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NMR processing:
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Side-chains:
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NOEs:
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
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GeNMR
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Refinement:
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Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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From structure:
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ArShift- Aromatic
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PPM
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From sequence:
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Camcoil
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Disordered proteins:
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Format conversion & validation:
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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Default NMR resonance assignments for a ProQ homolog from Legionella pneumophila.

NMR resonance assignments for a ProQ homolog from Legionella pneumophila.

Related Articles NMR resonance assignments for a ProQ homolog from Legionella pneumophila.

Biomol NMR Assign. 2018 Jun 22;:

Authors: Immer C, Hacker C, Wöhnert J

Abstract
Regulation of gene expression on a post-transcriptional level by small non-coding regulatory RNAs (sRNAs) is very common in bacteria. sRNAs base pair with sequences in their target messenger RNAs (mRNAs) and thereby regulate translation initiation or mRNA stability. Specialized RNA-binding proteins (RBPs) facilitate these regulatory sRNA/mRNA interactions by acting as RNA chaperones. A well-known example for such an RNA chaperone which is widespread in bacteria is the Hfq protein. Recently, the ProQ/FinO protein family was identified as a new class of RNA chaperones involved in sRNA based regulation. Only a few members of this protein family have been structurally characterized so far. In particular, the structural basis for RNA-binding and recognition has not yet been established for this class of proteins. Here, we report the 1H, 13C and 15N NMR resonance assignments for a ProQ homolog (Lpp 1663) from the gram-negative pathogenic bacterium Legionella pneumophila which will facilitate further structural and dynamic studies of this protein and its interaction with RNA targets.


PMID: 29934867 [PubMed - as supplied by publisher]



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