Tag: ssnmr
Publication: Review article on polyglutamine protein analysis by solid-state NMR spectroscopy.
Our new review article summarizing progress in polyglutamine protein studies by solid-state NMR is now available on the website of the journal Biochemical Society Transactions. This is an invited mini-review that was requested to cover the progress made in our understanding the aggregation and misfolding of mutant polyglutamine proteins implicated in diseases such as Huntington’s disease and several versions of spinocerebellar ataxia (SCA). We describe how studies from ssNMR has been used to better understand the structure of these protein aggregates, and thus helps us analyze how the aggregation process occurs and how aggregates may play a role in these diseases. The paper is published open-access, so you should be able to read it to see all the details. (Naturally, the format of the mini-review limited the word count and meant that much had to be omitted)
Citation:
Patrick C.A. van der Wel; Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation. Biochem Soc Trans 2024; BST20230731. doi: https://doi.org/10.1042/BST20230731
Publication: collaborative paper on perovskite-related materials, with Sn and Se ssNMR
Congrats to our collaborators from the group of Maria Loi and others for the publication of their new paper on in situ SnSe deposition as passivation for scalable and stable quasi-2D lead–tin perovskite solar cells, in the journal Energy & Environmental Science. Dr. Lasorsa in our group contributed tin and selenium ssNMR analysis to this interdisciplinary paper. For more information see the paper at the journal.
Publication:
Chen L, Tekelenburg EK, Gahlot K, Pitaro M, Xi J, Lasorsa A, et al. In situ SnSe deposition as passivation for scalable and stable quasi-2D lead–tin perovskite solar cells. Energy Environ Sci. 2023;10.1039.D3EE02507A.
Educational webinar on the use of ssNMR to measure dihedral angles.
Recently, Patrick gave an online lecture in the online webinar tutorial series of the Global NMR Discussion Meetings series (episode 70!). In this online lecture he introduced and discussed approaches to measure torsion angles (or dihedral angles) using advanced solid-state NMR spectroscopy. He discussed the basic idea of how these are implemented in ssNMR, but also how such structural data can be a useful complement to more traditional inter-atomic distance information obtained by ssNMR. You can now watch the recording of this lecture on Youtube, via this link.
Want to learn even more?
This lecture is connected to our recent review article on the same topic, which can be found online at: Frontiers | Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy (frontiersin.org)
Publication: 13C labeling of hyaluronic acid polysaccharides (for ssNMR analysis)
Congrats to Pushpa and her collaborators on the new paper in the journal Carbohydrate Polymers. This new report describes Pushpa’s work to achieve the production of high-molecular-weight (HMW) hyaluronic acid, as part of her PhyCan (physics of cancer) project. Our interest in this polysaccharide stems from its important role in the extracellular matrix (ECM) of tissues, and in particular certain types of cancer tissues. In such tumors the amount of HA is upregulated, seemingly contributing to the progression of cancer development. A challenge in understanding this process is that HMW is difficult to study with most structural techniques, as it can be very large (megadaltons!) and highly dynamic. In this project, Pushpa outfitted HMW HA with 13C (and 15N) isotope labels, and shows that this makes multidimensional NMR (including solid-state NMR) feasible. This approach is expected to be valuable for many research areas, as HA is also important for many biomedical engineering (BME) type applications. ECM-mimicking hydrogels are for instance of great interest for engineering 3D environments for growing cells.
Publication:
Rampratap P, Lasorsa A, Perrone B, Van Der Wel PCA, Walvoort MTC. Production of isotopically enriched high molecular weight hyaluronic acid and characterization by solid-state NMR. Carbohydrate Polymers. 2023 Sep;316:121063.
Publication: SSNMR of alginate hydrogel (re)hydration
A new open-access publication by Mustapha and collaborators has been published in the journal Food Hydrocolloids, describing how he used various ssNMR measurements to probe alginate hydrogel structure and (re)hydration. Alginates can be cross-linked with calcium to form hydrogels, which are used in many different types of applications. This includes their use in slow-release drug delivery as well as food/nutritional applications. In this new paper, Mustapha shows how 1H, 2H and 13C ssNMR measurements can be used to see how these hydrogels are structured, but especially also how they are hydrated by the aqueous solvent. A key feature of the work is the use of 1H MAS NMR to detect the water molecules in the hydrogel macropores as well as those waters directly interacting with the alginate. The two types of water molecules form distinct ‘pools’ in the hydrogel, which can be nicely distinguished by their different molecular motion. The latter is detected via different relaxation measurements, in these NMR experiments.
To read more:
El Hariri El Nokab, M..; Lasorsa, A.; Sebakhy, K. O.; Picchioni, F.; van der Wel, P. C. A. Solid-State NMR Spectroscopy Insights for Resolving Different Water Pools in Alginate Hydrogels. Food Hydrocolloids 2022, 107500.
Publication: Structural and motional changes in a cytochrome c – lipid complex implicated in apoptosis.
Congratulations to lab alum Dr. Mingyue Li and our collaborators on the publication of a new paper in the Journal of Molecular Biology. The paper is online via its DOI link. The paper describes how we used solid-state NMR spectroscopy to characterise the partial destabilization of the native fold of the protein cytochrome c, as it is bound to cardiolipin lipids. This protein-lipid complex is implicated in the process of programmed cell death, where it plays a key role in triggering the self-destruction of undesired or disease cells in higher organisms. Notably, the CL-bound protein catalyses the process of mitochondrial lipid peroxidation, which we see being reconstituted in vitro via mass-spectrometry lipidomics. The latter work is done by our longstanding collaborators in the group of Valerian Kagan at the University of Pittsburgh. The current paper builds on our earlier work, but is of especial interest based on the fact that we bridge some of our prior findings (that suggested the protein to be surprisingly “folded” on the membrane) to studies that report a greater degree of mobility of the CL-bound protein. Here we see how the experimental conditions regulate protein mobility and also pinpoint how different extents of mobility are present in the membrane-bound cytochrome c. Interestingly, the regional dynamics map partly, but not completely onto the previously identified “foldons” that define the folding landscape of this widely studied mitochondrial protein. For more details see the paper below. It is available as #openaccess so just follow the DOI link for access:
Reference:
Mingyue Li, Wanyang Sun, Vladimir A. Tyurin, Maria DeLucia, Jinwoo Ahn, Valerian E. Kagan, Patrick C.A. van der Wel (2021) Activation of Cytochrome C Peroxidase Function Through Coordinated Foldon Loop Dynamics upon Interaction with Anionic Lipids, Journal of Molecular Biology, Volume 433, Issue 15, 23 July 2021, 167057