Piserchio Andrea, Dalby Kevin N, Ghose Ranajeet
Department of Chemistry, The City College of New York, New York, NY, USA.
Methods Mol Biol. 2012;831:359-68. doi: 10.1007/978-1-61779-480-3_19.
A first step toward the analysis of the structure, dynamics, and interactions of proteins by NMR is obtaining an acceptable level of resonance assignments. This process is nontrivial in most eukaryotic kinases given their size and suboptimal behavior in solution. Using inactive ERK2 as a representative example, we describe the procedures we utilized to achieve a significant degree of completeness of backbone resonance assignment.
通过核磁共振(NMR)分析蛋白质的结构、动力学和相互作用的第一步是获得可接受水平的共振归属。鉴于大多数真核激酶的大小以及它们在溶液中的欠佳表现,这个过程并非易事。以无活性的细胞外信号调节激酶2(ERK2)作为代表性例子,我们描述了为实现主链共振归属的显著完整性所采用的程序。