Marcey Waters
University of North Carolina at Chapel Hill, NC·Chemistry
Proteins can act like molecular machines. A signal at one site changes the shape or behavior of a distant site, and many proteins assemble into larger structures.
- Fields
Chemistry
Biochemistry
Biophysics
- Topics
chemical biology
supramolecular chemistry
biomimetic systems
- Grants
- 2 known grants, through Jun 2027
What they work on
- Determine how amino acid sequence controls structure and self-assembly of coiled-coil peptides, rope-like bundles of protein helices, into nanospheres and fibrils, including the roles of positive and negative cooperativity.
- Build an artificial signaling cascade in foldamers, synthetic molecules that fold like proteins, to test how structural 'frustration' drives long-distance reorganization and stimulus-responsive behavior.
- Develop chemical biology tools to study how reader proteins recognize histone lysine methylation and acylation, and to improve detection of these post-translational modifications.
- Engineer reader proteins into eReaders and eWriters that sense, label and install two histone modifications at chosen sites, creating designer nucleosomes to study dual-modification pathways.
More about the research
These behaviors depend on networks of weak, noncovalent contacts between atoms, but how such networks pass signals is poorly understood. The lab studies these principles in two ways. It builds simplified, protein-like model molecules to work out the design rules. It also studies and re-engineers natural 'reader' proteins, which recognize chemical tags on the proteins that package DNA.
Why it matters
Faulty histone modification is linked to a wide range of diseases. The new tools could help researchers develop selective inhibitors and molecular probes against reader proteins, which are possible drug targets. The biomimetic work could give materials chemists design guidelines for 'smart' materials that respond to stimuli, and could clarify how proteins communicate internally.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Robert McGinty
University of North Carolina at Chapel Hill, NC·Biochemistry
Define how combinations of histone post-translational modifications recruit reader proteins across the proteome, using designer nucleosomes with chemically defined modification patterns in interactome screens.
Qingfei Zheng
Purdue University, IN·Biochemistry
Develop chemical probes that selectively label and enrich different histone monoaminylations, such as serotonylation and dopaminylation of histone H3 at glutamine 5 (H3Q5).
Y. George Zheng
University of Georgia, GA·Biochemistry
Determine the molecular mechanisms and regulation of protein arginine methyltransferase (PRMT) activity, building on the lab's preliminary results.
The school
University of North Carolina at Chapel Hill: 72 labs on PI Pages, $1.6B a year on research, 523 research doctorates a year.
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