Jeffrey C. Hoch, PhD

Our laboratory works on problems related to the physical basis for the biological activity of proteins. Broadly, this includes their structure, dynamics, stability, and interactions with other molecules. Some specific questions we are interested in include: The relationship of protein dynamics and structure to biological activity. An example is the role of structure and dynamics in the interaction between prolactin and the prolactin receptor. Prolactin is involved in hundreds of biochemical pathways, and has been shown to be involved in cancer (expression levels of both prolactin and its receptor are elevated in some forms of breast cancer). Understanding the physical basis for prolactin-receptor interaction will aid the search for molecules that inhibit or enhance the signaling functions of prolactin. In collaboration with Professor Choukri Ben-Mamoun we are investigating the structural biology of Plasmodium falciparum, the parasite that causes malaria. Despite the devastating impact of malaria on the developing world, cheap, safe, and effective treatments for malaria remain elusive. We are solving the structure of an enzyme that is essential for the survival of Plasmodium that has no homologs in mammals, and thus is potentially an important drug target. We plan to solve the structures of additional Plasmodium proteins. We are collaborating with Professor Sandra Weller on structural studies of proteins from herpes simplex virus. These are particularly challenging proteins to investigate, but the insights that can be derived from these studies should shed light on mechanisms of essential processes such as DNA replication, and could guide the discovery of novel antiviral compunds. We employ a variety of physical and computational methods, especially NMR, and also circular dichroism, fluoresence, and ultraviolet/visible absorption spectroscopies, water activity, differential and isothermal titration calorimietry, non-Fourier spectrum analysis, and molecular dynamics simulations. The NMR resources at the UConn Health Center are outstanding, and include spectrometers operating at 400, 500, 600, and 800 MHz. The latter three instruments are equipped with state-of-the-art cryogenically cooled probes. Computational resources include a power 1000-node cluster shared with the Center for Cell Analysis and Modeling.

[2026] NMRhub: An NMR Data Ecosystem Spanning the Complete Data Lifecycle. [2026] Backbone resonance assignment of the pentraxin domain of the neuronal pentraxin receptor (NPTXR). [2025] Scalable cyberinfrastructure for experimental NMR data. [2025] Backbone assignment of the N-terminal domain of the A subunit of the Bacillus cereus GerI germinant receptor. [2024] PDB NextGen Archive: centralizing access to integrated annotations and enriched structural information by the Worldwide Protein Data Bank. [2024] Restraint validation of biomolecular structures determined by NMR in the Protein Data Bank. [2024] Community recommendations on cryoEM data archiving and validation. [2023] Announcing the launch of Protein Data Bank China as an Associate Member of the Worldwide Protein Data Bank Partner