To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

Structural characterisati… - University of Gothenburg, Sweden Till startsida
To content Read more about how we use cookies on

Structural characterisation of a histone domain by projection-decomposition

Journal article
Authors Jonas Fredriksson
Wolfgang Bermel
Martin Billeter
Published in Journal of Magnetic Resonance
Volume 217
Pages 48-52
ISSN 1090-7807
Publication year 2012
Published at Department of Chemistry and Molecular Biology
Pages 48-52
Language en
Keywords NMR; Protein structure; Projection spectroscopy; Multi-way decomposition
Subject categories Structural Biology, Molecular biophysics


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 α-helices and a two-stranded β-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.

Page Manager: Webmaster|Last update: 9/11/2012

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?