Molecular Dynamics of the Intrinsically Disordered Myelin Basic 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. Myelin basic protein is intrinsically disordered under fully hydrated conditions. Protein folding can be induced by addition of 30% trifluorethanol to the buffer solution. The protein will be invested in its fully unfolded state by addition of 6 M guanidinium hydrochloride. 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 native state in aqueous solution, in its 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; Bernhard Frick; HARIS Luman and SEYDEL Tilo. (2019). Molecular Dynamics of the Intrinsically Disordered Myelin Basic Protein. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-874
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