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Updated: May 24, 2026
06:32
Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
Published on: March 9, 2022
Structural characterisation of a histone domain by projection-decomposition
Jonas Fredriksson1, Wolfgang Bermel, Martin Billeter
1Biophysics Group, Department of Chemistry, University of Gothenburg, Box 462, 405 30 Gothenburg, Sweden.
Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|March 13, 2012
Summary
Two nuclear magnetic resonance (NMR) experiments successfully characterized a yeast histone domain structure. Despite high chemical shift degeneracy, a stable core of 67 residues was identified using NOESY data.
Area of Science:
- Structural biology
- Biophysics
- Nuclear Magnetic Resonance (NMR) spectroscopy
Background:
- Histone domains are crucial for DNA packaging and regulation.
- Protein structure determination is essential for understanding function.
- High temperature can induce chemical shift degeneracy in proteins, complicating structural analysis.
Purpose of the Study:
- To assess the feasibility of structural characterization using specific NMR projection experiments.
- To investigate the structural properties of a yeast histone domain at 298 K.
- To evaluate the efficiency of a set of five projection experiments for complete protein characterization.
Main Methods:
- Utilized two specific 15N-HSQC-NOESY-15N-HSQC and 13C-HSQC-NOESY-15N-HSQC projection experiments.
- Acquired data over 18 hours of instrument time as part of a larger 2.5-day experiment set.
- Analyzed Nuclear Overhauser Effect (NOE) data to define inter-residue distances.
Main Results:
- Successfully defined a structured core of 67 residues within the histone domain.
- Identified a stable core composed of three alpha-helices and a two-stranded beta-sheet.
- Observed significant chemical shift degeneracy, uncharacteristic of a fully folded domain at 298 K.
Conclusions:
- Two NMR projection experiments provide sufficient data for structural characterization of proteins.
- A structured core, previously observed at lower temperatures, is maintained in the yeast histone domain at 298 K.
- The employed set of five projection experiments shows promise for complete protein characterization, including resonance assignment and structure determination.
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