Solution NMR studies of TGF-beta family signaling proteins
In the Hinck laboratory, we are interested in utilizing the tools of structural biology to understand how the structure and dynamics of biological macromolecules engenders them with their extraordinary ability to specifically and selectively bind partners and assemble into functional complexes. In my laboratory, we rely heavily on NMR spectroscopy as a tool for studying the structure and dynamics of biological macromolecules, but we also use X-ray crystallography and other accompanying biophysical tools, such as isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), and fluorescence spectroscopy. In addition, my laboratory employs cell-based studies to assess the significance of molecular features we have identified in a cellular context.
In my laboratory, a major area of emphasis is studying signaling proteins and receptors of the TGF-beta family, a highly diversified signaling family, with representative family members in both in invertebrates and vertebrates. In our research, we are interested in deciphering the molecular adaptations that the signaling proteins, single-pass transmembrane receptors, downstream effectors, and multitude of extracellular and intracellular modulators have acquired that enable the proteins of family to achieve their unique biological functions. In addition, we are interested in exploiting the unique adaptations our structural studies uncover to develop highly potent TGF-beta inhibitors for treatment of cancer or fibrosis.
- University of Wisconsin, Madison, WI, USA Ph.D., 1993 in Biochemistry, Advisor: John L. Markley
- University of Wisconsin, Madison, WI, USA; NIH Ruth Kirchenstein Postdoctoral Fellow; Advisor: Laura L. Kiessling
- National Institute of Dental Research, Bethesda, MD; NIH IRTA and Staff Fellow; Advisor: Dennis A. Torchia
Department of Structural Biology
University of Pittsburgh
1035 Biomedical Science Tower 3
Phone: (412) 648-8533
Fax: (412) 648-9008