news

Congratulations to Dr. Jennifer Boatz and other team members for the acceptance and publication of a nice new paper on the structure of the misfolded mutant protein from Huntington’s disease. The paper is online at the Journal of Molecular Biology. Based on an integration of multiple techniques (NMR, EM, and X-ray diffraction), Jennifer assembled a new structural model of the protofilaments that make up the hierarchical fiber architecture of mutant huntingtin exon 1. This is a timely and important step forward in our understanding of the (mis)behaviour of the HD protein, and in particular how it forms pathogenic inclusions and […]

Now online at the journal Experimental Biology and Medicine: our new review article summarizing recent contributions from solid-state NMR and electron microscopy to further our understanding of the (mis)behavior of the mutant proteins behind Huntington’s disease. Citation:  I. Matlahov & P.C.A. van der Wel (2019) Conformational studies of pathogenic expanded polyglutamine protein deposits from Huntington’s disease. Exp. Biol. Med. in press; DOI: 10.1177/1535370219856620

Our first paper of 2019 has just appeared online in the journal Structure. It describes the very nice solid-state NMR studies performed by Dr. Mingyue Li, on a protein-lipid complex involved in the early stages of mitochondrial apoptosis. Together with our collaborators in the groups of Valerian Kagan and Jinwoo Ahn (University of Pittsburgh), she looked at the structure and function of the peroxidase active cytochrome c in its membrane-bound state. For more details on the findings, including how the lipid substrate cardiolipin forms membrane nano domains and acts as a dynamic regulator, please see the paper at the journal. […]

Congrats to Talia, Jennifer and Irina, as well as our international network of collaborators on the acceptance of an exciting new paper in JACS. It describes the power of dynamic nuclear polarization (DNP) to enable multidimensional solid-state NMR studies of polyglutamine-expanded huntingtin exon 1 fibrils. Importantly in these experiments we did not apply stable-isotope labeling to these protein deposits that are implicated in Huntington’s disease. This approach enables great structural data and can hopefully prove applicable to many more (types of) samples. More info to follow, but for now: Read the accepted paper here at the journal.     Title: Structural […]

Our new review article discussing the concept of dynamics-based spectral editing (DYSE) in ssNMR is now available online in the journal Methods. In it, we describe how the dynamics-sensitive pulse sequences enable the filtering out (or spectral editing) of signals based on their differences in dynamics. Applications by ourselves and many other groups are discussed. Notably, these applications range across a huge swatch of different sample types, going from designer peptide nano materials to whole tissues and even living organisms.   Citation: Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR. Matlahov, I., Van der Wel, P.C.A. Methods, […]

  Our new paper discussing the role of modern solid-state NMR in integrated structural biology is now published in Emerging Topics in Life Sciences. It provides a review of a selection of recent solid-state NMR studies from (mostly) the last decade. Not only does it give a review of notable 3D structures obtained by solid-state NMR, but it also examines contributions going beyond static protein structures. This includes the characterization of biologically relevant dynamics, and the pinpointing of crucial intermolecular interactions. Reference: Patrick C.A. van der Wel (2018) “New applications of solid-state NMR in structural biology.” Emerging Topics in Life […]

Congratulations to collaborator Giorgio Cavigiolio, his group at CHORI (Children’s Hospital Oakland Research Institute), and Jennifer Boatz on the publication of our new collaborative paper. It reports functional and structural studies of the effect of oxidation on apolipoprotein A-I (ApoA1), using a variety of experiments and assays – including solid-state NMR. Oxidation of the protein causes it to become more monomeric and also less stably folded. As a consequence it becomes prone to aggregation into amyloid-like fibrils. Interestingly, these oxidized aggregates are able to subvert non-oxidized protein into an amyloidogenic (i.e. aggregation-prone) state. Another interesting aspect of these aggregated proteins […]

Congratulations to our collaborators for the new collaborative paper on the characteristic twisting of amyloid fibril filaments, which has just appeared online as accepted for publication in the Journal of Physical Chemistry B. The paper, titled “Energetics Underlying Twist Polymorphisms in Amyloid Fibrils“, describes molecular dynamics simulations of the twisting of amyloid-like structures of the GNNQQNY peptide fragment from the yeast prion protein Sup35p. This particular peptide has developed into an essential model system for studies of the structure and formation of amyloid fibrils, and (for instance) how they differ from crystalline assemblies formed by these and other polypeptides [1-3]. […]