Publications
2021
Chagot M E, Quinternet M, Manival X, Lebars I
Application of NMR Spectroscopy to Determine the 3D Structure of Small Non-Coding RNAs Journal Article
In: Methods Mol Biol, vol. 2300, pp. 251-266, 2021, ISBN: 33792884, (1940-6029 (Electronic) 1064-3745 (Linking) Journal Article).
Abstract | Links | BibTeX | Tags: 3D structure, dynamics, ENNIFAR, NMR, RNA, Unité ARN
@article{Chagot2021,
title = {Application of NMR Spectroscopy to Determine the 3D Structure of Small Non-Coding RNAs},
author = {M E Chagot and M Quinternet and X Manival and I Lebars},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=33792884},
doi = {10.1007/978-1-0716-1386-3_19},
isbn = {33792884},
year = {2021},
date = {2021-01-01},
journal = {Methods Mol Biol},
volume = {2300},
pages = {251-266},
abstract = {Many RNA architectures were discovered to be involved in a wide range of essential biological processes in all organisms from carrying genetic information to gene expression regulation. The remarkable ability of RNAs to adopt various architectures depending on their environment enables the achievement of their myriads of biological functions. Nuclear Magnetic Resonance (NMR) is a powerful technique to investigate both their structure and dynamics. NMR is also a key tool for studying interactions between RNAs and their numerous partners such as small molecules, ions, proteins, or other nucleic acids.In this chapter, to illustrate the use of NMR for 3D structure determination of small noncoding RNA, we describe detailed methods that we used for the yeast C/D box small nucleolar RNA U14 from sample preparation to 3D structure calculation.},
note = {1940-6029 (Electronic)
1064-3745 (Linking)
Journal Article},
keywords = {3D structure, dynamics, ENNIFAR, NMR, RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2002
Furrer Julien, Elbayed Karim, Bourdonneau Maryse, Raya Jésus, Limal David, Bianco Alberto, Piotto Martial
Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins Journal Article
In: Magnetic Resonance in Chemistry, vol. 40, no. 2, pp. 123–132, 2002, ISSN: 1097-458X.
Abstract | Links | BibTeX | Tags: 13C NMR, 1H NMR, high-resolution magic angle spinning, I2CT, magnetic susceptibility, NMR, relaxation, solid-phase peptide synthesis, Team-Bianco
@article{furrer_dynamic_2002,
title = {Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins},
author = {Julien Furrer and Karim Elbayed and Maryse Bourdonneau and Jésus Raya and David Limal and Alberto Bianco and Martial Piotto},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/mrc.970},
doi = {10.1002/mrc.970},
issn = {1097-458X},
year = {2002},
date = {2002-01-01},
urldate = {2020-03-31},
journal = {Magnetic Resonance in Chemistry},
volume = {40},
number = {2},
pages = {123--132},
abstract = {Under magic angle spinning, the NMR spectrum of the tetrapeptide Ala-Ile-Gly-Met bound to a Wang resin, and swollen in DMF, exhibits proton and carbon linewidths that are sharp enough to allow the complete characterization of the peptide using classical liquid-state NMR methods. The proton linewidths of the bound peptide remain, however, about three times larger than those of the free peptide in solution. The residual NMR linewidth originates essentially from incompletely averaged magnetic susceptibility effects due to the Wang resin. Replacing the aromatic Wang resin with a PEGA or POEPOP resin removes this effect. To investigate the contribution to line broadening of the peptide dynamics, relaxation studies were performed on the peptide bound to Wang and POEPOP resins. Copyright © 2001 John Wiley & Sons, Ltd.},
keywords = {13C NMR, 1H NMR, high-resolution magic angle spinning, I2CT, magnetic susceptibility, NMR, relaxation, solid-phase peptide synthesis, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}