Richard Page
Miami University-Oxford, OH·Biochemistry
Proteins are not rigid. They flex and shift shape, and these motions help decide whether an enzyme works, what it binds and how it acts in a cell.
- Fields
Biochemistry
Biophysics
Chemistry
- Topics
protein dynamics
protein structure
E3 ubiquitin ligase
- Grants
- 2 known grants, through Nov 2028
What they work on
- Determine how the structure and motions of the CHIP/Hsp70 complex decide whether a misfolded protein is refolded by the Hsp70 chaperone or tagged by the CHIP ubiquitin ligase for destruction.
- Test how phosphorylation and methylation, chemical tags added after protein synthesis, change CHIP and Hsp70 dynamics and CHIP-mediated ubiquitination of Hsp70-bound proteins.
- Define how motions within beta-lactamases, bacterial enzymes that destroy antibiotics, control their activity, and how covalently bound drugs alter those motions, to guide selective inhibitor design.
- Operate the Talon GPU cluster to support machine-learning screening of enzyme inhibitors and other research, sharing 20% of its time through the Open Science Grid.
More about the research
Binding partners, chemical reactions and post-translational modifications (PTMs), which are chemical tags added to a protein after it is made, can all change a protein's shape and motion. These changes switch its activity up or down. The lab's main research asks how such structural dynamics control function in two very different systems: cellular protein quality control and bacterial antibiotic resistance. A second grant supports shared GPU computing at Miami University.
Why it matters
Defects in protein quality control are linked to neurodegenerative disorders, cancers, ischemia reperfusion injury and hereditary cerebellar ataxias. Antibiotic-destroying beta-lactamases let bacterial infections resist treatment. Understanding how protein motions govern these systems could support rational design of new drugs, such as selective beta-lactamase inhibitors that restore antibiotic effectiveness.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Stephanie Gates
University of Missouri-Columbia, MO·Biochemistry
Dissect how the Hsp70/CHIP/BAG-1 chaperone complex affects each step of proteasomal degradation, including ubiquitin tagging, substrate binding and breakdown, using in vitro assays with purified proteins.
Mehdi Mollapour
Upstate Medical University, NY·Biochemistry
Determine how the co-chaperones FNIP1, FNIP2 and Tsc1 slow the Hsp90 chaperone cycle and help fold kinase and non-kinase client proteins, using biochemical and biophysical assays.
Jaewon Chang
Emory University, GA·Chemistry
Design and synthesize covalent warheads that react with lysine, tyrosine and serine residues on E3 ubiquitin ligases, the enzymes that tag proteins for destruction, going beyond the cysteine-reactive chemistry used so far.
The school
Miami University-Oxford: 5 labs on PI Pages, $29M a year on research, 71 research doctorates a year.
Reach out
A start for your email. Fill in the brackets.