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dept. of structural biology


VAN DER WEL HOME


RESEARCH

Solid State NMR

Protein & Amyloid

Protein-Lipid Interaction

SSNMR Methods


Publications

Teaching

Positions

Selected Links


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Dr. Patrick C.A. van der Wel
    Assistant professor
    Department of Structural Biology
    University of Pittsburgh School of Medicine
    Biomedical Science Tower 3, room 2044
    3501 Fifth Ave.
    Pittsburgh, PA 15260
    e-mail: pvdwel [AT] pitt.edu
    phone: (412) 3839896
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Patrick van der Wel


Research Interests 

Our interests are in the application of solid state NMR to biological structure determination. Biological SSNMR allows measurements of structural and motional features of (partially) immobilized biomolecules, and is of particular interest due to its ability to access such information in a site-specific manner without requiring solublity or crystallinity.

Various human disorders involve the misfolding of proteins into fibrillar aggregates (including diseases like Huntington and Alzheimer's), and one of the research aims is to address the structure and formation of these amyloid fibril aggregates. Furthermore, in the cells many proteins are immobilized (in their functional and active state) by being associated with or embedded in lipid bilayers that make up biological membranes. Such membrane-associated proteins are involved in a range of essential functions, such as membrane receptor proteins (common targets for pharmaceuticals). Our interests are in the interplay or interaction between the lipids in the membrane and the bound membrane proteins. Interestingly, this has been found to be a two-way process that can control and affect both the functioning of the proteins and the behavior of the lipids.

Addressing these topics relies on a combination of various solid state NMR methodologies and complementary techniques. Some of the links to the left address features of these topics and highlight some of my previous work, using different experimental SSNMR approaches. It shows how SSNMR enables structural measurements on (micro)crystalline and fibrillar polypeptide aggregates, as well as protein-lipid interactions.

Selected Publications (see here for a complete listing)