Biomolecular NMR Using a Microcoil NMR Probe − New Technique for the Chemical Shift Assignment of Aromatic Side Chains in Proteins

2004 ◽  
Vol 126 (18) ◽  
pp. 5873-5878 ◽  
Author(s):  
Wolfgang Peti ◽  
James Norcross ◽  
Gary Eldridge ◽  
Mark O'Neil-Johnson
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignment ◽  
New Technique ◽  
Side Chains ◽  
Biomolecular Nmr ◽  
Microcoil Nmr ◽  
Shift Assignment ◽  
Aromatic Side Chains

scholarly journals 1H, 13C and 15N assignment of stem-loop SL1 from the 5'-UTR of SARS-CoV-2

2021 ◽  
Author(s):  
Christian Richter ◽  
Katharina F. Hohmann ◽  
Sabrina Toews ◽  
Daniel Mathieu ◽  
Nadide Altincekic ◽  
...  
Keyword(s):  
Life Cycle ◽  
Chemical Shift ◽  
Base Pair ◽  
Chemical Shift Assignment ◽  
Potential Functions ◽  
Regulatory Rna ◽  
Structural Element ◽  
Stem Loop ◽  
Internal Loop ◽  
Shift Assignment

AbstractThe stem-loop (SL1) is the 5'-terminal structural element within the single-stranded SARS-CoV-2 RNA genome. It is formed by nucleotides 7–33 and consists of two short helical segments interrupted by an asymmetric internal loop. This architecture is conserved among Betacoronaviruses. SL1 is present in genomic SARS-CoV-2 RNA as well as in all subgenomic mRNA species produced by the virus during replication, thus representing a ubiquitous cis-regulatory RNA with potential functions at all stages of the viral life cycle. We present here the 1H, 13C and 15N chemical shift assignment of the 29 nucleotides-RNA construct 5_SL1, which denotes the native 27mer SL1 stabilized by an additional terminal G-C base-pair.

NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel

1998 ◽  
Vol 76 (2-3) ◽  
pp. 341-350 ◽  
Author(s):  
Voula Kanelis ◽  
Neil A Farrow ◽  
Lewis E Kay ◽  
Daniela Rotin ◽  
Julie D Forman-Kay
Keyword(s):  
Chemical Shift ◽  
Sodium Channel ◽  
Chemical Shifts ◽  
Epithelial Sodium Channel ◽  
Chemical Shift Assignment ◽  
Nmr Studies ◽  
Ww Domains ◽  
Ww Ii ◽  
Py Motif ◽  
Shift Assignment

Nedd4 (neuronal precursor cell-expressed developmentally down-regulated 4) is a ubiquitin-protein ligase containing multiple WW domains. We have previously demonstrated the association between the WW domains of Nedd4 and PPxY (PY) motifs of the epithelial sodium channel (ENaC). In this paper, we report the assignment of backbone 1Hα, 1HN, 15N, 13C', 13Cα, and aliphatic 13C resonances of a fragment of rat Nedd4 (rNedd4) containing the two C-terminal WW domains, WW(II+III), complexed to a PY motif-containing peptide derived from the β subunit of rat ENaC, the βP2 peptide. The secondary structures of these two WW domains, determined from chemical shifts of 13Cα and 13Cβ resonances, are virtually identical to those of the WW domains of the Yes-associated protein YAP65 and the peptidyl-prolyl isomerase Pin1. Triple resonance experiments that detect the 1Hα chemical shift were necessary to complete the chemical shift assignment, owing to the large number of proline residues in this fragment of rNedd4. A new experiment, which correlates sequential residues via their 15N nuclei and also detects 1Hα chemical shifts, is introduced and its utility for the chemical shift assignment of sequential proline residues is discussed. Data collected on the WW(II+III)-βP2 complex indicate that these WW domains have different affinities for the βP2 peptide.Key words: WW domain, PY motif, Nedd4, ENaC, NMR.

NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein

2019 ◽  
Vol 13 (1) ◽  
pp. 195-199
Author(s):  
N. Herr ◽  
M. N. Webby ◽  
E. M. M. Bulloch ◽  
M. Schmitz ◽  
R. L. Kingston
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignment ◽  
Terminal Region ◽  
Nmr Chemical Shift ◽  
Shift Assignment
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