1H, 13C and 15N chemical shift assignment of the stem-loops 5b + c from the 5′-UTR of SARS-CoV-2

Autor: Klara R. Mertinkus, J. Tassilo Grün, Nadide Altincekic, Jasleen Kaur Bains, Betül Ceylan, Jan-Peter Ferner, Lucio Frydman, Boris Fürtig, Martin Hengesbach, Katharina F. Hohmann, Daniel Hymon, Jihyun Kim, Božana Knezic, Mihajlo Novakovic, Andreas Oxenfarth, Stephen A. Peter, Nusrat S. Qureshi, Christian Richter, Tali Scherf, Andreas Schlundt, Robbin Schnieders, Harald Schwalbe, Elke Stirnal, Alexey Sudakov, Jennifer Vögele, Anna Wacker, Julia E. Weigand, Julia Wirmer-Bartoschek, Maria A. Wirtz Martin, Jens Wöhnert

Publikováno v: Biomolecular NMR Assignments, 16

The ongoing pandemic of the respiratory disease COVID-19 is caused by the SARS-CoV-2 (SCoV2) virus. SCoV2 is a member of the Betacoronavirus genus. The 30 kb positive sense, single stranded RNA genome of SCoV2 features 5'- and 3'-genomic ends that ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99f387aa7cf6d5f0b5a6907a6bb95fa8
https://hdl.handle.net/20.500.11850/534661

NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs

Autor: Nusrat Shahin, Qureshi, Tobias, Matzel, Erhan Can, Cetiner, Robbin, Schnieders, Hendrik R A, Jonker, Harald, Schwalbe, Boris, Fürtig

Publikováno v: Nucleic Acids Research

The ribosomal S1 protein (rS1) is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which cou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c6b6eaf20bff32fede29d670a88b7d29
https://pubmed.ncbi.nlm.nih.gov/34223902

NMR resonance assignments for the GTP-binding RNA aptamer 9-12 in complex with GTP

Autor: Robbin Schnieders, Jens Wöhnert, Antje C. Wolter, Elisabeth Strebitzer, Elke Duchardt-Ferner, Angela Pianu, Boris Fürtig, Christoph Kreutz, Johannes Kremser

Publikováno v: Biomolecular NMR Assignments. 13:281-286

Ligand binding RNAs such as artificially created RNA-aptamers are structurally highly diverse. Therefore, they represent important model systems for investigating RNA-folding, RNA-dynamics and the molecular recognition of chemically very different li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a60da1341dfeedc4c0461bca1d291203
https://doi.org/10.1007/s12104-019-09892-z

Magnetization Transfer to Enhance NOE Cross‐Peaks among Labile Protons: Applications to Imino–Imino Sequential Walks in SARS‐CoV‐2‐Derived RNAs

Autor: Andreas Oxenfarth, Mihajlo Novakovic, Robbin Schnieders, Eriks Kupče, Tali Scherf, Harald Schwalbe, J Tassilo Grün, Julia Wirmer-Bartoschek, Christian Richter, Lucio Frydman

Publikováno v: Angewandte Chemie International Edition
Angewandte Chemie (International Ed. in English)
Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)

2D NOESY plays a central role in structural NMR spectroscopy. We have recently discussed methods that rely on solvent‐driven exchanges to enhance NOE correlations between exchangeable and non‐exchangeable protons in nucleic acids. Such methods, h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::773193e7ee738be4afbc17be4e81cfbf

NMR Spectroscopy of Large Functional RNAs: From Sample Preparation to Low-Gamma Detection

Autor: Martin Hengesbach, Christian Richter, Boris Fürtig, Robbin Schnieders, Tobias Matzel, Alexey Sudakov, Harald Schwalbe, Bozana Knezic, Heidi Zetzsche

Publikováno v: Current protocols in nucleic acid chemistryLiterature Cited. 82(1)

NMR spectroscopy is a potent method for the structural and biophysical characterization of RNAs. The application of NMR spectroscopy is restricted in RNA size and most often requires isotope-labeled or even selectively labeled RNAs. Additionally, new

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3a5aad30737738b86175dcc30c86b50
https://pubmed.ncbi.nlm.nih.gov/32960489