Vranken Wim F
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium; Department of Structural Biology, VIB, 1050 Brussels, Belgium; Interuniversity Institute of Bioinformatics in Brussels, ULB-VUB, La Plaine Campus, Triomflaan, BC Building, 6th Floor, CP 263, 1050 Brussels, Belgium.
Prog Nucl Magn Reson Spectrosc. 2014 Oct;82:27-38. doi: 10.1016/j.pnmrs.2014.08.001. Epub 2014 Aug 26.
NMR spectroscopy is a key technique for understanding the behaviour of proteins, especially highly dynamic proteins that adopt multiple conformations in solution. Overall, protein structures determined from NMR spectroscopy data constitute just over 10% of the Protein Data Bank archive. This review covers the validation of these NMR protein structures, but rather than describing currently available methodology, it focuses on concepts that are important for understanding where and how validation is most relevant. First, the inherent characteristics of the protein under study have an influence on quality and quantity of the distinct types of data that can be acquired from NMR experiments. Second, these NMR data are necessarily transformed into a model for use in a structure calculation protocol, and the protein structures that result from this reflect the types of NMR data used as well as the protein characteristics. The validation of NMR protein structures should therefore take account, wherever possible, of the inherent behavioural characteristics of the protein, the types of available NMR data, and the calculation protocol. These concepts are discussed in the context of 'knowledge based' and 'model versus data' validation, with suggestions for questions to ask and different validation categories to consider. The principal aim of this review is to stimulate discussion and to help the reader understand the relationships between the above elements in order to make informed decisions on which validation approaches are the most relevant in particular cases.
核磁共振光谱法是理解蛋白质行为的关键技术，尤其是对于那些在溶液中呈现多种构象的高动态蛋白质。总体而言，通过核磁共振光谱数据确定的蛋白质结构仅占蛋白质数据库存档的10%多一点。本综述涵盖了这些核磁共振蛋白质结构的验证，但并非描述当前可用的方法，而是侧重于对理解验证在何处以及如何最为相关至关重要的概念。首先，所研究蛋白质的固有特性会影响可从核磁共振实验中获取的不同类型数据的质量和数量。其次，这些核磁共振数据必然会被转化为用于结构计算协议的模型，由此产生的蛋白质结构反映了所使用的核磁共振数据类型以及蛋白质特性。因此，核磁共振蛋白质结构的验证应尽可能考虑蛋白质的固有行为特性、可用的核磁共振数据类型以及计算协议。这些概念将在“基于知识”和“模型与数据”验证的背景下进行讨论，并提出需要询问的问题以及要考虑的不同验证类别建议。本综述的主要目的是激发讨论，并帮助读者理解上述要素之间的关系，以便在特定情况下就哪些验证方法最为相关做出明智的决策。
