Characterizing protein crystal contacts and their role in crystallization: rubredoxin as a case study.
Characterizing protein crystal contacts and their role in crystallization: rubredoxin as a case study.
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DOI：
10.1039/c3sm52175c
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发表时间：
2014-01-14
期刊：
影响因子：
3.4
通讯作者：
Charbonneau P
中科院分区：
文献类型：
--
作者：
Fusco D;Headd JJ;De Simone A;Wang J;Charbonneau P
结构生物学和软物质领域已经独立地寻找了使蛋白质结晶合理化的基本原理。然而，这两个学科之间的概念差异和有限的重叠迄今为止阻碍了对这一现象的全面理解。我们进行了计算研究的蛋白质从rubredoxin家庭的桥梁这两个领域。使用原子模拟，我们表征他们的晶体接触，并相应地parameterized补丁粒子模型。将这些示意性模型的相图与实验结果进行比较，使我们能够批判性地研究这两种方法背后的假设。该研究还揭示了蛋白质-蛋白质相互作用的特征，这些特征可以用来更普遍地结晶蛋白质。
The fields of structural biology and soft matter have independently sought out fundamental principles to rationalize protein crystallization. Yet the conceptual differences and the limited overlap between the two disciplines have thus far prevented a comprehensive understanding of the phenomenon to emerge. We conduct a computational study of proteins from the rubredoxin family that bridges the two fields. Using atomistic simulations, we characterize their crystal contacts, and accordingly parameterize patchy particle models. Comparing the phase diagrams of these schematic models with experimental results enables us to critically examine the assumptions behind the two approaches. The study also reveals features of protein-protein interactions that can be leveraged to crystallize proteins more generally.