Michael Kay
University of Utah, UT·Biochemistry
Studying how HIV interacts with the human cells it infects often requires molecules that are hard to make, and ways to find which human genes matter for infection. This grant supports a shared core within the CHEETAH Center, a group studying the structural biology of HIV infection, how cells restrict the virus, and viral dynamics.
- Fields
Biochemistry
Microbiology & Immunology
Chemistry
- Topics
host-virus interactions
structural biology
peptide synthesis
- Grants
- 1 known grant, through Apr 2027
What they work on
- Provide chemically synthesized peptides and proteins, including versions with fluorescent or isotope labels, modifications such as phosphorylation, and mirror-image or crosslinked components, for HIV-host studies that cell-based expression cannot supply.
- Develop new chemical peptide synthesis methods that extend chemical protein synthesis to larger and more challenging protein targets.
- Incorporate deep learning into computational protein design pipelines to create new protein tools and improve the expression, stability and uniformity of HIV-related target proteins.
- Run HIV-CRISPR screens, which disable human genes one by one, with existing and newly built libraries to identify and validate host genes involved in HIV infection.
More about the research
The core develops and provides tools for making, manipulating and discovering biomolecules for the center's labs.
Why it matters
Better tools for making peptides, designing proteins and finding human genes involved in HIV infection could open new ways to study how the virus interacts with its host. Identifying host proteins that matter for infection may point researchers toward new targets in the effort to understand and fight HIV.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Kraig Wheeler
Whitworth University, WA·Chemistry
Synthesize families of acyclic and cyclic dipeptides and extended peptides by solid-phase peptide synthesis, systematically varying molecular shape and pendant functional groups.
Brian Kuhlman
University of North Carolina at Chapel Hill, NC·Biochemistry
Test whether a protein core mixing water-repelling and water-attracting amino acids yields a partly unfolded, water-containing cold state, using de novo designed cold unfolding proteins, biophysical measurements and molecular dynamics simulations.
Alberto Perez
University of Florida, FL·Biophysics
Map the binding partners of the ET domain of BET proteins: identify candidates computationally, rank the strongest with machine learning and physics-based methods, and check top leads with NMR experiments.
The school
University of Utah: 58 labs on PI Pages, $789M a year on research, 366 research doctorates a year.
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