Structural Characterisation of a Histone Domain by Projection-Decomposition
Publication year: 2012
Source:Journal of Magnetic Resonance
Jonas Fredriksson, Wolfgang Bermel, Martin Billeter
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, 298K, 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 ?-helices and a two-stranded ?-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 hours 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.
Graphical Abstract
Graphical abstract Highlights
? Protein structures from projection-decomposition data. ? Complete protein characterisation in 2.5 days of measurements. ? NOESY data for a highly flexible histone domain. ? Correlation between NOESY shapes and protein 3D structure.
Source:
Journal of Magnetic Resonance