Solid state NMR of membrane proteins & amyloid fibrils



The Van der Wel group uses solid state NMR spectroscopy and complementary structural and biophysical techniques to study the protein (mis)folding, protein aggregation, and protein-membrane interactions. The use of ssNMR enables structural studies of aggregated and membrane-bound proteins, under conditions that present experimental challenges to more traditional structural biology. Nonetheless, these systems are of great medical and biological importance. Multiple diseases (e.g. Alzheimer's and Huntington's disease) are characterized by the misfolding and aggregation of normally un-aggregated proteins into fibrillar structures (amyloid fibrils). Understanding the formation and structure of these fibrils has been an experimental challenge, with ssNMR uniquely able to provide site-resolved measurements of the structure and dynamics of the protein fibrils. Through the study of the fibrils and other aggregated species we also further our understanding of the mechanisms of their formation and toxicity. Another focal point is the study of membrane-bound proteins. We have a particular interest in proteins that modulate the structure and dynamics of their membrane environment. We are engaged in studies of both cholesterol- and cardiolipin-binding proteins, with a current focus on the role of protein-lipid interactions in mitochondrial apoptosis (or programmed cell death). Again ssNMR is used to probe protein structure, but it also is a unique tool to elucidate structural changes in the membrane itself.



PhD 2002, University of Arkansas

Postdoctoral Training

2003-2008, Massachusetts Institute of Technology

Department of Structural Biology
University of Pittsburgh
BST3; Room 2044
3501 Fifth Avenue
Pittsburgh, PA 15260

Phone: (412) 383-9896
Fax: (412) 648-9008


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