Behavior of α, β tubulin in DMSO-containing electrolytes.

ABSTRACT: α, β-tubulin is a cytoskeletal protein that forms cylindrical structures termed microtubules, which are crucial to the cell for a variety of roles. Microtubules are frequently modelled as one-dimensional bionanowires that act as ion transporters in the cell. In this work, we used dynamic light scattering (DLS) to measure the hydrodynamic diameter of tubulin in the presence of a polar aprotic co-solvent. We found that the hydrodynamic diameter increased with increasing DMSO volume fraction, almost doubling at 20% DMSO. To evaluate if this was due to an enlarged solvation shell, we performed reference interaction site model (RISM) simulations and found that the extent of solvation was unchanged. Using fluorescence microscopy, we then showed that tubulin was polymerization competent in the pr

SUBMITTER: Kalra AP 

PROVIDER: S-EPMC9418024 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature