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Open Access Green as soon as Postprint is submitted to ZB.
Reconstitution of isotopically labeled ribosomal protein L29 in the 50S large ribosomal subunit for solution-state and solid-state NMR.
Methods Mol. Biol. 1764, 87-100 (2018)
Solid-state nuclear magnetic resonance (NMR) has recently emerged as a method of choice to study structural and dynamic properties of large biomolecular complexes at atomic resolution. Indeed, recent technological and methodological developments have enabled the study of ever more complex systems in the solid-state. However, to explore multicomponent protein complexes by NMR, specific labeling schemes need to be developed that are dependent on the biological question to be answered. We show here how to reconstitute an isotopically labeled protein within the unlabeled 50S or 70S ribosomal subunit. In particular, we focus on the 63-residue ribosomal protein L29 (~7 kDa), which is located at the exit of the tunnel of the large 50S ribosomal subunit (~1.5 MDa). The aim of this work is the preparation of a suitable sample to investigate allosteric conformational changes in a ribosomal protein that are induced by the nascent polypeptide chain and that trigger the interaction with different chaperones (e.g., trigger factor or SRP).
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Isotope Labeling ; Mas Solid-state Nmr Spectroscopy ; Protein Complex Reconstitution
ISSN (print) / ISBN
1064-3745
e-ISSN
1940-6029
Book Volume Title
Protein Complex Assembly
Journal
Methods in Molecular Biology
Quellenangaben
Volume: 1764,
Pages: 87-100
Publisher
Springer
Publishing Place
Berlin [u.a.]
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)