Sina Ghaemmaghami
University of Rochester, NY·Biochemistry
A protein works only when its chain of building blocks folds into the right three-dimensional shape. When proteins misfold, the errors contribute to aging, neurodegenerative disease, cancer and other illnesses.
- Fields
Biochemistry
Biophysics
Computer Science
- Topics
protein misfolding
protein folding
refoldability
- Grants
- 2 known grants, through May 2030
What they work on
- Develop and benchmark a standardized limited proteolysis-mass spectrometry (LiP-MS) workflow, which reads protein shape from enzyme cut sites, across multiple labs and instruments with statistical quality-control metrics.
- Build MisFold-DB, a public database of misfolding tendency and structural change sites for more than 10,000 proteins, by applying LiP-MS to bacterial species and eukaryotic cell lines.
- Test how sequence, structure, native entanglements, protein half-life, growth rate and lifespan relate to persistent misfolding, and build interpretable machine-learning models that predict which proteins misfold and where.
- Provide mass spectrometry-based proteomics and metabolomics for aging models, and develop methods to quantify protein misfolding, oxidative damage and turnover kinetics in aging samples.
- Integrate genome, proteome and metabolome data to identify aging-related genome elements and their epigenetic features, and build the multi-species Upstate NSC Omics Atlas for the aging research community.
More about the research
Even so, scientists cannot yet routinely measure which proteins bounce back after unfolding and which stay stuck in wrong shapes. Sina Ghaemmaghami's work uses mass spectrometry to measure protein misfolding, damage and turnover across whole proteomes, meaning all the proteins in a cell. It aims to understand how cells keep their proteins healthy and how this changes with age. The two projects build a shared misfolding database and run an aging-focused omics core facility.
Why it matters
Protein misfolding contributes to aging, neurodegenerative disorders and cancer. Standardized misfolding measurements, a public database and predictive models could help researchers find which proteins are vulnerable and why, informing studies of disease and protein engineering. The omics core and its cross-species atlas give aging researchers tools to identify molecular signatures of aging.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Drew Jones
New York University, NY·Biochemistry
Provide metabolomics services to cancer researchers, including global and untargeted metabolomics, lipidomics, mass spectrometry imaging and custom targeted methods for measuring specific metabolites.
Mark Chance
Case Western Reserve University, OH·Biochemistry
Provide proteomic and small-molecule analysis to cancer investigators, including protein identification, post-translational modification characterization, quantitative proteomics, protein interactome mapping and metabolomics, across collaborative and high-throughput service modes.
Rovshan Sadygov
University of Texas Medical Branch at Galveston, TX·Biochemistry
Develop methods to estimate protein turnover from the deuterium labeling of fragment ions in tandem mass spectra, which are less distorted by space-charging, limited dynamic range and co-eluting contaminants than intact peptide ions.
The school
University of Rochester: 38 labs on PI Pages, $492M a year on research, 308 research doctorates a year.
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