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dept. of structural biology


VAN DER WEL HOME


RESEARCH

Solid State NMR

Protein & Amyloid

Protein-Lipid Interaction

SSNMR Methods


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Membrane Protein-Lipid Interactions


One topic of particular interest is related to the fascinating range of interactions that govern the functioning of biomembranes, their components and proteins interacting with them. This is a very dynamic and biologically important environment, where structural biology and biophysical understanding go hand in hand.

We leverage biological SSNMR to enhance our understanding of these processes: it allows studies of lipid membranes that closely mimic the biomembrane, permits characterization of the lipids as well as the proteins, and reveals not only structure but also dynamics. Understanding of these issues is essential for membrane fusion and fission, as well as membrane protein functioning and numerous other processes.



Figure of WALP16, WALP23 and WALP31
Bilayer to hexagonal phase transition

See also this old page, and the references below.



References

  1. Van der Wel, P.C.A. et al. (2000)  "Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner." Biochemistry 39: 3124-33. *
  2. Van der Wel, P.C.A. et al. (2002) "Geometry and intrinsic tilt of a tryptophan anchored membrane spanning peptide by 2H NMR." Biophys. J. 83: 1479-1488 *
  3. Van der Wel, P.C.A. et al. (2007) "Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides." Biochemistry 46: 7514-7524 *