Structural characterisation of a histone domain by projection-decomposition

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• 作者：Jonas Fredriksson^a ; ¹ ; Wolfgang Bermel^b ; Martin Billeter^a ; ^{martin.billeter@chem.gu.se}
• 关键词：NMR ; Protein structure ; Projection spectroscopy ; Multi-way decomposition
• 刊名：Journal of Magnetic Resonance
• 出版年：2012
• 期刊代码：126_10907807
• 类别：ch
• 出版时间：April, 2012
• 卷：217
• 期：Complete
• 页码：48-52
• 文件大小：668 K

摘要

We demonstrate that two projection experiments, a ¹⁵N-HSQC-NOESY-¹⁵N-HSQC and a ¹³C-HSQC-NOESY-¹⁵N-HSQC, recorded for a histone domain from yeast, contain enough information to support a structural characterisation of the protein. At the temperature used, 298 K, the histone domain exhibits a very high extent of chemical shift degeneracy that is uncharacteristic for a fully folded domain. Nonetheless, a structured core of 67 residues, which is formed by three 伪-helices and a two-stranded 尾-sheet is defined by this NOESY data; this core structure was shown earlier to be present at lower temperature. The above two experiments, which together required 18 h of instrument time, are part of a set of five projection experiments acquired during 2.5 days with the goal of complete characterisation of proteins, including full resonance assignment and structure.