Kinetic Analysis of Protein Aggregation Monitored by Real-Time 2D Solid-State NMR Spectroscopy

 Title: Kinetic Analysis of Protein Aggregation Monitored by Real-Time 2D Solid-State NMR Spectroscopy Author: Baldus, Marc; Etzkorn, Manuel; Bockmann, Anja Note: Order does not necessarily reflect citation order of authors. Citation: Etzkorn, Manuel, Anja Bockmann, and Marc Baldus. 2011. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Journal of Biomolecular NMR 49(2): 121-129. Full Text & Related Files: 3042102.pdf (904.5Kb; PDF) Abstract: It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate state prior to aggregation. Based on a single real-time 2D $$^{13}\textrm{C}–^{13}\textrm{C}$$ transition spectrum, kinetic information about the refolding and aggregation step could be extracted. In addition, structural rearrangements associated with refolding are estimated and several different aggregation scenarios were compared to the experimental data. Published Version: doi:10.1007/s10858-011-9468-6 Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3042102/pdf/ Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:7349755 Downloads of this work: