Observing unfolding and proteolysis of a model protein in real-time: a time-resolved SANS study
The specific recognition, unfolding and degradation of faulty proteins is an essential process in any living cell in order to guarantee protein homeostasis and keep the proteome in a healthy and functional state. Dysfunction of this process can lead to accumulation of misfolded proteins that are potentially toxic and lead to multiple diseases. Despite the crucial importance of understanding this process, detailed structural insights, at a molecular level, are limited, mainly due to specific flexibility and conformational changes involved. Here, we propose to study the unfolding and proteolysis of a specifically tagged model protein, GFPssrA, by SANS in solution, in the presence of the archaeal unfoldase complex PAN and the proteolytic core particle 20S. Using alternate deuteration of the different partners will allow us to describe both the specific conformation of GFP and PAN during the process. Using archaeal (hyperthermophilic partners) will allow a temperature control and fine-tuning of the rate of the process. In addition, an online fluorescence device on D22 will monitor the folded state of GFP.
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GABEL Frank; COVES Jacques; MAHIEU Emilie and MARTEL Anne. (2019). Observing unfolding and proteolysis of a model protein in real-time: a time-resolved SANS study. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-966
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