On the use of dioxane as reference for determination of the hydrodynamic radius by NMR spectroscopy.

ABSTRACT: Measuring the compaction of a protein or complex is key to our understanding of the interactions within and between biomolecules. Experimentally, protein compaction is often probed either by estimating the radius of gyration (R_g) obtained from small-angle x-ray scattering (SAXS) experiments or the hydrodynamic radius (R_h) obtained, for example, by pulsed field gradient NMR (PFG NMR) spectroscopy. PFG NMR experiments generally report on the translational diffusion coefficient, which in turn can be used to estimate R_h using an internal standard to account for sample viscosity and uncertainty about the gradient strength. 1,4-Dioxane is one such commonly used internal standard, and the reference value of R_h is therefore important. We have revisited t

SUBMITTER: Tranchant EE 

PROVIDER: S-EPMC11560309 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature