The programmed ribosomal frameshift (PRF) region is found in the RNA genome of all coronaviruses and shifts the ribosome reading frame through formation of a three-stem pseudoknot structure, allowing the translation of essential viral proteins. Using NMR spectroscopy, comparative sequence analyses and functional assays we show that, in the absence of the ribosome, a 123-nucleotide sequence encompassing the PRF element of SARS-CoV-2 adopts a well-defined two-stem loop structure that is conserved...
Structures and Dynamics of Protein Folding on the Ribosome by NMR Spectroscopy
Structures and Dynamics of Protein Folding on the Ribosome by NMR Spectroscopy
Publication date: 2 February 2018
Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1</br>
Author(s): Anais M. Cassaignau, Christopher Waudby, Tomasz Wlodarski, Lisa Cabrita, John Christodoulou</br>
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[NMR paper] A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
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Nat Protoc. 2016 Aug;11(8):1492-1507
Authors: Cassaignau AM, Launay HM, Karyadi ME, Wang X, Waudby CA, Deckert A, Robertson AL, Christodoulou J, Cabrita LD
Abstract
During biosynthesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that is central...
[NMR paper] Protein folding on the ribosome studied using NMR spectroscopy.
Protein folding on the ribosome studied using NMR spectroscopy.
Protein folding on the ribosome studied using NMR spectroscopy.
Prog Nucl Magn Reson Spectrosc. 2013 Oct;74C:57-75
Authors: Waudby CA, Launay H, Cabrita LD, Christodoulou J
Abstract
NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution. In recent years NMR methods have also been...
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Protein folding on the ribosome studied using NMR spectroscopy
Protein folding on the ribosome studied using NMR spectroscopy
Publication date: Available online 27 July 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Christopher A. Waudby , Hélène Launay , Lisa D. Cabrita , John Christodoulou</br>
NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution. In recent years NMR methods have also been...
[NMR paper] Millisecond protein folding studied by NMR spectroscopy.
Millisecond protein folding studied by NMR spectroscopy.
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Protein Pept Lett. 2005 Feb;12(2):139-46
Authors: Zeeb M, Balbach J
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond...
Sarbecovirus programmed ribosome frameshift RNA element folding studied by NMR spectroscopy and comparative analyses
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