The effect of chain length on the internal diffusive dynamics of intrinsically disordered proteins
The goal of this project is to understand how the chain length of intrinsically disordered proteins affects the internal diffusive dynamics. For that purpose we will use our model system, the antimicrobial saliva protein Histatin 5 and variants thereof, varying in length between 12 - 60. Combining IN16B, BATS, and IN5 quasi-elastic neutron scattering would cover a very complete dynamic range. Combining modern data analysis frameworks and simulations, separating the different hierarchical levels of dynamics, unprecedented insights will be allowed. The focus will be on access to (sub)nanosecond internal diffusive motions of the protein in solution for a range of protein concentrations and different temperatures. This choice is based on previous scattering experiments and simulations, which together would yield a molecular understanding of the system of both medical and academic relevance. Here, we specifically apply for BATS to profit from its world-leading signal-to-noise and to fill the gap inaccessible by IN5 and IN16B.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
Marie Skepö; SEYDEL Tilo; SORENSEN Henrik Vinther and SVENSSON Oskar. (2023). The effect of chain length on the internal diffusive dynamics of intrinsically disordered proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-950
This data is not yet public
This data is not yet public
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