Deciphering the role of solvent viscosity for the dynamical properties of folded and intrinsically disordered proteins
The protein COR15A is intrinsically disordered in D2O, but strongly gains helical structure in 70% glycerol buffer. In a previous experiment on IN16B BATS (8-04-830) we measured QENS of COR15A in 0% and 70% deuterated glycerol buffer. Global protein diffusion in 70% glyc. was found to be reduced by a factor of 23 as compared to the value obtained in D2O. This is in agreement with the change of solvent viscosity between 70% glyc. and D2O (reduction of factor 24). Concerning internal protein dynamics, however, we found a 16 times smaller value of the internal diffusion coefficient in the folded protein in 70% glyc. than in the unfolded protein in D2O. We currently cannot differentiate between the effects of changed solvent viscosity and the specific role of protein folding for the reduced internal diffusivity in folded COR15A in 70% glyc. as compared to the unfolded protein in D2O. To complete our experimental QENS data, we suggest to measure a fully folded protein in D2O buffer and 70% glyc. as reference, which would allow us to distinguish between both effects. We would need 1 day on IN16B BATS mode to complete our study (6h per sample: 2 protein solutions and 2 buffers = 1 day).
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The recommended format for citing this dataset in a research publication is in the following format:
Andreas M. Stadler; APPEL Markus and SEYDEL Tilo. (2021). Deciphering the role of solvent viscosity for the dynamical properties of folded and intrinsically disordered proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.EASY-669
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