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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
Links dx.doi.org/10.1016/j.jmr.2012.02.00...
Keywords NMR; Protein structure; Projection spectroscopy; Multi-way decomposition
Subject categories Structural Biology, Molecular biophysics

Abstract

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
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