Description
The natural environment of proteins is a crowded environment as in cells, extracellular fluids or during processing. PEGyaltion is used to modify the bioavailibility of protein drugs or ubiquination signals protein degradation, alters cellular location, affect their activity or promotes or prevent protein interactions. In both cases the protein dynamics is changed due to obstruction. Here we examine 2 scenarios using deuteration to mask the obstructing polymer.
Semidilute polymer solutions have been a source of rich structural and dynamical properties and mimic a crowded environment. By dispersing model globular proteins like -Lactalbumin (La) and Hemoglobin (Hb), in aqueous solution of poly-(ethylene oxide) (PEO) we mimic a crowded environment and use state of the art neutron spin echo (NSE) and small angle neutron scattering (SANS) techniques to observe the corresponding protein dynamics in semidilute polymer solution[1]. NSE can access the fast diffusion process () prior to the slow diffusion process on long times and length scales (). In the second example we show first results how PEGyaltion affects protein internal dynamics.
[1] S. Gupta, R. Biehl, C. Sill, J. Allgaier, M. Sharp, M. Ohl, et al., Protein Entrapment in Polymeric Mesh: Diffusion in Crowded Environment with Fast Process on Short Scales, Macromolecules. (2016). doi:10.1021/acs.macromol.5b02281.
[1]: https://indico.esss.lu.se/event/756/picture/13.jpg
Primary author
Ralf Biehl
(JCNS)
