Author

Sophie N. Jackson

Western Washington UniversityORCID 0000-0001-9133-6906Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

Jeanine F. AmacheriD· 2 shared John M. AntosiD· 2 shared Adam WachsmaniD· 1 shared Benjamin C Richardson· 1 shared Caroline CeravoloiD· 1 shared Darren E. LeeiD· 1 shared Erich G. WalkenhaueriD· 1 shared Jadon M. BlountiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersBiochemistry

Jeanine F. AmacherORCID

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2 papers

Recent·Most cited

A FRET Ligation Assay using Fluorescent Proteins for Bacterial Sortase Enzymes

Adam Wachsman, Erich G. Walkenhauer, Kaia Stover, Benjamin C Richardson, Sophie N. Jackson, John M. Antos, Jeanine F. Amacher

The paper presents an optimized FRET-based assay using mTurquoise2 and SYFP2 to monitor sortase-mediated ligation products, enabling screening of substrates and sortase variants.

bioRxiv · Aug 24, 2026 · PreprintBiochemistry

Biochemical characterization of Bacillus anthracis sortase B: Use in sortase mediated ligation and substrate recognition dependent on residues beyond the canonical pentapeptide binding motif for sortase enzymes

Sophie N. Jackson, Darren E. Lee, Jadon M. Blount, Kayla A. Croney, Justin W. Ibershof, Caroline Ceravolo, Kate M. Brown, Noah J. Goodwin-Rice, Kyle M. Whitham, James McCarty, John M. Antos, Jeanine F. Amacher

This study characterizes Bacillus anthracis SrtB, showing that residues outside the canonical pentapeptide motif are critical for activity and that engineered variants can improve ligation efficiency.

Journal of Biological Chemistry · Mar 4, 2025Peer-reviewedBiochemistry