Structural Characterisation of a Histone Domain by Projection-Decomposition
 

Structural Characterisation of a Histone Domain by Projection-Decomposition


Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Jonas Fredriksson, Wolfgang Bermel, Martin Billeter</br>
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

http://ars.sciencedirect.com/content...000638-fx1.jpg 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.</br>
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Source: Journal of Magnetic Resonance