Patrick van der Wel
Address: Department of Structural Biology University of Pittsburgh BST3; room 2044 3501 Fifth Ave Pittsburgh, PA 15260
Phone: (412) 383-9896 Fax: (412) 648-9008 Email: pvdwel@pitt.edu Homepage: VisitPhD.: 2002, University of Arkansas Postdoc: Massachusetts Institute of Technology Research: Our primary interest is in the application and development of solid state NMR methods to the study of proteins that are aggregated or otherwise immobilized. This 'immobilized' state can take a variety of forms, but notably includes amyloid-like fibrils and membrane-bound proteins, sample conditions that are inherently difficult to study by methods like X-ray crystallography and solution NMR. Multiple human disorders (e.g. Alzheimer'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 fibrillar state. We are employing ssNMR methods to study such amyloid fibrils and thereby further our understanding of the underlying mechanisms of their formation. Membrane-bound proteins mediate the cross-membrane transport of chemicals (e.g. ions) and information, but also affect their membrane environment. One of the issues in studying membrane proteins is that their activity (and structure) is often sensitive to the nature of this surrounding membrane (or the lack thereof), which can complicate the execution and interpretation of structure determinations based on solution NMR and X-ray crystallography. Our interest is in the study of membrane proteins while bound to lipid bilayers, and study the protein-lipid interaction under these conditions. Various membrane-associated proteins are even able to modulate the structure of the surrounding membrane, an ability that is essential for the cell and necessary processes such as membrane fusion and fission.
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