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Samuel Barker

As seen in: Wiley Online Library, The Journal of Biological Chemistry
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Articles

Structural and Biophysical Characterization of the Yersinia Type Three Secretion System ATPase YscN

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By Samuel Barker, Andrew Hammer, Sean Johnson, Porter K. Ellis
| Wiley Online Library Verified
Conflicts of Interest The authors declare no conflicts of interest. Data Availability Statement Main text data are contained within this article and structure coordinates are deposited in the RCSB Protein Data Bank (PDB IDs: 9E58 and 9DMD). Supplemental data are in the document. Supporting Information Filename Description prot70112-sup-0001-supinfo.docxWord 2007 document , 2.1 MB Figure S1: Impact of YscNR359A active site mutation on structure and activity.
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Structural and functional characterization of the IpaD π-helix reveals critical roles in DOC interaction, T3SS apparatus maturation, and Shigella virulence

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By Samuel Barker, Sean Johnson, Nicholas E. Dickenson
| The Journal of Biological Chemistry Verified
Circular dichroism (CD) spectroscopy provided an efficient means of preliminary structural characterization of the two IpaD mutants and a way to ensure that the mutations did not compromise the overall protein structure. The far-UV CD spectra of wild-type IpaD and the two engineered mutants were collected in the absence and presence of DOC and are all nearly superimposable (Figure 1A).
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