In-cell 13C NMR spectroscopy for the study of intrinsically disordered proteins

2014 ◽  
Vol 9 (9) ◽  
pp. 2005-2016 ◽  
Author(s):  
Isabella C Felli ◽  
Leonardo Gonnelli ◽  
Roberta Pierattelli
Keyword(s):  
Nmr Spectroscopy ◽  
13C Nmr ◽  
Intrinsically Disordered Proteins ◽  
13C Nmr Spectroscopy ◽  
Disordered Proteins ◽  
Intrinsically Disordered

scholarly journals Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy

Molecules ◽  
2013 ◽  
Vol 18 (9) ◽  
pp. 10802-10828 ◽  
Author(s):  
Simone Kosol ◽  
Sara Contreras-Martos ◽  
Cesyen Cedeño ◽  
Peter Tompa
Keyword(s):  
Nmr Spectroscopy ◽  
Structural Characterization ◽  
Intrinsically Disordered Proteins ◽  
Disordered Proteins ◽  
Intrinsically Disordered

scholarly journals Towards Targeting the Disordered SARS-CoV-2 Nsp2 C-terminal Region: Partial Structure and Dampened Mobility Revealed by NMR Spectroscopy

2020 ◽  
Author(s):  
Miguel Mompeán ◽  
Miguel Á. Treviño ◽  
Douglas V. Laurents
Keyword(s):  
Nmr Spectroscopy ◽  
Drug Targets ◽  
Intrinsically Disordered Proteins ◽  
Small Population ◽  
Terminal Region ◽  
Disordered Proteins ◽  
X Ray Crystallography ◽  
Intrinsically Disordered ◽  
Level Information ◽  
Human Proteins

AbstractIntrinsically disordered proteins (IDPs) play essential roles in regulating physiological processes in eukaryotic cells. Many virus use their own IDPs to “hack” these processes to disactive host defenses and promote viral growth. Thus, viral IDPs are attractive drug targets. While IDPs are hard to study by X-ray crystallography or cryo-EM, atomic level information on their conformational perferences and dynamics can be obtained using NMR spectroscopy. SARS-CoV-2 Nsp2 interacts with human proteins that regulate translation initiation and endosome vesicle sorting, and the C-terminal region of this protein is predicted to be disordered. Molecules that block these interactions could be valuable leads for drug development. To enable inhibitor screening and to uncover conformational preferences and dynamics, we have expressed and purified the 13C,15N-labeled C-terminal region of Nsp2. The 13Cβ and backbone 13CO, 1HN, 13Cα and 15N nuclei were assigned by analysis of a series of 2D 1H-15N HSQC and 13C-15N CON as well as 3D HNCO, HNCA, CBCAcoNH and HncocaNH spectra. Overall, the chemical shift data confirm that this region is chiefly disordered, but contains two five-residue segments that adopt a small population of β-strand structure. Whereas the region is flexible on ms/ms timescales as gauged by T1ρ measurements, the {1H}-15N NOEs reveal a flexibility on ns/ps timescales that is midway between a fully flexible and a completely rigid chain.

H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins

2009 ◽  
Vol 198 (2) ◽  
pp. 275-281 ◽  
Author(s):  
Wolfgang Bermel ◽  
Ivano Bertini ◽  
Veronika Csizmok ◽  
Isabella C. Felli ◽  
Roberta Pierattelli ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Intrinsically Disordered Proteins ◽  
Heteronuclear Nmr ◽  
Disordered Proteins ◽  
Intrinsically Disordered ◽  
Heteronuclear Nmr Spectroscopy

Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy

2016 ◽  
Vol 128 (26) ◽  
pp. 7544-7548 ◽  
Author(s):  
Juan Lopez ◽  
Robert Schneider ◽  
Francois-Xavier Cantrelle ◽  
Isabelle Huvent ◽  
Guy Lippens
Keyword(s):  
Nmr Spectroscopy ◽  
Intrinsically Disordered Proteins ◽  
Disordered Proteins ◽  
Cross Polarization ◽  
Intrinsically Disordered
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