Ryan Julian
University of California-Riverside, CA·Chemistry
The same gene can give rise to many slightly different versions of a protein, called proteoforms. Differences arise through alternative splicing, chemical tags added after the protein is made, or spontaneous chemical changes.
- Fields
Chemistry
Biochemistry
- Topics
proteoforms
top-down proteomics
mass spectrometry
- Grants
- 1 known grant, through Feb 2030
What they work on
- Design and synthesize photoactivated chemical modifiers that install a weak link at chosen residues in a protein backbone, so the protein can be split at that spot on demand.
- Develop mass spectrometry methods that use light-generated radicals to trigger selective dissociation at the modified sites, replacing the random fragmentation of current top-down proteomics.
- Apply selective dissociation to distinguish nearly identical proteoforms, such as isomers that differ only in where a single modification sits, toward populating a human proteoform atlas.
More about the research
Proteoforms are what actually carry out work in cells, and their structures cannot be predicted from DNA alone. Telling them apart is hard. Two proteoforms may differ only in where a single chemical tag sits, which makes them nearly identical to most analytical tools.
Why it matters
Many diseases involve specific protein versions, not just genes. Better tools for identifying proteoforms could help researchers pinpoint which protein forms drive health and disease, a first step toward finding treatment targets. The methods could also help build a reference atlas of human proteoforms.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Liangliang Sun
Michigan State University, MI·Chemistry
Advance CE-MS top-down proteomics to build a first draft proteoform atlas of HeLa cells. The atlas will contain at least one intact protein form for every protein-coding gene.
Si Wu
University of Alabama, AL·Chemistry
Develop and benchmark a 2D-RPLC-CE-MS/MS platform, which combines two separation steps with mass spectrometry, to screen intact proteoforms globally in single ovarian cancer spheroids.
Qibin Zhang
University of North Carolina at Greensboro, NC·Chemistry
Extend OzNOxESI, an ion reaction inside a mass spectrometer that reveals double-bond positions, from phospholipids to all lipid classes, especially glycerolipids and sphingolipids.
The school
University of California-Riverside: 21 labs on PI Pages, $232M a year on research, 328 research doctorates a year.
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