The Impact of Crowding on the Dynamics of the Intrinsically Disordered COR15A Protein
The properties of unfolded and intrinsically disordered proteins are highly dependent on the solution conditions. QENS is a well-established technique for the investigation of the average dynamic properties of disordered polymers and proteins in solution. The protein COR15A from Arabidopsis thaliana is intrinsically disordered under fully hydrated conditions, but obtains alpha-helical structure during dehydration, which is reversible upon rehydration. Protein folding can also be induced by high concentrations of low-molecular-mass crowding agents such as sucrose or glycerol. We would like to measure the dynamical properties of the COR15A protein as a function of the crowding agent glycerol. The properties of intrinsically disordered proteins are believed to be similar to those of polymers in solution. In our experiments, we would like to investigate, whether or not those polymer-like properties can be seen in the fully unfolded state and eventually are lost (or not) when the protein is more and more folded.
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Andreas M. Stadler; APPEL Markus; Christopher J. Garvey; HARIS Luman; HINCHA Dirk and SEYDEL Tilo. (2019). The Impact of Crowding on the Dynamics of the Intrinsically Disordered COR15A Protein. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-830
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