingredient in laundry washing is hampered by its unfolding in the presence of anionic surfactants. In this work we present molecular dynamics (MD) computer simulations on cutinase and analysis procedures to distinguish the movements related to its functional behavior (e.g., substrate binding) from those related to the unfolding of the enzyme. Two kinds of MD-simulations were performed: a simulation mimicking the thermal motion at room temperature, and several simulations in which unfolding is induced either by high temperature or by using a modified water-protein interaction potential. Essential dynamics analyses (A. Amadei et al., Proteins 17:412-425, 1993) on the simulations identify distinct regions in the molecular structure of cutinase in which the motions occur for function and initial unfolding. The unfolding in various simulations starts in a similar way, suggesting that mutations in the regions involved might stabilize the enzyme without affecting its functionality.
来自豌豆镰孢菌的角质酶作为洗衣去污成分在洗衣过程中的应用受到其在阴离子表面活性剂存在下展开的阻碍。在这项工作中，我们展示了对角质酶的分子动力学（MD）计算机模拟以及分析程序，以区分与其功能行为（例如底物结合）相关的运动和与酶展开相关的运动。进行了两种MD模拟：一种模拟室温下的热运动，以及几种通过高温或使用改性水 - 蛋白质相互作用势诱导展开的模拟。对模拟结果进行的主成分动力学分析（A. Amadei等人，《蛋白质》17:412 - 425，1993）确定了角质酶分子结构中发生功能运动和初始展开运动的不同区域。各种模拟中的展开以相似的方式开始，这表明所涉及区域的突变可能会稳定酶而不影响其功能。
