Beger R D, Bolton P H
Department of Chemistry, Wesleyan University, Middletown, CT 06459, USA.
J Biomol NMR. 1997 Sep;10(2):129-42. doi: 10.1023/a:1018302105638.
The chemical shifts of the backbone atoms of proteins can be used to obtain restraints that can be incorporated into structure determination methods. Each chemical shift can be used to define a restraint and these restraints can be simultaneously used to define the local, secondary structure features. The global fold can be determined by a combined use of the chemical shift based restraints along with the long-range information present in the NOEs of partially deuterated proteins or the amide-amide NOEs but not from such limited NOE data sets alone. This approach has been demonstrated to be capable of determining the overall folding pattern of four proteins. This suggests that solution-state NMR methods can be extended to the structure determination of larger proteins by using the information present in the chemical shifts of the backbone atoms along with the data that can be obtained on a small number of labeled forms.
蛋白质主链原子的化学位移可用于获得可纳入结构测定方法的约束条件。每个化学位移可用于定义一个约束条件，这些约束条件可同时用于定义局部二级结构特征。通过结合基于化学位移的约束条件以及部分氘代蛋白质的NOE或酰胺-酰胺NOE中存在的长程信息，而非仅从如此有限的NOE数据集，可确定整体折叠结构。已证明这种方法能够确定四种蛋白质的整体折叠模式。这表明，通过利用主链原子化学位移中存在的信息以及可从少量标记形式获得的数据，溶液态核磁共振方法可扩展到更大蛋白质的结构测定。
