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Hodsdon Laboratory -- Projects
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Our laboratory strives to improve understanding of human pathology at a molecular level. We utilize a combination of NMR spectroscopy, other biophsycial techniques, and cell-based assays to describe how the tertiary structures and thermodynamic behaviors of aqueous proteins determine their physiologic function. Important molecular characterizations include dynamic conformational fluctuations, static structural stabilities, protein surface electrostatics, ligand-binding and protein-protein assocation reactions, all of which serve as the physico-chemical "toolkit" to create the activities of biological life.

Protein systems that we are currently or have previously studied:

1. pH-dependence to Hormone/Cytokine-Receptor Recognition.

2. Role of Zn2+-binding to Potential Functional Role of the Proinsulin C-peptide.

3. Role of Ca2+-binding to the C-terminal Tail of Polycystin-2.

4. Protein Interactions Involved in Synaptic Vesicle Trafficking.

5. Role of Glycosaminoglycans in Cytokine Function.

6. The GLUT4-tethering Protein, TUG, Contains Multiple Ubiquitin-like Domains.

6. Polymorphic Drug Metabolizing Enzymes.




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