†Institute for Research in Biomedicine, Via Vincenzo Vela 6, CH-6500 Bellinzona, Switzerland.
‡Laboratory of Physical Chemistry, Eidgenössische Technische Hochschule Zürich, Vladimir-Prelog-Weg 2, 8093 Zürich, Switzerland.
J Am Chem Soc. 2015 May 20;137(19):6270-8. doi: 10.1021/jacs.5b01289. Epub 2015 May 7.
Residual dipolar couplings (RDCs) are important probes in structural biology, but their analysis is often complicated by the determination of an alignment tensor or its associated assumptions. We here apply the maximum entropy principle to derive a tensor-free formalism which allows for direct, dynamic analysis of RDCs and holds the classic tensor formalism as a special case. Specifically, the framework enables us to robustly analyze data regardless of whether a clear separation of internal and overall dynamics is possible. Such a separation is often difficult in the core subjects of current structural biology, which include multidomain and intrinsically disordered proteins as well as nucleic acids. We demonstrate the method is tractable and self-consistent and generalizes to data sets comprised of observations from multiple different alignment conditions.
残基偶极耦合 (RDCs) 是结构生物学中的重要探针，但由于需要确定对准张量或其相关假设，其分析通常很复杂。我们在这里应用最大熵原理推导出一种无张量形式，允许直接、动态地分析 RDC，并将经典张量形式作为特例。具体来说，该框架使我们能够无论是否可以清晰地区分内部和整体动力学，都能稳健地分析数据。这种分离在当前结构生物学的核心主题中往往很困难，这些主题包括多域和固有无序的蛋白质以及核酸。我们证明该方法是可行的、一致的，并且可以推广到由多个不同对准条件下的观测结果组成的数据集。
