Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
 

Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy


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 13Câ??13C 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.

• Content Type Journal Article
• Pages 1-9
• DOI 10.1007/s10858-011-9468-6
• Authors
  • Manuel Etzkorn, Department of NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
  • Anja Böckmann, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS-UCBL, Université de Lyon, 7, passage du Vercors, 69367 Lyon, France
  • Marc Baldus, Department of NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738

Source: Journal of Biomolecular NMR