Chemical shift assignments and secondary structure prediction of the phosphorelay protein VanU from Vibrio anguillarum.
Abstract
Vibrio anguillarum is a biofilm forming Gram-negative bacterium that survives prolonged
periods in seawater and causes vibriosis in marine life. A quorum-sensing signal transduction
pathway initiates biofilm formation in response to environmental stresses. The phosphotransferase
protein VanU is the focal point of the quorum-sensing pathway and facilitates the
regulation between independent phosphorelay systems that activate or repress biofilm
formation. Here we report the (1)H, (13)C, and (15)N backbone and side chain resonance
assignments and secondary structure prediction for VanU from V. anguillarum.
Type
Journal articleSubject
VibrioPhosphotransferases
Bacterial Proteins
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
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https://hdl.handle.net/10161/28901Published Version (Please cite this version)
10.1007/s12104-013-9478-2Publication Info
Bobay, Benjamin G; Thompson, Richele J; Milton, Debra L; & Cavanagh, John (2014). Chemical shift assignments and secondary structure prediction of the phosphorelay
protein VanU from Vibrio anguillarum. Biomolecular NMR assignments, 8(1). pp. 177-179. 10.1007/s12104-013-9478-2. Retrieved from https://hdl.handle.net/10161/28901.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Benjamin Bobay
Assistant Professor in Radiology
I am the Assistant Director of the Duke University NMR Center and an Assistant Professor
in the Duke Radiology Department. I was originally trained as a structural biochemist
with an emphasis on utilizing NMR and continue to use this technique daily helping
collaborators characterize protein structures and small molecules through a diverse
set of NMR experiments. Through the structural characterization of various proteins,
from both planta and eukaryotes, I have developed a robust protocol of ut

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