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Combining NMR Spectroscopy and Molecular Dynamic Simulations to Solve and Analyze the Structure of Protein-RNA Complexes
S. Campagne, M. Krepl, J. Sponer, FH. Allain,
Methods in enzymology.
2019 ;
614 (-) :
393-422.
[pub] 20181210
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
Perzistentní odkaz
https://www.medvik.cz/link/bmc19034839
- MeSH
- CELF proteiny chemie metabolismus MeSH
- interakční proteinové domény a motivy MeSH
- konformace nukleové kyseliny MeSH
- konformace proteinů, alfa-helix MeSH
- konformace proteinů, beta-řetězec MeSH
- lidé MeSH
- magnetická rezonanční spektroskopie metody MeSH
- RNA chemie genetika metabolismus MeSH
- sestřihové faktory chemie metabolismus MeSH
- simulace molekulární dynamiky * MeSH
- termodynamika MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- vodíková vazba MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Understanding the RNA binding specificity of protein is of primary interest to decipher their function in the cell. Here, we review the methodology used to solve the structures of protein-RNA complexes using solution-state NMR spectroscopy: from sample preparation to structure calculation procedures. We also describe how molecular dynamics simulations can help providing additional information on the role of key amino acid side chains and of water molecules in protein-RNA recognition.
Department of Biology ETH Zürich Institute of Molecular Biology and Biophysics Zürich Switzerland
Institute of Biophysics of the Czech Academy of Sciences Brno Czech Republic
Citace poskytuje Crossref.org
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- $a Understanding the RNA binding specificity of protein is of primary interest to decipher their function in the cell. Here, we review the methodology used to solve the structures of protein-RNA complexes using solution-state NMR spectroscopy: from sample preparation to structure calculation procedures. We also describe how molecular dynamics simulations can help providing additional information on the role of key amino acid side chains and of water molecules in protein-RNA recognition.
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