Combining NMR Spectroscopy and Molecular Dynamic Simulations to Solve and Analyze the Structure of Protein-RNA Complexes.
Binding Sites
CELF Proteins
/ chemistry
Humans
Hydrogen Bonding
Magnetic Resonance Spectroscopy
/ methods
Molecular Dynamics Simulation
Nucleic Acid Conformation
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
RNA
/ chemistry
RNA Splicing Factors
/ chemistry
Thermodynamics
MD simulation
Protein–RNA interactions
Solution-state NMR
Structures
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2019
2019
Historique:
entrez:
7
1
2019
pubmed:
7
1
2019
medline:
20
8
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30611432
pii: S0076-6879(18)30359-8
doi: 10.1016/bs.mie.2018.09.002
pii:
doi:
Substances chimiques
CELF Proteins
0
RBFOX1 protein, human
0
RNA Splicing Factors
0
RNA
63231-63-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
393-422Informations de copyright
© 2019 Elsevier Inc. All rights reserved.